pi 3 5 p2  (Echelon Biosciences)


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    Echelon Biosciences pi 3 5 p2
    Pi 3 5 P2, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    pi 3 5 p2  (Echelon Biosciences)


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    Echelon Biosciences pi 3 5 p2
    Pi 3 5 P2, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    pi 3 5 p2  (Echelon Biosciences)


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    Echelon Biosciences pi 3 5 p2
    Structure of the TRPML1‐GCaMP6m‐based Ca 2+ sensor. Colocalization of TRPML1‐GCaMP6m (green) with LysoTracker (red) in Hela cells. Scale bar, 5 µm. ML‐SA1 (20 µM)‐induced peak GCaMP6m responses (ΔF/F 0 ) were increased in CRISPR‐Cas9‐mediated LAMTOR1 KD cells. N = 9–10 cells from 4 independent experiments. TAT‐2031 treatment (10 µM) increased ML‐SA1‐induced TRPML1 Ca 2+ release in both control and LAMTOR1 KD cells. Quantification of peak responses as shown in (D). N = 11–19 cells from 5 independent experiments. Colocalization of TRPML1‐GCaMP6m (green) with LysoTracker (red) in hippocampal neurons. Scale bar, 10 µm. Treatment with GPN (200 µM), BAPTA‐AM (20 µM), or ML‐SI1 (20 µM) blocked ML‐SA1‐induced TRPML1‐GCaMP6m responses in neurons. Quantification of responses in (G). N = 5–8 cells from 3 independent experiments. Both LAMTOR1 KD and TAT‐2031 treatment (10 µM) increased ML‐SA1‐induced TRPML1‐GCaMP6m responses in neurons. Quantification of peak responses as shown in I. N = 6–13 cells from 3 independent experiments. LAMTOR1 KD increased <t>PI(3,5)P2</t> (0.5 µM)‐induced TRPML1‐GCaMP6m responses and the blocking effect of ML‐SI1 treatment (20 µM). Quantification of peak TRPML1‐GCaMP6m responses as shown in (K). N = 6–16 cells from 3 independent experiments. Data information: Data with error bars are represented as means ± SEM. Statistical significance was assessed by Student’s t ‐test (C), two‐way ANOVA with Tukey’s post‐hoc analysis (E, J, L), and one‐way ANOVA with Dunnett’s post‐test (H). * P < 0.05, ** P < 0.01, *** P < 0.001, ### P < 0.001, n.s., not significant. Note that the traces in D, G, I, and K represent the mean values of each group. See also Fig . Source data are available online for this figure.
    Pi 3 5 P2, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "LAMTOR1 inhibition of TRPML1‐dependent lysosomal calcium release regulates dendritic lysosome trafficking and hippocampal neuronal function"

    Article Title: LAMTOR1 inhibition of TRPML1‐dependent lysosomal calcium release regulates dendritic lysosome trafficking and hippocampal neuronal function

    Journal: The EMBO Journal

    doi: 10.15252/embj.2021108119

    Structure of the TRPML1‐GCaMP6m‐based Ca 2+ sensor. Colocalization of TRPML1‐GCaMP6m (green) with LysoTracker (red) in Hela cells. Scale bar, 5 µm. ML‐SA1 (20 µM)‐induced peak GCaMP6m responses (ΔF/F 0 ) were increased in CRISPR‐Cas9‐mediated LAMTOR1 KD cells. N = 9–10 cells from 4 independent experiments. TAT‐2031 treatment (10 µM) increased ML‐SA1‐induced TRPML1 Ca 2+ release in both control and LAMTOR1 KD cells. Quantification of peak responses as shown in (D). N = 11–19 cells from 5 independent experiments. Colocalization of TRPML1‐GCaMP6m (green) with LysoTracker (red) in hippocampal neurons. Scale bar, 10 µm. Treatment with GPN (200 µM), BAPTA‐AM (20 µM), or ML‐SI1 (20 µM) blocked ML‐SA1‐induced TRPML1‐GCaMP6m responses in neurons. Quantification of responses in (G). N = 5–8 cells from 3 independent experiments. Both LAMTOR1 KD and TAT‐2031 treatment (10 µM) increased ML‐SA1‐induced TRPML1‐GCaMP6m responses in neurons. Quantification of peak responses as shown in I. N = 6–13 cells from 3 independent experiments. LAMTOR1 KD increased PI(3,5)P2 (0.5 µM)‐induced TRPML1‐GCaMP6m responses and the blocking effect of ML‐SI1 treatment (20 µM). Quantification of peak TRPML1‐GCaMP6m responses as shown in (K). N = 6–16 cells from 3 independent experiments. Data information: Data with error bars are represented as means ± SEM. Statistical significance was assessed by Student’s t ‐test (C), two‐way ANOVA with Tukey’s post‐hoc analysis (E, J, L), and one‐way ANOVA with Dunnett’s post‐test (H). * P < 0.05, ** P < 0.01, *** P < 0.001, ### P < 0.001, n.s., not significant. Note that the traces in D, G, I, and K represent the mean values of each group. See also Fig . Source data are available online for this figure.
    Figure Legend Snippet: Structure of the TRPML1‐GCaMP6m‐based Ca 2+ sensor. Colocalization of TRPML1‐GCaMP6m (green) with LysoTracker (red) in Hela cells. Scale bar, 5 µm. ML‐SA1 (20 µM)‐induced peak GCaMP6m responses (ΔF/F 0 ) were increased in CRISPR‐Cas9‐mediated LAMTOR1 KD cells. N = 9–10 cells from 4 independent experiments. TAT‐2031 treatment (10 µM) increased ML‐SA1‐induced TRPML1 Ca 2+ release in both control and LAMTOR1 KD cells. Quantification of peak responses as shown in (D). N = 11–19 cells from 5 independent experiments. Colocalization of TRPML1‐GCaMP6m (green) with LysoTracker (red) in hippocampal neurons. Scale bar, 10 µm. Treatment with GPN (200 µM), BAPTA‐AM (20 µM), or ML‐SI1 (20 µM) blocked ML‐SA1‐induced TRPML1‐GCaMP6m responses in neurons. Quantification of responses in (G). N = 5–8 cells from 3 independent experiments. Both LAMTOR1 KD and TAT‐2031 treatment (10 µM) increased ML‐SA1‐induced TRPML1‐GCaMP6m responses in neurons. Quantification of peak responses as shown in I. N = 6–13 cells from 3 independent experiments. LAMTOR1 KD increased PI(3,5)P2 (0.5 µM)‐induced TRPML1‐GCaMP6m responses and the blocking effect of ML‐SI1 treatment (20 µM). Quantification of peak TRPML1‐GCaMP6m responses as shown in (K). N = 6–16 cells from 3 independent experiments. Data information: Data with error bars are represented as means ± SEM. Statistical significance was assessed by Student’s t ‐test (C), two‐way ANOVA with Tukey’s post‐hoc analysis (E, J, L), and one‐way ANOVA with Dunnett’s post‐test (H). * P < 0.05, ** P < 0.01, *** P < 0.001, ### P < 0.001, n.s., not significant. Note that the traces in D, G, I, and K represent the mean values of each group. See also Fig . Source data are available online for this figure.

    Techniques Used: CRISPR, Blocking Assay

    pi 3 5 p2  (Echelon Biosciences)


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    Echelon Biosciences pi 3 5 p2
    Structure of the TRPML1‐GCaMP6m‐based Ca 2+ sensor. Colocalization of TRPML1‐GCaMP6m (green) with LysoTracker (red) in Hela cells. Scale bar, 5 µm. ML‐SA1 (20 µM)‐induced peak GCaMP6m responses (ΔF/F 0 ) were increased in CRISPR‐Cas9‐mediated LAMTOR1 KD cells. N = 9–10 cells from 4 independent experiments. TAT‐2031 treatment (10 µM) increased ML‐SA1‐induced TRPML1 Ca 2+ release in both control and LAMTOR1 KD cells. Quantification of peak responses as shown in (D). N = 11–19 cells from 5 independent experiments. Colocalization of TRPML1‐GCaMP6m (green) with LysoTracker (red) in hippocampal neurons. Scale bar, 10 µm. Treatment with GPN (200 µM), BAPTA‐AM (20 µM), or ML‐SI1 (20 µM) blocked ML‐SA1‐induced TRPML1‐GCaMP6m responses in neurons. Quantification of responses in (G). N = 5–8 cells from 3 independent experiments. Both LAMTOR1 KD and TAT‐2031 treatment (10 µM) increased ML‐SA1‐induced TRPML1‐GCaMP6m responses in neurons. Quantification of peak responses as shown in I. N = 6–13 cells from 3 independent experiments. LAMTOR1 KD increased <t>PI(3,5)P2</t> (0.5 µM)‐induced TRPML1‐GCaMP6m responses and the blocking effect of ML‐SI1 treatment (20 µM). Quantification of peak TRPML1‐GCaMP6m responses as shown in (K). N = 6–16 cells from 3 independent experiments. Data information: Data with error bars are represented as means ± SEM. Statistical significance was assessed by Student’s t ‐test (C), two‐way ANOVA with Tukey’s post‐hoc analysis (E, J, L), and one‐way ANOVA with Dunnett’s post‐test (H). * P < 0.05, ** P < 0.01, *** P < 0.001, ### P < 0.001, n.s., not significant. Note that the traces in D, G, I, and K represent the mean values of each group. See also Fig . Source data are available online for this figure.
    Pi 3 5 P2, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 94 stars, based on 1 article reviews
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    1) Product Images from "LAMTOR1 inhibition of TRPML1‐dependent lysosomal calcium release regulates dendritic lysosome trafficking and hippocampal neuronal function"

    Article Title: LAMTOR1 inhibition of TRPML1‐dependent lysosomal calcium release regulates dendritic lysosome trafficking and hippocampal neuronal function

    Journal: The EMBO Journal

    doi: 10.15252/embj.2021108119

    Structure of the TRPML1‐GCaMP6m‐based Ca 2+ sensor. Colocalization of TRPML1‐GCaMP6m (green) with LysoTracker (red) in Hela cells. Scale bar, 5 µm. ML‐SA1 (20 µM)‐induced peak GCaMP6m responses (ΔF/F 0 ) were increased in CRISPR‐Cas9‐mediated LAMTOR1 KD cells. N = 9–10 cells from 4 independent experiments. TAT‐2031 treatment (10 µM) increased ML‐SA1‐induced TRPML1 Ca 2+ release in both control and LAMTOR1 KD cells. Quantification of peak responses as shown in (D). N = 11–19 cells from 5 independent experiments. Colocalization of TRPML1‐GCaMP6m (green) with LysoTracker (red) in hippocampal neurons. Scale bar, 10 µm. Treatment with GPN (200 µM), BAPTA‐AM (20 µM), or ML‐SI1 (20 µM) blocked ML‐SA1‐induced TRPML1‐GCaMP6m responses in neurons. Quantification of responses in (G). N = 5–8 cells from 3 independent experiments. Both LAMTOR1 KD and TAT‐2031 treatment (10 µM) increased ML‐SA1‐induced TRPML1‐GCaMP6m responses in neurons. Quantification of peak responses as shown in I. N = 6–13 cells from 3 independent experiments. LAMTOR1 KD increased PI(3,5)P2 (0.5 µM)‐induced TRPML1‐GCaMP6m responses and the blocking effect of ML‐SI1 treatment (20 µM). Quantification of peak TRPML1‐GCaMP6m responses as shown in (K). N = 6–16 cells from 3 independent experiments. Data information: Data with error bars are represented as means ± SEM. Statistical significance was assessed by Student’s t ‐test (C), two‐way ANOVA with Tukey’s post‐hoc analysis (E, J, L), and one‐way ANOVA with Dunnett’s post‐test (H). * P < 0.05, ** P < 0.01, *** P < 0.001, ### P < 0.001, n.s., not significant. Note that the traces in D, G, I, and K represent the mean values of each group. See also Fig . Source data are available online for this figure.
    Figure Legend Snippet: Structure of the TRPML1‐GCaMP6m‐based Ca 2+ sensor. Colocalization of TRPML1‐GCaMP6m (green) with LysoTracker (red) in Hela cells. Scale bar, 5 µm. ML‐SA1 (20 µM)‐induced peak GCaMP6m responses (ΔF/F 0 ) were increased in CRISPR‐Cas9‐mediated LAMTOR1 KD cells. N = 9–10 cells from 4 independent experiments. TAT‐2031 treatment (10 µM) increased ML‐SA1‐induced TRPML1 Ca 2+ release in both control and LAMTOR1 KD cells. Quantification of peak responses as shown in (D). N = 11–19 cells from 5 independent experiments. Colocalization of TRPML1‐GCaMP6m (green) with LysoTracker (red) in hippocampal neurons. Scale bar, 10 µm. Treatment with GPN (200 µM), BAPTA‐AM (20 µM), or ML‐SI1 (20 µM) blocked ML‐SA1‐induced TRPML1‐GCaMP6m responses in neurons. Quantification of responses in (G). N = 5–8 cells from 3 independent experiments. Both LAMTOR1 KD and TAT‐2031 treatment (10 µM) increased ML‐SA1‐induced TRPML1‐GCaMP6m responses in neurons. Quantification of peak responses as shown in I. N = 6–13 cells from 3 independent experiments. LAMTOR1 KD increased PI(3,5)P2 (0.5 µM)‐induced TRPML1‐GCaMP6m responses and the blocking effect of ML‐SI1 treatment (20 µM). Quantification of peak TRPML1‐GCaMP6m responses as shown in (K). N = 6–16 cells from 3 independent experiments. Data information: Data with error bars are represented as means ± SEM. Statistical significance was assessed by Student’s t ‐test (C), two‐way ANOVA with Tukey’s post‐hoc analysis (E, J, L), and one‐way ANOVA with Dunnett’s post‐test (H). * P < 0.05, ** P < 0.01, *** P < 0.001, ### P < 0.001, n.s., not significant. Note that the traces in D, G, I, and K represent the mean values of each group. See also Fig . Source data are available online for this figure.

    Techniques Used: CRISPR, Blocking Assay

    pi 3 5 p2  (Echelon Biosciences)


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    Echelon Biosciences pi 3 5 p2
    Pi 3 5 P2, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    pi 3 5 p2  (Echelon Biosciences)


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    dibutanoyl dic4 pi 3 5 p2  (Echelon Biosciences)


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    Echelon Biosciences dibutanoyl dic4 pi 3 5 p2
    Dibutanoyl Dic4 Pi 3 5 P2, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    pi 3 5 p 2  (Echelon Biosciences)


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    Echelon Biosciences pi 3 5 p 2
    ( A–B ) Representative TPC2-A1-N-evoked currents from enlarged endo-lysosomes isolated from HEK293 cells transiently expressing human TPC2 (hTPC2) ( A ) or a gain-of-function variant, (hTPC2 M484L ) ( B ). Currents were obtained before and after addition of 10 µM TPC2-A1-N in the absence or presence of 1 mM ATP. Recordings were carried out using standard bath and pipette solutions and applying ramp protocols (−100 mV to +100 mV over 500 ms) every 5 s at a holding potential of −60 mV. ( C–D ) Similar to A and B except that TPC2-A1-P (10 µM) was used. ( E–G ) Statistical analysis of current densities (mean ± SEM) recorded at −100 mV for endo-lysosomes expressing TPC2 or TPC2 M484L for TPC2-A1-N ( E ) and TPC2-A1-P ( F ), and the fold-change in current evoked by TPC2-A1-P versus TPC2-A1-N in the two variants ( G ). Red bars are WT and maroon bars are mutant. An unpaired t-test was applied. *p<0.05, **p<0.01, and ***p<0.001 (n > 10 endo-lysosomes per condition). ( H–I ) Ca 2+ signals evoked by TPC2-A1-N ( H ) or TPC2-A1-P ( I ) in Fura-2-loaded HEK293 cells stably expressing hTPC2 L11A/L12A . Recordings (mean responses from three to four independent experiments) were obtained in standard or Na + -free extracellular solution. ( J ) Statistical analysis of the maximal change in Fura-2 ratio (mean ± SEM). An unpaired t-test was applied. *p<0.05. ( K–N ) Agonist-evoked cation currents from enlarged endo-lysosomes isolated from HEK293 cells stably expressing human TPC2 under bi-ionic conditions: 160 mM Na + in the cytosol (bath) and 105 mM Ca 2+ in the lumen (pipette). Representative current-voltage curves before and after stimulation with either 10 μM TPC2-A1-N ( K ), 10 μM TPC2-A1-P ( L ), 50 nM NAADP (4 recordings out of 8 attempts) ( M ), or 1 μM PI(3,5)P 2 ( N ). ATP (1 mM) was added at the end of each experiment. Recordings were carried out using ramp protocols (−100 mV to +100 mV over 500 ms) every 5 s at a holding potential of 0 mV. ( O ) Expanded views of K-N, showing the reversal potentials (E rev ) of currents evoked by the indicated agonist. ( P–Q ) Statistical analyses of E rev ( P ) and the calculated relative cationic permeability ratios ( P Ca / P Na ) ( Q ). Shown are mean values ± SEM. ( R–S ) Representative TPC2-A1-N- ( R ) or TPC2-A1-P- ( S ) evoked currents from endo-lysosomes isolated from HEK293 cells transiently expressing hTPC2 L265P under bi-ionic conditions. Figure 2—source data 1. TPC2 agonists alter Ca/Na permeability of TPC2.
    Pi 3 5 P 2, supplied by Echelon Biosciences, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "Agonist-mediated switching of ion selectivity in TPC2 differentially promotes lysosomal function"

    Article Title: Agonist-mediated switching of ion selectivity in TPC2 differentially promotes lysosomal function

    Journal: eLife

    doi: 10.7554/eLife.54712

    ( A–B ) Representative TPC2-A1-N-evoked currents from enlarged endo-lysosomes isolated from HEK293 cells transiently expressing human TPC2 (hTPC2) ( A ) or a gain-of-function variant, (hTPC2 M484L ) ( B ). Currents were obtained before and after addition of 10 µM TPC2-A1-N in the absence or presence of 1 mM ATP. Recordings were carried out using standard bath and pipette solutions and applying ramp protocols (−100 mV to +100 mV over 500 ms) every 5 s at a holding potential of −60 mV. ( C–D ) Similar to A and B except that TPC2-A1-P (10 µM) was used. ( E–G ) Statistical analysis of current densities (mean ± SEM) recorded at −100 mV for endo-lysosomes expressing TPC2 or TPC2 M484L for TPC2-A1-N ( E ) and TPC2-A1-P ( F ), and the fold-change in current evoked by TPC2-A1-P versus TPC2-A1-N in the two variants ( G ). Red bars are WT and maroon bars are mutant. An unpaired t-test was applied. *p<0.05, **p<0.01, and ***p<0.001 (n > 10 endo-lysosomes per condition). ( H–I ) Ca 2+ signals evoked by TPC2-A1-N ( H ) or TPC2-A1-P ( I ) in Fura-2-loaded HEK293 cells stably expressing hTPC2 L11A/L12A . Recordings (mean responses from three to four independent experiments) were obtained in standard or Na + -free extracellular solution. ( J ) Statistical analysis of the maximal change in Fura-2 ratio (mean ± SEM). An unpaired t-test was applied. *p<0.05. ( K–N ) Agonist-evoked cation currents from enlarged endo-lysosomes isolated from HEK293 cells stably expressing human TPC2 under bi-ionic conditions: 160 mM Na + in the cytosol (bath) and 105 mM Ca 2+ in the lumen (pipette). Representative current-voltage curves before and after stimulation with either 10 μM TPC2-A1-N ( K ), 10 μM TPC2-A1-P ( L ), 50 nM NAADP (4 recordings out of 8 attempts) ( M ), or 1 μM PI(3,5)P 2 ( N ). ATP (1 mM) was added at the end of each experiment. Recordings were carried out using ramp protocols (−100 mV to +100 mV over 500 ms) every 5 s at a holding potential of 0 mV. ( O ) Expanded views of K-N, showing the reversal potentials (E rev ) of currents evoked by the indicated agonist. ( P–Q ) Statistical analyses of E rev ( P ) and the calculated relative cationic permeability ratios ( P Ca / P Na ) ( Q ). Shown are mean values ± SEM. ( R–S ) Representative TPC2-A1-N- ( R ) or TPC2-A1-P- ( S ) evoked currents from endo-lysosomes isolated from HEK293 cells transiently expressing hTPC2 L265P under bi-ionic conditions. Figure 2—source data 1. TPC2 agonists alter Ca/Na permeability of TPC2.
    Figure Legend Snippet: ( A–B ) Representative TPC2-A1-N-evoked currents from enlarged endo-lysosomes isolated from HEK293 cells transiently expressing human TPC2 (hTPC2) ( A ) or a gain-of-function variant, (hTPC2 M484L ) ( B ). Currents were obtained before and after addition of 10 µM TPC2-A1-N in the absence or presence of 1 mM ATP. Recordings were carried out using standard bath and pipette solutions and applying ramp protocols (−100 mV to +100 mV over 500 ms) every 5 s at a holding potential of −60 mV. ( C–D ) Similar to A and B except that TPC2-A1-P (10 µM) was used. ( E–G ) Statistical analysis of current densities (mean ± SEM) recorded at −100 mV for endo-lysosomes expressing TPC2 or TPC2 M484L for TPC2-A1-N ( E ) and TPC2-A1-P ( F ), and the fold-change in current evoked by TPC2-A1-P versus TPC2-A1-N in the two variants ( G ). Red bars are WT and maroon bars are mutant. An unpaired t-test was applied. *p<0.05, **p<0.01, and ***p<0.001 (n > 10 endo-lysosomes per condition). ( H–I ) Ca 2+ signals evoked by TPC2-A1-N ( H ) or TPC2-A1-P ( I ) in Fura-2-loaded HEK293 cells stably expressing hTPC2 L11A/L12A . Recordings (mean responses from three to four independent experiments) were obtained in standard or Na + -free extracellular solution. ( J ) Statistical analysis of the maximal change in Fura-2 ratio (mean ± SEM). An unpaired t-test was applied. *p<0.05. ( K–N ) Agonist-evoked cation currents from enlarged endo-lysosomes isolated from HEK293 cells stably expressing human TPC2 under bi-ionic conditions: 160 mM Na + in the cytosol (bath) and 105 mM Ca 2+ in the lumen (pipette). Representative current-voltage curves before and after stimulation with either 10 μM TPC2-A1-N ( K ), 10 μM TPC2-A1-P ( L ), 50 nM NAADP (4 recordings out of 8 attempts) ( M ), or 1 μM PI(3,5)P 2 ( N ). ATP (1 mM) was added at the end of each experiment. Recordings were carried out using ramp protocols (−100 mV to +100 mV over 500 ms) every 5 s at a holding potential of 0 mV. ( O ) Expanded views of K-N, showing the reversal potentials (E rev ) of currents evoked by the indicated agonist. ( P–Q ) Statistical analyses of E rev ( P ) and the calculated relative cationic permeability ratios ( P Ca / P Na ) ( Q ). Shown are mean values ± SEM. ( R–S ) Representative TPC2-A1-N- ( R ) or TPC2-A1-P- ( S ) evoked currents from endo-lysosomes isolated from HEK293 cells transiently expressing hTPC2 L265P under bi-ionic conditions. Figure 2—source data 1. TPC2 agonists alter Ca/Na permeability of TPC2.

    Techniques Used: Isolation, Expressing, Variant Assay, Transferring, Mutagenesis, Stable Transfection, Permeability


    Figure Legend Snippet:

    Techniques Used: Stable Transfection, Expressing, Generated, Recombinant, Mutagenesis, Plasmid Preparation, Subcloning, Construct, Transfection, Software, Fluorescence, Imaging

    pi 3 5 p 2  (Echelon Biosciences)


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    ( A ) Representative basal I TPC2 step currents elicited by a voltage step protocol in the whole-endolysosome (EL) configuration. Voltage steps from −140 to 100 mV with a voltage increment (∆V) of 20 mV for 0.5 s were used to elicit I TPC2 in A-D. HP = 0 mV. Unless otherwise indicated, symmetric (bath/cytosol vs pipette/lumen) Na + (150 mM) solutions were used for all whole-endolysosome recordings, and PI(3,5)P 2 (0.3 µM), LyNa-VA1.2 (100 µM), and LyNA1 (300 µM) were bath- applied to induce I TPC2 . ( B–D ) Representative I TPC2 step currents activated by PI(3,5)P 2 ( B ), LyNa-VA1.2 ( C ), and LyNA1 ( D ). ( E ) Representative normalized I-V plots based on the instantaneous currents activated by various agonists. ( F ) Rectification index, calculated as the ratio of the current amplitudes between +80 and −80 mV, of PI(3,5)P 2 -, LyNa-VA1.2-, and LyNA1- activated I TPC2 . ( G ) The inactivation of I TPC2 at −120 mV was quantified as the ratio of current amplitudes at 10 vs. 500 ms, based on step currents in B , ( C ) and D. ( H ) Voltage steps from −120 to 100 mV (∆V = 20 mV) for 1 s were used to elicit tail currents at −120 mV shown in ( I ) and ( J ). ( I ) The tail currents of PI(3,5)P 2 - evoked whole-endolysosome I TPC2 . ( J ) The tail currents of LyNa-VA1.2- activated whole-endolysosome I TPC2 . Arrows in ( I ) and ( J ) indicate where the currents were measured to calculate the channel conductance (G = I/V). ( K ) Normalized G-V curves of PI(3,5)P 2 - and LyNa-VA1.2- activated I TPC2 . LyNa-VA1.2 activated I TPC2 in a voltage dependent manner with a V 1/2 = −20.3 ± 3.5 mV (n = 5 patches). For panels F and G , individual data and Mean ± S.E.M. are presented. ***, p<0.001. Individual data for ( F ) and ( G ) are presented in  .  Figure 2—source data 1. The inactivation of I TPC2 and rectification index of TPC2.
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    1) Product Images from "Agonist-specific voltage-dependent gating of lysosomal two-pore Na + channels"

    Article Title: Agonist-specific voltage-dependent gating of lysosomal two-pore Na + channels

    Journal: eLife

    doi: 10.7554/eLife.51423

    ( A ) Representative basal I TPC2 step currents elicited by a voltage step protocol in the whole-endolysosome (EL) configuration. Voltage steps from −140 to 100 mV with a voltage increment (∆V) of 20 mV for 0.5 s were used to elicit I TPC2 in A-D. HP = 0 mV. Unless otherwise indicated, symmetric (bath/cytosol vs pipette/lumen) Na + (150 mM) solutions were used for all whole-endolysosome recordings, and PI(3,5)P 2 (0.3 µM), LyNa-VA1.2 (100 µM), and LyNA1 (300 µM) were bath- applied to induce I TPC2 . ( B–D ) Representative I TPC2 step currents activated by PI(3,5)P 2 ( B ), LyNa-VA1.2 ( C ), and LyNA1 ( D ). ( E ) Representative normalized I-V plots based on the instantaneous currents activated by various agonists. ( F ) Rectification index, calculated as the ratio of the current amplitudes between +80 and −80 mV, of PI(3,5)P 2 -, LyNa-VA1.2-, and LyNA1- activated I TPC2 . ( G ) The inactivation of I TPC2 at −120 mV was quantified as the ratio of current amplitudes at 10 vs. 500 ms, based on step currents in B , ( C ) and D. ( H ) Voltage steps from −120 to 100 mV (∆V = 20 mV) for 1 s were used to elicit tail currents at −120 mV shown in ( I ) and ( J ). ( I ) The tail currents of PI(3,5)P 2 - evoked whole-endolysosome I TPC2 . ( J ) The tail currents of LyNa-VA1.2- activated whole-endolysosome I TPC2 . Arrows in ( I ) and ( J ) indicate where the currents were measured to calculate the channel conductance (G = I/V). ( K ) Normalized G-V curves of PI(3,5)P 2 - and LyNa-VA1.2- activated I TPC2 . LyNa-VA1.2 activated I TPC2 in a voltage dependent manner with a V 1/2 = −20.3 ± 3.5 mV (n = 5 patches). For panels F and G , individual data and Mean ± S.E.M. are presented. ***, p<0.001. Individual data for ( F ) and ( G ) are presented in  .  Figure 2—source data 1. The inactivation of I TPC2 and rectification index of TPC2.
    Figure Legend Snippet: ( A ) Representative basal I TPC2 step currents elicited by a voltage step protocol in the whole-endolysosome (EL) configuration. Voltage steps from −140 to 100 mV with a voltage increment (∆V) of 20 mV for 0.5 s were used to elicit I TPC2 in A-D. HP = 0 mV. Unless otherwise indicated, symmetric (bath/cytosol vs pipette/lumen) Na + (150 mM) solutions were used for all whole-endolysosome recordings, and PI(3,5)P 2 (0.3 µM), LyNa-VA1.2 (100 µM), and LyNA1 (300 µM) were bath- applied to induce I TPC2 . ( B–D ) Representative I TPC2 step currents activated by PI(3,5)P 2 ( B ), LyNa-VA1.2 ( C ), and LyNA1 ( D ). ( E ) Representative normalized I-V plots based on the instantaneous currents activated by various agonists. ( F ) Rectification index, calculated as the ratio of the current amplitudes between +80 and −80 mV, of PI(3,5)P 2 -, LyNa-VA1.2-, and LyNA1- activated I TPC2 . ( G ) The inactivation of I TPC2 at −120 mV was quantified as the ratio of current amplitudes at 10 vs. 500 ms, based on step currents in B , ( C ) and D. ( H ) Voltage steps from −120 to 100 mV (∆V = 20 mV) for 1 s were used to elicit tail currents at −120 mV shown in ( I ) and ( J ). ( I ) The tail currents of PI(3,5)P 2 - evoked whole-endolysosome I TPC2 . ( J ) The tail currents of LyNa-VA1.2- activated whole-endolysosome I TPC2 . Arrows in ( I ) and ( J ) indicate where the currents were measured to calculate the channel conductance (G = I/V). ( K ) Normalized G-V curves of PI(3,5)P 2 - and LyNa-VA1.2- activated I TPC2 . LyNa-VA1.2 activated I TPC2 in a voltage dependent manner with a V 1/2 = −20.3 ± 3.5 mV (n = 5 patches). For panels F and G , individual data and Mean ± S.E.M. are presented. ***, p<0.001. Individual data for ( F ) and ( G ) are presented in . Figure 2—source data 1. The inactivation of I TPC2 and rectification index of TPC2.

    Techniques Used: Transferring

    ( A ) The effects of PI(3,5)P 2 (0.3 µM) and LyNa-VA1.2 (100 µM) on whole-endolysosome I TPC2-K204A in TPC2 K204A -transfected HEK293 cells . ( B ) Comparison effects of LyNa-VA1.2 and PI(3,5)P 2 on WT and PI(3,5)P 2 -insensitive K204A  mutant TPC2 channels (also see  ). ( C ) The synergistic effects of PI(3,5)P 2 (50 nM) and LyNa-VA1.1 on whole-endolysosome I TPC2 and I TPC2-K204A currents. Data are presented as Mean ± S.E.M (n = 3 patches). ( D ) The summary of EC 50 of LyNa-VA1.1 with or without PI(3,5)P 2 for WT and K204A mutant TPC2 channels. ( E, F ) Co-application of PI(3,5)P 2 (0.3 µM) and LyNa-VA1.1 (50 µM) activated whole-endolysome I TPC in WT ( E ) but not TPC1/2 DKO ( F ) HAP1 cells. Note that the endogenous TPCs were more difficult to activate compared to overexpressed TPCs. ( G ) Summary of LyNa-VA1.1 effects on whole-endolysome I TPC in WT and TPC1/2 DKO cells. For panels B, D and F, individual data and Mean ± S.E.M are presented. *, p<0.05; **, p<0.01; ***, p<0.001; N.S., no significance. Individual data for ( B–D ) and ( G ) are presented in  .  Figure 3—source data 1. Synergistic activation of TPC2 channels by TCAs and PI(3,5)P 2 .
    Figure Legend Snippet: ( A ) The effects of PI(3,5)P 2 (0.3 µM) and LyNa-VA1.2 (100 µM) on whole-endolysosome I TPC2-K204A in TPC2 K204A -transfected HEK293 cells . ( B ) Comparison effects of LyNa-VA1.2 and PI(3,5)P 2 on WT and PI(3,5)P 2 -insensitive K204A mutant TPC2 channels (also see ). ( C ) The synergistic effects of PI(3,5)P 2 (50 nM) and LyNa-VA1.1 on whole-endolysosome I TPC2 and I TPC2-K204A currents. Data are presented as Mean ± S.E.M (n = 3 patches). ( D ) The summary of EC 50 of LyNa-VA1.1 with or without PI(3,5)P 2 for WT and K204A mutant TPC2 channels. ( E, F ) Co-application of PI(3,5)P 2 (0.3 µM) and LyNa-VA1.1 (50 µM) activated whole-endolysome I TPC in WT ( E ) but not TPC1/2 DKO ( F ) HAP1 cells. Note that the endogenous TPCs were more difficult to activate compared to overexpressed TPCs. ( G ) Summary of LyNa-VA1.1 effects on whole-endolysome I TPC in WT and TPC1/2 DKO cells. For panels B, D and F, individual data and Mean ± S.E.M are presented. *, p<0.05; **, p<0.01; ***, p<0.001; N.S., no significance. Individual data for ( B–D ) and ( G ) are presented in . Figure 3—source data 1. Synergistic activation of TPC2 channels by TCAs and PI(3,5)P 2 .

    Techniques Used: Transfection, Mutagenesis, Activation Assay

    ( A ) Basal whole-endolysosome I TPC1 (left) or I TPC1-R540I (right) was elicited by voltage steps (−140 to +100 mV with ΔV = 20 mV) in the absence of PI(3,5)P 2 in TPC1-transfected Cos1 cells . Tail currents were elicited at −120 mV. ( B ) The effects of PI(3,5)P 2 (0.3 µM) on I TPC1 (left) and I TPC1-R540I (right) step currents. ( C ) I-V plots of steady-state I TPC1 and I TPC1-R540I step currents shown in B. ( D ) LyNa-VA1.2-induced whole-endolysosome I TPC2-I551R was evoked by a voltage ramp from −120 to +120 mV (duration = 200 ms). ( E ) The basal (right), LyNa-VA1.2 (200 µM)- (middle) and PI(3,5)P 2 (0.3 µM)- (left) activated lysosomal I TPC1-I551R were recorded from the same vacuole. A preconditioning voltage (+80 mV, 0.1 s) was applied before voltage steps starting from −140 to 100 mV (0.5 s, ∆V = 20 mV). HP = 0 mV.
    Figure Legend Snippet: ( A ) Basal whole-endolysosome I TPC1 (left) or I TPC1-R540I (right) was elicited by voltage steps (−140 to +100 mV with ΔV = 20 mV) in the absence of PI(3,5)P 2 in TPC1-transfected Cos1 cells . Tail currents were elicited at −120 mV. ( B ) The effects of PI(3,5)P 2 (0.3 µM) on I TPC1 (left) and I TPC1-R540I (right) step currents. ( C ) I-V plots of steady-state I TPC1 and I TPC1-R540I step currents shown in B. ( D ) LyNa-VA1.2-induced whole-endolysosome I TPC2-I551R was evoked by a voltage ramp from −120 to +120 mV (duration = 200 ms). ( E ) The basal (right), LyNa-VA1.2 (200 µM)- (middle) and PI(3,5)P 2 (0.3 µM)- (left) activated lysosomal I TPC1-I551R were recorded from the same vacuole. A preconditioning voltage (+80 mV, 0.1 s) was applied before voltage steps starting from −140 to 100 mV (0.5 s, ∆V = 20 mV). HP = 0 mV.

    Techniques Used: Transfection

    ( A ) Representative PI(3,5)P 2 -evoked whole-endolysosome I TPC2 elicited by a voltage ramp from −120 to 120 mV. The recordings were performed under a bi-ionic condition with 150 (in mM) Na + in the pipette solution and 150 Na + or 150 K + in the bath solution. PI(3,5)P 2 (0.3 µM) was bath-applied. ( B, C ) Representative PI(3,5)P 2 - evoked I TPC2 elicited with voltage steps (−140 mV to 100 mV with a ∆V = 20 mV, 0.5 s) with 150 mM Na + ( B ) or K + ( C ) in the bath solution. ( D, E ) Representative LyNa-VA1.2-activated I TPC2 step currents. ( F ) Representative I-V plots of LyNa-VA1.2- activated I TPC2 measured from the instantaneous currents in ( D ) and ( E ). Note the reversal potentials (E rev ) of LyNa-VA1.2- activated I TPC2 in the presence of Na + or K + bath solution. ( G ) LyNa-VA1.2- activated I TPC2 under the bi-ionic conditions of bath/cytosolic Na + and pipette/luminal Ca 2+ . 150 Na + solution contained (in mM) 145 NaCl, 5 NaOH, 20 HEPES, (pH 7.2); isotonic (105 mM) Ca 2+ solution contained (in mM) 100 CaCl 2 , 5 Ca(OH) 2 , 20 HEPES (pH 7.2). Right panel zoom-in micrograph shows the E rev of LyNa-VA1.2- activated I TPC2 . ( H–J ) Representative I-V plots of LyNa-VA1.2- evoked I TPC2-N653G ( J ) measured from Na + ( H ) and K + ( I ) bath solution. ( K ) Summary of Na + vs. K + /Ca 2+ selectivity of WT TPC2 and TPC2 N653G channels. Individual data and Mean ± S.E.M are presented (also see  ). N.S., no significance.  Figure 5—source data 1. Ionic selectivity of WT TPC2 and N653G mutant channels.
    Figure Legend Snippet: ( A ) Representative PI(3,5)P 2 -evoked whole-endolysosome I TPC2 elicited by a voltage ramp from −120 to 120 mV. The recordings were performed under a bi-ionic condition with 150 (in mM) Na + in the pipette solution and 150 Na + or 150 K + in the bath solution. PI(3,5)P 2 (0.3 µM) was bath-applied. ( B, C ) Representative PI(3,5)P 2 - evoked I TPC2 elicited with voltage steps (−140 mV to 100 mV with a ∆V = 20 mV, 0.5 s) with 150 mM Na + ( B ) or K + ( C ) in the bath solution. ( D, E ) Representative LyNa-VA1.2-activated I TPC2 step currents. ( F ) Representative I-V plots of LyNa-VA1.2- activated I TPC2 measured from the instantaneous currents in ( D ) and ( E ). Note the reversal potentials (E rev ) of LyNa-VA1.2- activated I TPC2 in the presence of Na + or K + bath solution. ( G ) LyNa-VA1.2- activated I TPC2 under the bi-ionic conditions of bath/cytosolic Na + and pipette/luminal Ca 2+ . 150 Na + solution contained (in mM) 145 NaCl, 5 NaOH, 20 HEPES, (pH 7.2); isotonic (105 mM) Ca 2+ solution contained (in mM) 100 CaCl 2 , 5 Ca(OH) 2 , 20 HEPES (pH 7.2). Right panel zoom-in micrograph shows the E rev of LyNa-VA1.2- activated I TPC2 . ( H–J ) Representative I-V plots of LyNa-VA1.2- evoked I TPC2-N653G ( J ) measured from Na + ( H ) and K + ( I ) bath solution. ( K ) Summary of Na + vs. K + /Ca 2+ selectivity of WT TPC2 and TPC2 N653G channels. Individual data and Mean ± S.E.M are presented (also see ). N.S., no significance. Figure 5—source data 1. Ionic selectivity of WT TPC2 and N653G mutant channels.

    Techniques Used: Transferring, Mutagenesis


    Figure Legend Snippet:

    Techniques Used: Recombinant, Plasmid Preparation, Sequencing, Software

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    ( A–B ) Representative TPC2-A1-N-evoked currents from enlarged endo-lysosomes isolated from HEK293 cells transiently expressing human TPC2 (hTPC2) ( A ) or a gain-of-function variant, (hTPC2 M484L ) ( B ). Currents were obtained before and after addition of 10 µM TPC2-A1-N in the absence or presence of 1 mM ATP. Recordings were carried out using standard bath and pipette solutions and applying ramp protocols (−100 mV to +100 mV over 500 ms) every 5 s at a holding potential of −60 mV. ( C–D ) Similar to A and B except that TPC2-A1-P (10 µM) was used. ( E–G ) Statistical analysis of current densities (mean ± SEM) recorded at −100 mV for endo-lysosomes expressing TPC2 or TPC2 M484L for TPC2-A1-N ( E ) and TPC2-A1-P ( F ), and the fold-change in current evoked by TPC2-A1-P versus TPC2-A1-N in the two variants ( G ). Red bars are WT and maroon bars are mutant. An unpaired t-test was applied. *p<0.05, **p<0.01, and ***p<0.001 (n > 10 endo-lysosomes per condition). ( H–I ) Ca 2+ signals evoked by TPC2-A1-N ( H ) or TPC2-A1-P ( I ) in Fura-2-loaded HEK293 cells stably expressing hTPC2 L11A/L12A . Recordings (mean responses from three to four independent experiments) were obtained in standard or Na + -free extracellular solution. ( J ) Statistical analysis of the maximal change in Fura-2 ratio (mean ± SEM). An unpaired t-test was applied. *p<0.05. ( K–N ) Agonist-evoked cation currents from enlarged endo-lysosomes isolated from HEK293 cells stably expressing human TPC2 under bi-ionic conditions: 160 mM Na + in the cytosol (bath) and 105 mM Ca 2+ in the lumen (pipette). Representative current-voltage curves before and after stimulation with either 10 μM TPC2-A1-N ( K ), 10 μM TPC2-A1-P ( L ), 50 nM NAADP (4 recordings out of 8 attempts) ( M ), or 1 μM PI(3,5)P 2 ( N ). ATP (1 mM) was added at the end of each experiment. Recordings were carried out using ramp protocols (−100 mV to +100 mV over 500 ms) every 5 s at a holding potential of 0 mV. ( O ) Expanded views of K-N, showing the reversal potentials (E rev ) of currents evoked by the indicated agonist. ( P–Q ) Statistical analyses of E rev ( P ) and the calculated relative cationic permeability ratios ( P Ca / P Na ) ( Q ). Shown are mean values ± SEM. ( R–S ) Representative TPC2-A1-N- ( R ) or TPC2-A1-P- ( S ) evoked currents from endo-lysosomes isolated from HEK293 cells transiently expressing hTPC2 L265P under bi-ionic conditions. Figure 2—source data 1. TPC2 agonists alter Ca/Na permeability of TPC2.
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    ( A–B ) Representative TPC2-A1-N-evoked currents from enlarged endo-lysosomes isolated from HEK293 cells transiently expressing human TPC2 (hTPC2) ( A ) or a gain-of-function variant, (hTPC2 M484L ) ( B ). Currents were obtained before and after addition of 10 µM TPC2-A1-N in the absence or presence of 1 mM ATP. Recordings were carried out using standard bath and pipette solutions and applying ramp protocols (−100 mV to +100 mV over 500 ms) every 5 s at a holding potential of −60 mV. ( C–D ) Similar to A and B except that TPC2-A1-P (10 µM) was used. ( E–G ) Statistical analysis of current densities (mean ± SEM) recorded at −100 mV for endo-lysosomes expressing TPC2 or TPC2 M484L for TPC2-A1-N ( E ) and TPC2-A1-P ( F ), and the fold-change in current evoked by TPC2-A1-P versus TPC2-A1-N in the two variants ( G ). Red bars are WT and maroon bars are mutant. An unpaired t-test was applied. *p<0.05, **p<0.01, and ***p<0.001 (n > 10 endo-lysosomes per condition). ( H–I ) Ca 2+ signals evoked by TPC2-A1-N ( H ) or TPC2-A1-P ( I ) in Fura-2-loaded HEK293 cells stably expressing hTPC2 L11A/L12A . Recordings (mean responses from three to four independent experiments) were obtained in standard or Na + -free extracellular solution. ( J ) Statistical analysis of the maximal change in Fura-2 ratio (mean ± SEM). An unpaired t-test was applied. *p<0.05. ( K–N ) Agonist-evoked cation currents from enlarged endo-lysosomes isolated from HEK293 cells stably expressing human TPC2 under bi-ionic conditions: 160 mM Na + in the cytosol (bath) and 105 mM Ca 2+ in the lumen (pipette). Representative current-voltage curves before and after stimulation with either 10 μM TPC2-A1-N ( K ), 10 μM TPC2-A1-P ( L ), 50 nM NAADP (4 recordings out of 8 attempts) ( M ), or 1 μM PI(3,5)P 2 ( N ). ATP (1 mM) was added at the end of each experiment. Recordings were carried out using ramp protocols (−100 mV to +100 mV over 500 ms) every 5 s at a holding potential of 0 mV. ( O ) Expanded views of K-N, showing the reversal potentials (E rev ) of currents evoked by the indicated agonist. ( P–Q ) Statistical analyses of E rev ( P ) and the calculated relative cationic permeability ratios ( P Ca / P Na ) ( Q ). Shown are mean values ± SEM. ( R–S ) Representative TPC2-A1-N- ( R ) or TPC2-A1-P- ( S ) evoked currents from endo-lysosomes isolated from HEK293 cells transiently expressing hTPC2 L265P under bi-ionic conditions. Figure 2—source data 1. TPC2 agonists alter Ca/Na permeability of TPC2.

    Journal: eLife

    Article Title: Agonist-mediated switching of ion selectivity in TPC2 differentially promotes lysosomal function

    doi: 10.7554/eLife.54712

    Figure Lengend Snippet: ( A–B ) Representative TPC2-A1-N-evoked currents from enlarged endo-lysosomes isolated from HEK293 cells transiently expressing human TPC2 (hTPC2) ( A ) or a gain-of-function variant, (hTPC2 M484L ) ( B ). Currents were obtained before and after addition of 10 µM TPC2-A1-N in the absence or presence of 1 mM ATP. Recordings were carried out using standard bath and pipette solutions and applying ramp protocols (−100 mV to +100 mV over 500 ms) every 5 s at a holding potential of −60 mV. ( C–D ) Similar to A and B except that TPC2-A1-P (10 µM) was used. ( E–G ) Statistical analysis of current densities (mean ± SEM) recorded at −100 mV for endo-lysosomes expressing TPC2 or TPC2 M484L for TPC2-A1-N ( E ) and TPC2-A1-P ( F ), and the fold-change in current evoked by TPC2-A1-P versus TPC2-A1-N in the two variants ( G ). Red bars are WT and maroon bars are mutant. An unpaired t-test was applied. *p<0.05, **p<0.01, and ***p<0.001 (n > 10 endo-lysosomes per condition). ( H–I ) Ca 2+ signals evoked by TPC2-A1-N ( H ) or TPC2-A1-P ( I ) in Fura-2-loaded HEK293 cells stably expressing hTPC2 L11A/L12A . Recordings (mean responses from three to four independent experiments) were obtained in standard or Na + -free extracellular solution. ( J ) Statistical analysis of the maximal change in Fura-2 ratio (mean ± SEM). An unpaired t-test was applied. *p<0.05. ( K–N ) Agonist-evoked cation currents from enlarged endo-lysosomes isolated from HEK293 cells stably expressing human TPC2 under bi-ionic conditions: 160 mM Na + in the cytosol (bath) and 105 mM Ca 2+ in the lumen (pipette). Representative current-voltage curves before and after stimulation with either 10 μM TPC2-A1-N ( K ), 10 μM TPC2-A1-P ( L ), 50 nM NAADP (4 recordings out of 8 attempts) ( M ), or 1 μM PI(3,5)P 2 ( N ). ATP (1 mM) was added at the end of each experiment. Recordings were carried out using ramp protocols (−100 mV to +100 mV over 500 ms) every 5 s at a holding potential of 0 mV. ( O ) Expanded views of K-N, showing the reversal potentials (E rev ) of currents evoked by the indicated agonist. ( P–Q ) Statistical analyses of E rev ( P ) and the calculated relative cationic permeability ratios ( P Ca / P Na ) ( Q ). Shown are mean values ± SEM. ( R–S ) Representative TPC2-A1-N- ( R ) or TPC2-A1-P- ( S ) evoked currents from endo-lysosomes isolated from HEK293 cells transiently expressing hTPC2 L265P under bi-ionic conditions. Figure 2—source data 1. TPC2 agonists alter Ca/Na permeability of TPC2.

    Article Snippet: Chemical compound, drug , PI(3,5)P 2 , Echelon Biosciences , P-3508 , .

    Techniques: Isolation, Expressing, Variant Assay, Transferring, Mutagenesis, Stable Transfection, Permeability

    Journal: eLife

    Article Title: Agonist-mediated switching of ion selectivity in TPC2 differentially promotes lysosomal function

    doi: 10.7554/eLife.54712

    Figure Lengend Snippet:

    Article Snippet: Chemical compound, drug , PI(3,5)P 2 , Echelon Biosciences , P-3508 , .

    Techniques: Stable Transfection, Expressing, Generated, Recombinant, Mutagenesis, Plasmid Preparation, Subcloning, Construct, Transfection, Software, Fluorescence, Imaging