dic8 pip 3  (Echelon Biosciences)


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    Structured Review

    Echelon Biosciences dic8 pip 3
    TMEM16A Ca 2+ -evoked Cl − currents rundown in excised patches and are recovered by a <t>diC8-PI(4,5)P</t> 2 application. A , example currents recorded at the indicated times during 150 ms steps to −60 and +60 mV, recorded using excised inside–out macropatches from Xenopus laevis oocytes. B , normalized plot of current measured at −60 mV versus time, fit with a single exponential ( red line ). C , box plot distribution of the rate of current decay (τ), measured by fitting plots of relative current versus time with single exponentials (N = 11). The central line denotes the median, the box denotes 25 to 75% of the data, and the whiskers represent 10 to 90% of the data. D , a soluble synthetic analog of PI(4,5)P 2 , <t>diC8-PI(4,5)P</t> 2 , was applied to excised inside–out patches once current had stably rundown. Currents were recorded at −60 mV. E , box plot distribution of the fold current recovered after the application of <t>diC8-PI(4,5)P</t> 2 with Ca 2+ (N = 8). <t>diC8-PI(4,5)P</t> 2 , dioctanoyl phosphatidylinositol 4,5-bisphosphate; TMEM16A, TransMEMbrane 16A.
    Dic8 Pip 3, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Phosphate position is key in mediating transmembrane ion channel TMEM16A–phosphatidylinositol 4,5-bisphosphate interaction"

    Article Title: Phosphate position is key in mediating transmembrane ion channel TMEM16A–phosphatidylinositol 4,5-bisphosphate interaction

    Journal: The Journal of Biological Chemistry

    doi: 10.1016/j.jbc.2022.102264

    TMEM16A Ca 2+ -evoked Cl − currents rundown in excised patches and are recovered by a diC8-PI(4,5)P 2 application. A , example currents recorded at the indicated times during 150 ms steps to −60 and +60 mV, recorded using excised inside–out macropatches from Xenopus laevis oocytes. B , normalized plot of current measured at −60 mV versus time, fit with a single exponential ( red line ). C , box plot distribution of the rate of current decay (τ), measured by fitting plots of relative current versus time with single exponentials (N = 11). The central line denotes the median, the box denotes 25 to 75% of the data, and the whiskers represent 10 to 90% of the data. D , a soluble synthetic analog of PI(4,5)P 2 , diC8-PI(4,5)P 2 , was applied to excised inside–out patches once current had stably rundown. Currents were recorded at −60 mV. E , box plot distribution of the fold current recovered after the application of diC8-PI(4,5)P 2 with Ca 2+ (N = 8). diC8-PI(4,5)P 2 , dioctanoyl phosphatidylinositol 4,5-bisphosphate; TMEM16A, TransMEMbrane 16A.
    Figure Legend Snippet: TMEM16A Ca 2+ -evoked Cl − currents rundown in excised patches and are recovered by a diC8-PI(4,5)P 2 application. A , example currents recorded at the indicated times during 150 ms steps to −60 and +60 mV, recorded using excised inside–out macropatches from Xenopus laevis oocytes. B , normalized plot of current measured at −60 mV versus time, fit with a single exponential ( red line ). C , box plot distribution of the rate of current decay (τ), measured by fitting plots of relative current versus time with single exponentials (N = 11). The central line denotes the median, the box denotes 25 to 75% of the data, and the whiskers represent 10 to 90% of the data. D , a soluble synthetic analog of PI(4,5)P 2 , diC8-PI(4,5)P 2 , was applied to excised inside–out patches once current had stably rundown. Currents were recorded at −60 mV. E , box plot distribution of the fold current recovered after the application of diC8-PI(4,5)P 2 with Ca 2+ (N = 8). diC8-PI(4,5)P 2 , dioctanoyl phosphatidylinositol 4,5-bisphosphate; TMEM16A, TransMEMbrane 16A.

    Techniques Used: Stable Transfection

    Phospholipid analogs differentially recovered TMEM16A. Soluble synthetic analogs of PIP 3 (diC8-PIP 3 ), PI(3,4)P 2 (diC8-PI(3,4)P 2 ), and PI(3,5)P 2 were applied to excised inside–out patches once current had stably rundown. Currents were recorded at −60 mV. A , box plot distribution of the fold current recovered after the application of diC8-PI(4,5)P 2 (N = 9), diC8-PIP 3 (N = 7), diC8-PI(3,4)P 2 (N = 6), or diC8-PI(3,5)P 2 (N = 5). Representative plots of normalized currents versus time, before and during application of 100 μM diC8-PIP 3 ( B ), diC8-PI(3,4)P 2 ( C ), or diC8-PI(3,5)P 2 ( D ). ∗ represents p < 0.025 as determined by ANOVA and Tukey's HSD post hoc tests. diC8-PI(3,4)P 2 , dioctanoyl phosphatidylinositol 3,4-bisphosphate; diC8-PI(3,5)P 2 , dioctanoyl phosphatidylinositol 3,5-bisphosphate; diC8-PI(4,5)P 2 , dioctanoyl phosphatidylinositol 4,5-bisphosphate; diC8-HSD, honestly significant difference; PIP 3, dioctanoyl phosphatidylinositol 3,4,5-trisphosphate; PI(3,4)P 2 , phosphatidylinositol 3,4-bisphosphate; PI(3,5)P 2 , dioctanoyl phosphatidylinositol 3,5-bisphosphate; PIP 3, phosphatidyl 3,4,5-trisphosphate; TMEM16A, TransMEMbrane 16A.
    Figure Legend Snippet: Phospholipid analogs differentially recovered TMEM16A. Soluble synthetic analogs of PIP 3 (diC8-PIP 3 ), PI(3,4)P 2 (diC8-PI(3,4)P 2 ), and PI(3,5)P 2 were applied to excised inside–out patches once current had stably rundown. Currents were recorded at −60 mV. A , box plot distribution of the fold current recovered after the application of diC8-PI(4,5)P 2 (N = 9), diC8-PIP 3 (N = 7), diC8-PI(3,4)P 2 (N = 6), or diC8-PI(3,5)P 2 (N = 5). Representative plots of normalized currents versus time, before and during application of 100 μM diC8-PIP 3 ( B ), diC8-PI(3,4)P 2 ( C ), or diC8-PI(3,5)P 2 ( D ). ∗ represents p < 0.025 as determined by ANOVA and Tukey's HSD post hoc tests. diC8-PI(3,4)P 2 , dioctanoyl phosphatidylinositol 3,4-bisphosphate; diC8-PI(3,5)P 2 , dioctanoyl phosphatidylinositol 3,5-bisphosphate; diC8-PI(4,5)P 2 , dioctanoyl phosphatidylinositol 4,5-bisphosphate; diC8-HSD, honestly significant difference; PIP 3, dioctanoyl phosphatidylinositol 3,4,5-trisphosphate; PI(3,4)P 2 , phosphatidylinositol 3,4-bisphosphate; PI(3,5)P 2 , dioctanoyl phosphatidylinositol 3,5-bisphosphate; PIP 3, phosphatidyl 3,4,5-trisphosphate; TMEM16A, TransMEMbrane 16A.

    Techniques Used: Stable Transfection

    Phospholipids with phosphates at position 4′ of the inositol ring recover current. Soluble synthetic analogs of PI3P, PI4P, and PI5P were applied to excised inside–out patches once current had stably rundown. Currents were recorded at −60 mV. Representative plots of normalized currents versus time, before and during application of 100 μM diC8-PI3P ( A ), 100 μM diC8-PI5P ( B ), or 100 μM diC8-PI4P ( D ). C , box plot distribution of the fold current recovered after the application of diC8-PI(4,5)P 2 (N = 9), diC8-PI3P (N = 7), diC8-PI4P (N = 7), or diC8-PI5P (N = 5). ∗ denotes p < 0.05 between indicated treatment and diC8-PI(4,5)P 2 , as determined by ANOVA and Tukey’s HSD post hoc tests. diC8-PI3P, dioctanoyl 3-monophosphate; diC8-PI4P, dioctanoyl 4-monophosphate; diC8-PI5P, dioctanoyl 5-monophosphate; HSD, honestly significant difference.
    Figure Legend Snippet: Phospholipids with phosphates at position 4′ of the inositol ring recover current. Soluble synthetic analogs of PI3P, PI4P, and PI5P were applied to excised inside–out patches once current had stably rundown. Currents were recorded at −60 mV. Representative plots of normalized currents versus time, before and during application of 100 μM diC8-PI3P ( A ), 100 μM diC8-PI5P ( B ), or 100 μM diC8-PI4P ( D ). C , box plot distribution of the fold current recovered after the application of diC8-PI(4,5)P 2 (N = 9), diC8-PI3P (N = 7), diC8-PI4P (N = 7), or diC8-PI5P (N = 5). ∗ denotes p < 0.05 between indicated treatment and diC8-PI(4,5)P 2 , as determined by ANOVA and Tukey’s HSD post hoc tests. diC8-PI3P, dioctanoyl 3-monophosphate; diC8-PI4P, dioctanoyl 4-monophosphate; diC8-PI5P, dioctanoyl 5-monophosphate; HSD, honestly significant difference.

    Techniques Used: Stable Transfection

    Docking suggests key PI(4,5)P 2 phosphate interactions with TMEM16A. Docking was performed with either diC8-PI(4,5)P 2 or IP 3 into a homology model of Xenopus laevis TMEM16A (xTMEM16A). A , position of diC8-PI(4,5)P 2 shown against the homology model of xTMEM16A. Lines indicating the position of the intracellular and extracellular boundaries of the plasma membrane were created using the OPM entry for mouse TMEM16A (PDB: 5OYB ). B , detailed view of the hypothesized PI(4,5)P 2 –xTMEM16A interaction. Interacting residues (E442, K446, R450, K592, and K912 from the other chain) and phosphates (positions 2′–5′) are highlighted. C , superposition of docked IP 3 (foreground) on the PI(4,5)P 2 –xTMEM16A (transparency) interaction. diC8-PI(4,5)P 2 , dioctanoyl phosphatidylinositol 4,5-bisphosphate; PDB, Protein Data Bank; PI(4,5)P 2, dioctanoyl phosphatidylinositol 4,5-bisphosphate; TMEM16A, TransMEMbrane 16A; xTMEM16A, Xenopus laevis TransMEMbrane 16A.
    Figure Legend Snippet: Docking suggests key PI(4,5)P 2 phosphate interactions with TMEM16A. Docking was performed with either diC8-PI(4,5)P 2 or IP 3 into a homology model of Xenopus laevis TMEM16A (xTMEM16A). A , position of diC8-PI(4,5)P 2 shown against the homology model of xTMEM16A. Lines indicating the position of the intracellular and extracellular boundaries of the plasma membrane were created using the OPM entry for mouse TMEM16A (PDB: 5OYB ). B , detailed view of the hypothesized PI(4,5)P 2 –xTMEM16A interaction. Interacting residues (E442, K446, R450, K592, and K912 from the other chain) and phosphates (positions 2′–5′) are highlighted. C , superposition of docked IP 3 (foreground) on the PI(4,5)P 2 –xTMEM16A (transparency) interaction. diC8-PI(4,5)P 2 , dioctanoyl phosphatidylinositol 4,5-bisphosphate; PDB, Protein Data Bank; PI(4,5)P 2, dioctanoyl phosphatidylinositol 4,5-bisphosphate; TMEM16A, TransMEMbrane 16A; xTMEM16A, Xenopus laevis TransMEMbrane 16A.

    Techniques Used:

    dic8 pip 3  (Echelon Biosciences)


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    Structured Review

    Echelon Biosciences dic8 pip 3
    TMEM16A Ca 2+ -evoked Cl − currents rundown in excised patches and are recovered by a <t>diC8-PI(4,5)P</t> 2 application. A , example currents recorded at the indicated times during 150 ms steps to −60 and +60 mV, recorded using excised inside–out macropatches from Xenopus laevis oocytes. B , normalized plot of current measured at −60 mV versus time, fit with a single exponential ( red line ). C , box plot distribution of the rate of current decay (τ), measured by fitting plots of relative current versus time with single exponentials (N = 11). The central line denotes the median, the box denotes 25 to 75% of the data, and the whiskers represent 10 to 90% of the data. D , a soluble synthetic analog of PI(4,5)P 2 , <t>diC8-PI(4,5)P</t> 2 , was applied to excised inside–out patches once current had stably rundown. Currents were recorded at −60 mV. E , box plot distribution of the fold current recovered after the application of <t>diC8-PI(4,5)P</t> 2 with Ca 2+ (N = 8). <t>diC8-PI(4,5)P</t> 2 , dioctanoyl phosphatidylinositol 4,5-bisphosphate; TMEM16A, TransMEMbrane 16A.
    Dic8 Pip 3, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/dic8 pip 3/product/Echelon Biosciences
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    dic8 pip 3 - by Bioz Stars, 2024-07
    93/100 stars

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    1) Product Images from "Phosphate position is key in mediating transmembrane ion channel TMEM16A–phosphatidylinositol 4,5-bisphosphate interaction"

    Article Title: Phosphate position is key in mediating transmembrane ion channel TMEM16A–phosphatidylinositol 4,5-bisphosphate interaction

    Journal: The Journal of Biological Chemistry

    doi: 10.1016/j.jbc.2022.102264

    TMEM16A Ca 2+ -evoked Cl − currents rundown in excised patches and are recovered by a diC8-PI(4,5)P 2 application. A , example currents recorded at the indicated times during 150 ms steps to −60 and +60 mV, recorded using excised inside–out macropatches from Xenopus laevis oocytes. B , normalized plot of current measured at −60 mV versus time, fit with a single exponential ( red line ). C , box plot distribution of the rate of current decay (τ), measured by fitting plots of relative current versus time with single exponentials (N = 11). The central line denotes the median, the box denotes 25 to 75% of the data, and the whiskers represent 10 to 90% of the data. D , a soluble synthetic analog of PI(4,5)P 2 , diC8-PI(4,5)P 2 , was applied to excised inside–out patches once current had stably rundown. Currents were recorded at −60 mV. E , box plot distribution of the fold current recovered after the application of diC8-PI(4,5)P 2 with Ca 2+ (N = 8). diC8-PI(4,5)P 2 , dioctanoyl phosphatidylinositol 4,5-bisphosphate; TMEM16A, TransMEMbrane 16A.
    Figure Legend Snippet: TMEM16A Ca 2+ -evoked Cl − currents rundown in excised patches and are recovered by a diC8-PI(4,5)P 2 application. A , example currents recorded at the indicated times during 150 ms steps to −60 and +60 mV, recorded using excised inside–out macropatches from Xenopus laevis oocytes. B , normalized plot of current measured at −60 mV versus time, fit with a single exponential ( red line ). C , box plot distribution of the rate of current decay (τ), measured by fitting plots of relative current versus time with single exponentials (N = 11). The central line denotes the median, the box denotes 25 to 75% of the data, and the whiskers represent 10 to 90% of the data. D , a soluble synthetic analog of PI(4,5)P 2 , diC8-PI(4,5)P 2 , was applied to excised inside–out patches once current had stably rundown. Currents were recorded at −60 mV. E , box plot distribution of the fold current recovered after the application of diC8-PI(4,5)P 2 with Ca 2+ (N = 8). diC8-PI(4,5)P 2 , dioctanoyl phosphatidylinositol 4,5-bisphosphate; TMEM16A, TransMEMbrane 16A.

    Techniques Used: Stable Transfection

    Phospholipid analogs differentially recovered TMEM16A. Soluble synthetic analogs of PIP 3 (diC8-PIP 3 ), PI(3,4)P 2 (diC8-PI(3,4)P 2 ), and PI(3,5)P 2 were applied to excised inside–out patches once current had stably rundown. Currents were recorded at −60 mV. A , box plot distribution of the fold current recovered after the application of diC8-PI(4,5)P 2 (N = 9), diC8-PIP 3 (N = 7), diC8-PI(3,4)P 2 (N = 6), or diC8-PI(3,5)P 2 (N = 5). Representative plots of normalized currents versus time, before and during application of 100 μM diC8-PIP 3 ( B ), diC8-PI(3,4)P 2 ( C ), or diC8-PI(3,5)P 2 ( D ). ∗ represents p < 0.025 as determined by ANOVA and Tukey's HSD post hoc tests. diC8-PI(3,4)P 2 , dioctanoyl phosphatidylinositol 3,4-bisphosphate; diC8-PI(3,5)P 2 , dioctanoyl phosphatidylinositol 3,5-bisphosphate; diC8-PI(4,5)P 2 , dioctanoyl phosphatidylinositol 4,5-bisphosphate; diC8-HSD, honestly significant difference; PIP 3, dioctanoyl phosphatidylinositol 3,4,5-trisphosphate; PI(3,4)P 2 , phosphatidylinositol 3,4-bisphosphate; PI(3,5)P 2 , dioctanoyl phosphatidylinositol 3,5-bisphosphate; PIP 3, phosphatidyl 3,4,5-trisphosphate; TMEM16A, TransMEMbrane 16A.
    Figure Legend Snippet: Phospholipid analogs differentially recovered TMEM16A. Soluble synthetic analogs of PIP 3 (diC8-PIP 3 ), PI(3,4)P 2 (diC8-PI(3,4)P 2 ), and PI(3,5)P 2 were applied to excised inside–out patches once current had stably rundown. Currents were recorded at −60 mV. A , box plot distribution of the fold current recovered after the application of diC8-PI(4,5)P 2 (N = 9), diC8-PIP 3 (N = 7), diC8-PI(3,4)P 2 (N = 6), or diC8-PI(3,5)P 2 (N = 5). Representative plots of normalized currents versus time, before and during application of 100 μM diC8-PIP 3 ( B ), diC8-PI(3,4)P 2 ( C ), or diC8-PI(3,5)P 2 ( D ). ∗ represents p < 0.025 as determined by ANOVA and Tukey's HSD post hoc tests. diC8-PI(3,4)P 2 , dioctanoyl phosphatidylinositol 3,4-bisphosphate; diC8-PI(3,5)P 2 , dioctanoyl phosphatidylinositol 3,5-bisphosphate; diC8-PI(4,5)P 2 , dioctanoyl phosphatidylinositol 4,5-bisphosphate; diC8-HSD, honestly significant difference; PIP 3, dioctanoyl phosphatidylinositol 3,4,5-trisphosphate; PI(3,4)P 2 , phosphatidylinositol 3,4-bisphosphate; PI(3,5)P 2 , dioctanoyl phosphatidylinositol 3,5-bisphosphate; PIP 3, phosphatidyl 3,4,5-trisphosphate; TMEM16A, TransMEMbrane 16A.

    Techniques Used: Stable Transfection

    Phospholipids with phosphates at position 4′ of the inositol ring recover current. Soluble synthetic analogs of PI3P, PI4P, and PI5P were applied to excised inside–out patches once current had stably rundown. Currents were recorded at −60 mV. Representative plots of normalized currents versus time, before and during application of 100 μM diC8-PI3P ( A ), 100 μM diC8-PI5P ( B ), or 100 μM diC8-PI4P ( D ). C , box plot distribution of the fold current recovered after the application of diC8-PI(4,5)P 2 (N = 9), diC8-PI3P (N = 7), diC8-PI4P (N = 7), or diC8-PI5P (N = 5). ∗ denotes p < 0.05 between indicated treatment and diC8-PI(4,5)P 2 , as determined by ANOVA and Tukey’s HSD post hoc tests. diC8-PI3P, dioctanoyl 3-monophosphate; diC8-PI4P, dioctanoyl 4-monophosphate; diC8-PI5P, dioctanoyl 5-monophosphate; HSD, honestly significant difference.
    Figure Legend Snippet: Phospholipids with phosphates at position 4′ of the inositol ring recover current. Soluble synthetic analogs of PI3P, PI4P, and PI5P were applied to excised inside–out patches once current had stably rundown. Currents were recorded at −60 mV. Representative plots of normalized currents versus time, before and during application of 100 μM diC8-PI3P ( A ), 100 μM diC8-PI5P ( B ), or 100 μM diC8-PI4P ( D ). C , box plot distribution of the fold current recovered after the application of diC8-PI(4,5)P 2 (N = 9), diC8-PI3P (N = 7), diC8-PI4P (N = 7), or diC8-PI5P (N = 5). ∗ denotes p < 0.05 between indicated treatment and diC8-PI(4,5)P 2 , as determined by ANOVA and Tukey’s HSD post hoc tests. diC8-PI3P, dioctanoyl 3-monophosphate; diC8-PI4P, dioctanoyl 4-monophosphate; diC8-PI5P, dioctanoyl 5-monophosphate; HSD, honestly significant difference.

    Techniques Used: Stable Transfection

    Docking suggests key PI(4,5)P 2 phosphate interactions with TMEM16A. Docking was performed with either diC8-PI(4,5)P 2 or IP 3 into a homology model of Xenopus laevis TMEM16A (xTMEM16A). A , position of diC8-PI(4,5)P 2 shown against the homology model of xTMEM16A. Lines indicating the position of the intracellular and extracellular boundaries of the plasma membrane were created using the OPM entry for mouse TMEM16A (PDB: 5OYB ). B , detailed view of the hypothesized PI(4,5)P 2 –xTMEM16A interaction. Interacting residues (E442, K446, R450, K592, and K912 from the other chain) and phosphates (positions 2′–5′) are highlighted. C , superposition of docked IP 3 (foreground) on the PI(4,5)P 2 –xTMEM16A (transparency) interaction. diC8-PI(4,5)P 2 , dioctanoyl phosphatidylinositol 4,5-bisphosphate; PDB, Protein Data Bank; PI(4,5)P 2, dioctanoyl phosphatidylinositol 4,5-bisphosphate; TMEM16A, TransMEMbrane 16A; xTMEM16A, Xenopus laevis TransMEMbrane 16A.
    Figure Legend Snippet: Docking suggests key PI(4,5)P 2 phosphate interactions with TMEM16A. Docking was performed with either diC8-PI(4,5)P 2 or IP 3 into a homology model of Xenopus laevis TMEM16A (xTMEM16A). A , position of diC8-PI(4,5)P 2 shown against the homology model of xTMEM16A. Lines indicating the position of the intracellular and extracellular boundaries of the plasma membrane were created using the OPM entry for mouse TMEM16A (PDB: 5OYB ). B , detailed view of the hypothesized PI(4,5)P 2 –xTMEM16A interaction. Interacting residues (E442, K446, R450, K592, and K912 from the other chain) and phosphates (positions 2′–5′) are highlighted. C , superposition of docked IP 3 (foreground) on the PI(4,5)P 2 –xTMEM16A (transparency) interaction. diC8-PI(4,5)P 2 , dioctanoyl phosphatidylinositol 4,5-bisphosphate; PDB, Protein Data Bank; PI(4,5)P 2, dioctanoyl phosphatidylinositol 4,5-bisphosphate; TMEM16A, TransMEMbrane 16A; xTMEM16A, Xenopus laevis TransMEMbrane 16A.

    Techniques Used:

    pip 3 p 3908  (Echelon Biosciences)


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    Echelon Biosciences pip 3 p 3908
    Pip 3 P 3908, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 93 stars, based on 1 article reviews
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    free pip 3 p 3908  (Echelon Biosciences)


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    Structured Review

    Echelon Biosciences free pip 3 p 3908
    Free Pip 3 P 3908, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/free pip 3 p 3908/product/Echelon Biosciences
    Average 93 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
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    dioctanoyl pip 3  (Echelon Biosciences)


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    Structured Review

    Echelon Biosciences dioctanoyl pip 3
    ( A ) Schematic representation of PTEN, highlighting various phosphorylation sites. The PBM (residues 1–7) is followed by a phosphatase domain (14–185), the C2 domain (190–351), the 50-amino-acid tail (353–400) containing multiple phosphorylation sites and the PDZ-binding motif (401–403). Differentially phosphorylated constructs of PTEN were produced, referred to as Phos-wtPTEN, Phos-PTEN-4A and Phos-PTEN-2A. ( B ) Phosphatase activity of PTEN against soluble diC 8 -PIP 3 substrates. All activity assays and lipid-binding assays have error bars showing S.D. from the mean, derived from experiments carried out in triplicate. Some error bars are smaller than the marker. All experiments were conducted at least three times. ( C ) Phosphatase activity against IP 4 , a soluble head group substrate. ( D ) Phosphatase activity against a phosphotyrosine-containing polypeptide. ( E ) Phosphatase activity against lipid vesicles containing a long-chain <t>PIP</t> <t>3</t> substrate. PIP 2 -containing vesicles (5%) were incubated with PI3K to generate PIP 3 , which was subsequently dephosphorylated with various concentrations of PTEN. ( F ) Protein/lipid FRET curves of variously phosphorylated PTEN constructs binding to 5% PIP 2 -containing membrane-mimicking vesicles.
    Dioctanoyl Pip 3, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "The intrinsically disordered tails of PTEN and PTEN-L have distinct roles in regulating substrate specificity and membrane activity"

    Article Title: The intrinsically disordered tails of PTEN and PTEN-L have distinct roles in regulating substrate specificity and membrane activity

    Journal: Biochemical Journal

    doi: 10.1042/BJ20150931

    ( A ) Schematic representation of PTEN, highlighting various phosphorylation sites. The PBM (residues 1–7) is followed by a phosphatase domain (14–185), the C2 domain (190–351), the 50-amino-acid tail (353–400) containing multiple phosphorylation sites and the PDZ-binding motif (401–403). Differentially phosphorylated constructs of PTEN were produced, referred to as Phos-wtPTEN, Phos-PTEN-4A and Phos-PTEN-2A. ( B ) Phosphatase activity of PTEN against soluble diC 8 -PIP 3 substrates. All activity assays and lipid-binding assays have error bars showing S.D. from the mean, derived from experiments carried out in triplicate. Some error bars are smaller than the marker. All experiments were conducted at least three times. ( C ) Phosphatase activity against IP 4 , a soluble head group substrate. ( D ) Phosphatase activity against a phosphotyrosine-containing polypeptide. ( E ) Phosphatase activity against lipid vesicles containing a long-chain PIP 3 substrate. PIP 2 -containing vesicles (5%) were incubated with PI3K to generate PIP 3 , which was subsequently dephosphorylated with various concentrations of PTEN. ( F ) Protein/lipid FRET curves of variously phosphorylated PTEN constructs binding to 5% PIP 2 -containing membrane-mimicking vesicles.
    Figure Legend Snippet: ( A ) Schematic representation of PTEN, highlighting various phosphorylation sites. The PBM (residues 1–7) is followed by a phosphatase domain (14–185), the C2 domain (190–351), the 50-amino-acid tail (353–400) containing multiple phosphorylation sites and the PDZ-binding motif (401–403). Differentially phosphorylated constructs of PTEN were produced, referred to as Phos-wtPTEN, Phos-PTEN-4A and Phos-PTEN-2A. ( B ) Phosphatase activity of PTEN against soluble diC 8 -PIP 3 substrates. All activity assays and lipid-binding assays have error bars showing S.D. from the mean, derived from experiments carried out in triplicate. Some error bars are smaller than the marker. All experiments were conducted at least three times. ( C ) Phosphatase activity against IP 4 , a soluble head group substrate. ( D ) Phosphatase activity against a phosphotyrosine-containing polypeptide. ( E ) Phosphatase activity against lipid vesicles containing a long-chain PIP 3 substrate. PIP 2 -containing vesicles (5%) were incubated with PI3K to generate PIP 3 , which was subsequently dephosphorylated with various concentrations of PTEN. ( F ) Protein/lipid FRET curves of variously phosphorylated PTEN constructs binding to 5% PIP 2 -containing membrane-mimicking vesicles.

    Techniques Used: Binding Assay, Construct, Produced, Activity Assay, Derivative Assay, Marker, Incubation

    ( A ) Schematic representation of PTEN-L. The 173-residue N-terminal extension contains the six alanine residue signal sequence. The predicted α-helix between residues 151-L and 174-L (highlighted) has sequence similarity with the PTEN-family members Ci-VSP and TPTE (transmembrane phosphatase with tensin homology), identified here as the MBH. ( B ) Phosphatase activity against lipid vesicles containing a long-chain PIP 3 substrate. PIP 2 -containing vesicles (5%) were incubated with PI3K to generate PIP 3 , which was subsequently dephosphorylated with various concentrations of PTEN. Experiments shown in ( B )–( E ) were conducted at least three times in triplicate. ( C ) Protein/lipid FRET of PTEN-L-6A and wtPTEN. ( D ) Interfacial kinetics experiment, showing different behaviours of wtPTEN, PTEN-L and PTEN-L-ΔMBH. The reactions were conducted with 10 nM protein for 30 min. At this point the reactions were supplemented with more PIP 3 -containing liposomes to a 4-fold molar excess of liposomes to protein. ( E ) Surface dilution of PIP 3 also highlights the different interfacial kinetics of wtPTEN, PTEN-L and PTEN-L-ΔMBH. The bulk concentration of PIP 3 was kept constant by varying the concentration of the carrier lipids. The surface concentration of PIP 3 was altered between 5% or 2.5%. Although wtPTEN and PTEN-L-ΔMBH show only minor perturbations in phosphatase rate between the two surface concentrations of PIP 3 , PTEN-L sees a drastic reduction in phosphatase activity upon dilution of PIP 3 ’s surface concentration.
    Figure Legend Snippet: ( A ) Schematic representation of PTEN-L. The 173-residue N-terminal extension contains the six alanine residue signal sequence. The predicted α-helix between residues 151-L and 174-L (highlighted) has sequence similarity with the PTEN-family members Ci-VSP and TPTE (transmembrane phosphatase with tensin homology), identified here as the MBH. ( B ) Phosphatase activity against lipid vesicles containing a long-chain PIP 3 substrate. PIP 2 -containing vesicles (5%) were incubated with PI3K to generate PIP 3 , which was subsequently dephosphorylated with various concentrations of PTEN. Experiments shown in ( B )–( E ) were conducted at least three times in triplicate. ( C ) Protein/lipid FRET of PTEN-L-6A and wtPTEN. ( D ) Interfacial kinetics experiment, showing different behaviours of wtPTEN, PTEN-L and PTEN-L-ΔMBH. The reactions were conducted with 10 nM protein for 30 min. At this point the reactions were supplemented with more PIP 3 -containing liposomes to a 4-fold molar excess of liposomes to protein. ( E ) Surface dilution of PIP 3 also highlights the different interfacial kinetics of wtPTEN, PTEN-L and PTEN-L-ΔMBH. The bulk concentration of PIP 3 was kept constant by varying the concentration of the carrier lipids. The surface concentration of PIP 3 was altered between 5% or 2.5%. Although wtPTEN and PTEN-L-ΔMBH show only minor perturbations in phosphatase rate between the two surface concentrations of PIP 3 , PTEN-L sees a drastic reduction in phosphatase activity upon dilution of PIP 3 ’s surface concentration.

    Techniques Used: Sequencing, Activity Assay, Incubation, Concentration Assay

    dic 8 pip 3  (Echelon Biosciences)


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    Echelon Biosciences dic8 pip 3
    TMEM16A Ca 2+ -evoked Cl − currents rundown in excised patches and are recovered by a <t>diC8-PI(4,5)P</t> 2 application. A , example currents recorded at the indicated times during 150 ms steps to −60 and +60 mV, recorded using excised inside–out macropatches from Xenopus laevis oocytes. B , normalized plot of current measured at −60 mV versus time, fit with a single exponential ( red line ). C , box plot distribution of the rate of current decay (τ), measured by fitting plots of relative current versus time with single exponentials (N = 11). The central line denotes the median, the box denotes 25 to 75% of the data, and the whiskers represent 10 to 90% of the data. D , a soluble synthetic analog of PI(4,5)P 2 , <t>diC8-PI(4,5)P</t> 2 , was applied to excised inside–out patches once current had stably rundown. Currents were recorded at −60 mV. E , box plot distribution of the fold current recovered after the application of <t>diC8-PI(4,5)P</t> 2 with Ca 2+ (N = 8). <t>diC8-PI(4,5)P</t> 2 , dioctanoyl phosphatidylinositol 4,5-bisphosphate; TMEM16A, TransMEMbrane 16A.
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    Echelon Biosciences pip 3 p 3908
    TMEM16A Ca 2+ -evoked Cl − currents rundown in excised patches and are recovered by a <t>diC8-PI(4,5)P</t> 2 application. A , example currents recorded at the indicated times during 150 ms steps to −60 and +60 mV, recorded using excised inside–out macropatches from Xenopus laevis oocytes. B , normalized plot of current measured at −60 mV versus time, fit with a single exponential ( red line ). C , box plot distribution of the rate of current decay (τ), measured by fitting plots of relative current versus time with single exponentials (N = 11). The central line denotes the median, the box denotes 25 to 75% of the data, and the whiskers represent 10 to 90% of the data. D , a soluble synthetic analog of PI(4,5)P 2 , <t>diC8-PI(4,5)P</t> 2 , was applied to excised inside–out patches once current had stably rundown. Currents were recorded at −60 mV. E , box plot distribution of the fold current recovered after the application of <t>diC8-PI(4,5)P</t> 2 with Ca 2+ (N = 8). <t>diC8-PI(4,5)P</t> 2 , dioctanoyl phosphatidylinositol 4,5-bisphosphate; TMEM16A, TransMEMbrane 16A.
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    Echelon Biosciences free pip 3 p 3908
    TMEM16A Ca 2+ -evoked Cl − currents rundown in excised patches and are recovered by a <t>diC8-PI(4,5)P</t> 2 application. A , example currents recorded at the indicated times during 150 ms steps to −60 and +60 mV, recorded using excised inside–out macropatches from Xenopus laevis oocytes. B , normalized plot of current measured at −60 mV versus time, fit with a single exponential ( red line ). C , box plot distribution of the rate of current decay (τ), measured by fitting plots of relative current versus time with single exponentials (N = 11). The central line denotes the median, the box denotes 25 to 75% of the data, and the whiskers represent 10 to 90% of the data. D , a soluble synthetic analog of PI(4,5)P 2 , <t>diC8-PI(4,5)P</t> 2 , was applied to excised inside–out patches once current had stably rundown. Currents were recorded at −60 mV. E , box plot distribution of the fold current recovered after the application of <t>diC8-PI(4,5)P</t> 2 with Ca 2+ (N = 8). <t>diC8-PI(4,5)P</t> 2 , dioctanoyl phosphatidylinositol 4,5-bisphosphate; TMEM16A, TransMEMbrane 16A.
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    Echelon Biosciences dioctanoyl pip 3
    ( A ) Schematic representation of PTEN, highlighting various phosphorylation sites. The PBM (residues 1–7) is followed by a phosphatase domain (14–185), the C2 domain (190–351), the 50-amino-acid tail (353–400) containing multiple phosphorylation sites and the PDZ-binding motif (401–403). Differentially phosphorylated constructs of PTEN were produced, referred to as Phos-wtPTEN, Phos-PTEN-4A and Phos-PTEN-2A. ( B ) Phosphatase activity of PTEN against soluble diC 8 -PIP 3 substrates. All activity assays and lipid-binding assays have error bars showing S.D. from the mean, derived from experiments carried out in triplicate. Some error bars are smaller than the marker. All experiments were conducted at least three times. ( C ) Phosphatase activity against IP 4 , a soluble head group substrate. ( D ) Phosphatase activity against a phosphotyrosine-containing polypeptide. ( E ) Phosphatase activity against lipid vesicles containing a long-chain <t>PIP</t> <t>3</t> substrate. PIP 2 -containing vesicles (5%) were incubated with PI3K to generate PIP 3 , which was subsequently dephosphorylated with various concentrations of PTEN. ( F ) Protein/lipid FRET curves of variously phosphorylated PTEN constructs binding to 5% PIP 2 -containing membrane-mimicking vesicles.
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    Echelon Biosciences dic 8 pip 3
    ( A ) Schematic representation of PTEN, highlighting various phosphorylation sites. The PBM (residues 1–7) is followed by a phosphatase domain (14–185), the C2 domain (190–351), the 50-amino-acid tail (353–400) containing multiple phosphorylation sites and the PDZ-binding motif (401–403). Differentially phosphorylated constructs of PTEN were produced, referred to as Phos-wtPTEN, Phos-PTEN-4A and Phos-PTEN-2A. ( B ) Phosphatase activity of PTEN against soluble diC 8 -PIP 3 substrates. All activity assays and lipid-binding assays have error bars showing S.D. from the mean, derived from experiments carried out in triplicate. Some error bars are smaller than the marker. All experiments were conducted at least three times. ( C ) Phosphatase activity against IP 4 , a soluble head group substrate. ( D ) Phosphatase activity against a phosphotyrosine-containing polypeptide. ( E ) Phosphatase activity against lipid vesicles containing a long-chain <t>PIP</t> <t>3</t> substrate. PIP 2 -containing vesicles (5%) were incubated with PI3K to generate PIP 3 , which was subsequently dephosphorylated with various concentrations of PTEN. ( F ) Protein/lipid FRET curves of variously phosphorylated PTEN constructs binding to 5% PIP 2 -containing membrane-mimicking vesicles.
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    TMEM16A Ca 2+ -evoked Cl − currents rundown in excised patches and are recovered by a diC8-PI(4,5)P 2 application. A , example currents recorded at the indicated times during 150 ms steps to −60 and +60 mV, recorded using excised inside–out macropatches from Xenopus laevis oocytes. B , normalized plot of current measured at −60 mV versus time, fit with a single exponential ( red line ). C , box plot distribution of the rate of current decay (τ), measured by fitting plots of relative current versus time with single exponentials (N = 11). The central line denotes the median, the box denotes 25 to 75% of the data, and the whiskers represent 10 to 90% of the data. D , a soluble synthetic analog of PI(4,5)P 2 , diC8-PI(4,5)P 2 , was applied to excised inside–out patches once current had stably rundown. Currents were recorded at −60 mV. E , box plot distribution of the fold current recovered after the application of diC8-PI(4,5)P 2 with Ca 2+ (N = 8). diC8-PI(4,5)P 2 , dioctanoyl phosphatidylinositol 4,5-bisphosphate; TMEM16A, TransMEMbrane 16A.

    Journal: The Journal of Biological Chemistry

    Article Title: Phosphate position is key in mediating transmembrane ion channel TMEM16A–phosphatidylinositol 4,5-bisphosphate interaction

    doi: 10.1016/j.jbc.2022.102264

    Figure Lengend Snippet: TMEM16A Ca 2+ -evoked Cl − currents rundown in excised patches and are recovered by a diC8-PI(4,5)P 2 application. A , example currents recorded at the indicated times during 150 ms steps to −60 and +60 mV, recorded using excised inside–out macropatches from Xenopus laevis oocytes. B , normalized plot of current measured at −60 mV versus time, fit with a single exponential ( red line ). C , box plot distribution of the rate of current decay (τ), measured by fitting plots of relative current versus time with single exponentials (N = 11). The central line denotes the median, the box denotes 25 to 75% of the data, and the whiskers represent 10 to 90% of the data. D , a soluble synthetic analog of PI(4,5)P 2 , diC8-PI(4,5)P 2 , was applied to excised inside–out patches once current had stably rundown. Currents were recorded at −60 mV. E , box plot distribution of the fold current recovered after the application of diC8-PI(4,5)P 2 with Ca 2+ (N = 8). diC8-PI(4,5)P 2 , dioctanoyl phosphatidylinositol 4,5-bisphosphate; TMEM16A, TransMEMbrane 16A.

    Article Snippet: The following dioctanoyl phospholipids were obtained from Echelon Biosciences: diC8-PI3P, diC8-PI4P, diC8-PI5P, diC8-PI(3,4)P 2 , diC8-PI(4,5)P 2 , diC8-PI(3,5)P 2 , and diC8-PIP 3 .

    Techniques: Stable Transfection

    Phospholipid analogs differentially recovered TMEM16A. Soluble synthetic analogs of PIP 3 (diC8-PIP 3 ), PI(3,4)P 2 (diC8-PI(3,4)P 2 ), and PI(3,5)P 2 were applied to excised inside–out patches once current had stably rundown. Currents were recorded at −60 mV. A , box plot distribution of the fold current recovered after the application of diC8-PI(4,5)P 2 (N = 9), diC8-PIP 3 (N = 7), diC8-PI(3,4)P 2 (N = 6), or diC8-PI(3,5)P 2 (N = 5). Representative plots of normalized currents versus time, before and during application of 100 μM diC8-PIP 3 ( B ), diC8-PI(3,4)P 2 ( C ), or diC8-PI(3,5)P 2 ( D ). ∗ represents p < 0.025 as determined by ANOVA and Tukey's HSD post hoc tests. diC8-PI(3,4)P 2 , dioctanoyl phosphatidylinositol 3,4-bisphosphate; diC8-PI(3,5)P 2 , dioctanoyl phosphatidylinositol 3,5-bisphosphate; diC8-PI(4,5)P 2 , dioctanoyl phosphatidylinositol 4,5-bisphosphate; diC8-HSD, honestly significant difference; PIP 3, dioctanoyl phosphatidylinositol 3,4,5-trisphosphate; PI(3,4)P 2 , phosphatidylinositol 3,4-bisphosphate; PI(3,5)P 2 , dioctanoyl phosphatidylinositol 3,5-bisphosphate; PIP 3, phosphatidyl 3,4,5-trisphosphate; TMEM16A, TransMEMbrane 16A.

    Journal: The Journal of Biological Chemistry

    Article Title: Phosphate position is key in mediating transmembrane ion channel TMEM16A–phosphatidylinositol 4,5-bisphosphate interaction

    doi: 10.1016/j.jbc.2022.102264

    Figure Lengend Snippet: Phospholipid analogs differentially recovered TMEM16A. Soluble synthetic analogs of PIP 3 (diC8-PIP 3 ), PI(3,4)P 2 (diC8-PI(3,4)P 2 ), and PI(3,5)P 2 were applied to excised inside–out patches once current had stably rundown. Currents were recorded at −60 mV. A , box plot distribution of the fold current recovered after the application of diC8-PI(4,5)P 2 (N = 9), diC8-PIP 3 (N = 7), diC8-PI(3,4)P 2 (N = 6), or diC8-PI(3,5)P 2 (N = 5). Representative plots of normalized currents versus time, before and during application of 100 μM diC8-PIP 3 ( B ), diC8-PI(3,4)P 2 ( C ), or diC8-PI(3,5)P 2 ( D ). ∗ represents p < 0.025 as determined by ANOVA and Tukey's HSD post hoc tests. diC8-PI(3,4)P 2 , dioctanoyl phosphatidylinositol 3,4-bisphosphate; diC8-PI(3,5)P 2 , dioctanoyl phosphatidylinositol 3,5-bisphosphate; diC8-PI(4,5)P 2 , dioctanoyl phosphatidylinositol 4,5-bisphosphate; diC8-HSD, honestly significant difference; PIP 3, dioctanoyl phosphatidylinositol 3,4,5-trisphosphate; PI(3,4)P 2 , phosphatidylinositol 3,4-bisphosphate; PI(3,5)P 2 , dioctanoyl phosphatidylinositol 3,5-bisphosphate; PIP 3, phosphatidyl 3,4,5-trisphosphate; TMEM16A, TransMEMbrane 16A.

    Article Snippet: The following dioctanoyl phospholipids were obtained from Echelon Biosciences: diC8-PI3P, diC8-PI4P, diC8-PI5P, diC8-PI(3,4)P 2 , diC8-PI(4,5)P 2 , diC8-PI(3,5)P 2 , and diC8-PIP 3 .

    Techniques: Stable Transfection

    Phospholipids with phosphates at position 4′ of the inositol ring recover current. Soluble synthetic analogs of PI3P, PI4P, and PI5P were applied to excised inside–out patches once current had stably rundown. Currents were recorded at −60 mV. Representative plots of normalized currents versus time, before and during application of 100 μM diC8-PI3P ( A ), 100 μM diC8-PI5P ( B ), or 100 μM diC8-PI4P ( D ). C , box plot distribution of the fold current recovered after the application of diC8-PI(4,5)P 2 (N = 9), diC8-PI3P (N = 7), diC8-PI4P (N = 7), or diC8-PI5P (N = 5). ∗ denotes p < 0.05 between indicated treatment and diC8-PI(4,5)P 2 , as determined by ANOVA and Tukey’s HSD post hoc tests. diC8-PI3P, dioctanoyl 3-monophosphate; diC8-PI4P, dioctanoyl 4-monophosphate; diC8-PI5P, dioctanoyl 5-monophosphate; HSD, honestly significant difference.

    Journal: The Journal of Biological Chemistry

    Article Title: Phosphate position is key in mediating transmembrane ion channel TMEM16A–phosphatidylinositol 4,5-bisphosphate interaction

    doi: 10.1016/j.jbc.2022.102264

    Figure Lengend Snippet: Phospholipids with phosphates at position 4′ of the inositol ring recover current. Soluble synthetic analogs of PI3P, PI4P, and PI5P were applied to excised inside–out patches once current had stably rundown. Currents were recorded at −60 mV. Representative plots of normalized currents versus time, before and during application of 100 μM diC8-PI3P ( A ), 100 μM diC8-PI5P ( B ), or 100 μM diC8-PI4P ( D ). C , box plot distribution of the fold current recovered after the application of diC8-PI(4,5)P 2 (N = 9), diC8-PI3P (N = 7), diC8-PI4P (N = 7), or diC8-PI5P (N = 5). ∗ denotes p < 0.05 between indicated treatment and diC8-PI(4,5)P 2 , as determined by ANOVA and Tukey’s HSD post hoc tests. diC8-PI3P, dioctanoyl 3-monophosphate; diC8-PI4P, dioctanoyl 4-monophosphate; diC8-PI5P, dioctanoyl 5-monophosphate; HSD, honestly significant difference.

    Article Snippet: The following dioctanoyl phospholipids were obtained from Echelon Biosciences: diC8-PI3P, diC8-PI4P, diC8-PI5P, diC8-PI(3,4)P 2 , diC8-PI(4,5)P 2 , diC8-PI(3,5)P 2 , and diC8-PIP 3 .

    Techniques: Stable Transfection

    Docking suggests key PI(4,5)P 2 phosphate interactions with TMEM16A. Docking was performed with either diC8-PI(4,5)P 2 or IP 3 into a homology model of Xenopus laevis TMEM16A (xTMEM16A). A , position of diC8-PI(4,5)P 2 shown against the homology model of xTMEM16A. Lines indicating the position of the intracellular and extracellular boundaries of the plasma membrane were created using the OPM entry for mouse TMEM16A (PDB: 5OYB ). B , detailed view of the hypothesized PI(4,5)P 2 –xTMEM16A interaction. Interacting residues (E442, K446, R450, K592, and K912 from the other chain) and phosphates (positions 2′–5′) are highlighted. C , superposition of docked IP 3 (foreground) on the PI(4,5)P 2 –xTMEM16A (transparency) interaction. diC8-PI(4,5)P 2 , dioctanoyl phosphatidylinositol 4,5-bisphosphate; PDB, Protein Data Bank; PI(4,5)P 2, dioctanoyl phosphatidylinositol 4,5-bisphosphate; TMEM16A, TransMEMbrane 16A; xTMEM16A, Xenopus laevis TransMEMbrane 16A.

    Journal: The Journal of Biological Chemistry

    Article Title: Phosphate position is key in mediating transmembrane ion channel TMEM16A–phosphatidylinositol 4,5-bisphosphate interaction

    doi: 10.1016/j.jbc.2022.102264

    Figure Lengend Snippet: Docking suggests key PI(4,5)P 2 phosphate interactions with TMEM16A. Docking was performed with either diC8-PI(4,5)P 2 or IP 3 into a homology model of Xenopus laevis TMEM16A (xTMEM16A). A , position of diC8-PI(4,5)P 2 shown against the homology model of xTMEM16A. Lines indicating the position of the intracellular and extracellular boundaries of the plasma membrane were created using the OPM entry for mouse TMEM16A (PDB: 5OYB ). B , detailed view of the hypothesized PI(4,5)P 2 –xTMEM16A interaction. Interacting residues (E442, K446, R450, K592, and K912 from the other chain) and phosphates (positions 2′–5′) are highlighted. C , superposition of docked IP 3 (foreground) on the PI(4,5)P 2 –xTMEM16A (transparency) interaction. diC8-PI(4,5)P 2 , dioctanoyl phosphatidylinositol 4,5-bisphosphate; PDB, Protein Data Bank; PI(4,5)P 2, dioctanoyl phosphatidylinositol 4,5-bisphosphate; TMEM16A, TransMEMbrane 16A; xTMEM16A, Xenopus laevis TransMEMbrane 16A.

    Article Snippet: The following dioctanoyl phospholipids were obtained from Echelon Biosciences: diC8-PI3P, diC8-PI4P, diC8-PI5P, diC8-PI(3,4)P 2 , diC8-PI(4,5)P 2 , diC8-PI(3,5)P 2 , and diC8-PIP 3 .

    Techniques:

    ( A ) Schematic representation of PTEN, highlighting various phosphorylation sites. The PBM (residues 1–7) is followed by a phosphatase domain (14–185), the C2 domain (190–351), the 50-amino-acid tail (353–400) containing multiple phosphorylation sites and the PDZ-binding motif (401–403). Differentially phosphorylated constructs of PTEN were produced, referred to as Phos-wtPTEN, Phos-PTEN-4A and Phos-PTEN-2A. ( B ) Phosphatase activity of PTEN against soluble diC 8 -PIP 3 substrates. All activity assays and lipid-binding assays have error bars showing S.D. from the mean, derived from experiments carried out in triplicate. Some error bars are smaller than the marker. All experiments were conducted at least three times. ( C ) Phosphatase activity against IP 4 , a soluble head group substrate. ( D ) Phosphatase activity against a phosphotyrosine-containing polypeptide. ( E ) Phosphatase activity against lipid vesicles containing a long-chain PIP 3 substrate. PIP 2 -containing vesicles (5%) were incubated with PI3K to generate PIP 3 , which was subsequently dephosphorylated with various concentrations of PTEN. ( F ) Protein/lipid FRET curves of variously phosphorylated PTEN constructs binding to 5% PIP 2 -containing membrane-mimicking vesicles.

    Journal: Biochemical Journal

    Article Title: The intrinsically disordered tails of PTEN and PTEN-L have distinct roles in regulating substrate specificity and membrane activity

    doi: 10.1042/BJ20150931

    Figure Lengend Snippet: ( A ) Schematic representation of PTEN, highlighting various phosphorylation sites. The PBM (residues 1–7) is followed by a phosphatase domain (14–185), the C2 domain (190–351), the 50-amino-acid tail (353–400) containing multiple phosphorylation sites and the PDZ-binding motif (401–403). Differentially phosphorylated constructs of PTEN were produced, referred to as Phos-wtPTEN, Phos-PTEN-4A and Phos-PTEN-2A. ( B ) Phosphatase activity of PTEN against soluble diC 8 -PIP 3 substrates. All activity assays and lipid-binding assays have error bars showing S.D. from the mean, derived from experiments carried out in triplicate. Some error bars are smaller than the marker. All experiments were conducted at least three times. ( C ) Phosphatase activity against IP 4 , a soluble head group substrate. ( D ) Phosphatase activity against a phosphotyrosine-containing polypeptide. ( E ) Phosphatase activity against lipid vesicles containing a long-chain PIP 3 substrate. PIP 2 -containing vesicles (5%) were incubated with PI3K to generate PIP 3 , which was subsequently dephosphorylated with various concentrations of PTEN. ( F ) Protein/lipid FRET curves of variously phosphorylated PTEN constructs binding to 5% PIP 2 -containing membrane-mimicking vesicles.

    Article Snippet: Recombinant PTEN was incubated with 50 μM dioctanoyl-PIP 3 (diC 8 -PIP 3 ) (Echelon) in 50 mM Tris/HCl, pH 8.0, and 2 mM DTT for 10 min at 37°C in a final volume of 25 μl.

    Techniques: Binding Assay, Construct, Produced, Activity Assay, Derivative Assay, Marker, Incubation

    ( A ) Schematic representation of PTEN-L. The 173-residue N-terminal extension contains the six alanine residue signal sequence. The predicted α-helix between residues 151-L and 174-L (highlighted) has sequence similarity with the PTEN-family members Ci-VSP and TPTE (transmembrane phosphatase with tensin homology), identified here as the MBH. ( B ) Phosphatase activity against lipid vesicles containing a long-chain PIP 3 substrate. PIP 2 -containing vesicles (5%) were incubated with PI3K to generate PIP 3 , which was subsequently dephosphorylated with various concentrations of PTEN. Experiments shown in ( B )–( E ) were conducted at least three times in triplicate. ( C ) Protein/lipid FRET of PTEN-L-6A and wtPTEN. ( D ) Interfacial kinetics experiment, showing different behaviours of wtPTEN, PTEN-L and PTEN-L-ΔMBH. The reactions were conducted with 10 nM protein for 30 min. At this point the reactions were supplemented with more PIP 3 -containing liposomes to a 4-fold molar excess of liposomes to protein. ( E ) Surface dilution of PIP 3 also highlights the different interfacial kinetics of wtPTEN, PTEN-L and PTEN-L-ΔMBH. The bulk concentration of PIP 3 was kept constant by varying the concentration of the carrier lipids. The surface concentration of PIP 3 was altered between 5% or 2.5%. Although wtPTEN and PTEN-L-ΔMBH show only minor perturbations in phosphatase rate between the two surface concentrations of PIP 3 , PTEN-L sees a drastic reduction in phosphatase activity upon dilution of PIP 3 ’s surface concentration.

    Journal: Biochemical Journal

    Article Title: The intrinsically disordered tails of PTEN and PTEN-L have distinct roles in regulating substrate specificity and membrane activity

    doi: 10.1042/BJ20150931

    Figure Lengend Snippet: ( A ) Schematic representation of PTEN-L. The 173-residue N-terminal extension contains the six alanine residue signal sequence. The predicted α-helix between residues 151-L and 174-L (highlighted) has sequence similarity with the PTEN-family members Ci-VSP and TPTE (transmembrane phosphatase with tensin homology), identified here as the MBH. ( B ) Phosphatase activity against lipid vesicles containing a long-chain PIP 3 substrate. PIP 2 -containing vesicles (5%) were incubated with PI3K to generate PIP 3 , which was subsequently dephosphorylated with various concentrations of PTEN. Experiments shown in ( B )–( E ) were conducted at least three times in triplicate. ( C ) Protein/lipid FRET of PTEN-L-6A and wtPTEN. ( D ) Interfacial kinetics experiment, showing different behaviours of wtPTEN, PTEN-L and PTEN-L-ΔMBH. The reactions were conducted with 10 nM protein for 30 min. At this point the reactions were supplemented with more PIP 3 -containing liposomes to a 4-fold molar excess of liposomes to protein. ( E ) Surface dilution of PIP 3 also highlights the different interfacial kinetics of wtPTEN, PTEN-L and PTEN-L-ΔMBH. The bulk concentration of PIP 3 was kept constant by varying the concentration of the carrier lipids. The surface concentration of PIP 3 was altered between 5% or 2.5%. Although wtPTEN and PTEN-L-ΔMBH show only minor perturbations in phosphatase rate between the two surface concentrations of PIP 3 , PTEN-L sees a drastic reduction in phosphatase activity upon dilution of PIP 3 ’s surface concentration.

    Article Snippet: Recombinant PTEN was incubated with 50 μM dioctanoyl-PIP 3 (diC 8 -PIP 3 ) (Echelon) in 50 mM Tris/HCl, pH 8.0, and 2 mM DTT for 10 min at 37°C in a final volume of 25 μl.

    Techniques: Sequencing, Activity Assay, Incubation, Concentration Assay