caldesmon 1 cell signaling technology  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc caldesmon 1 cell signaling technology
    Calpain 1, calpain 2, <t>caldesmon-1</t> and ERK 1/2 are novel TRPC6 binding partners. (A) Table of proteomics results of TRPC6-binding partners from WT human podocytes overexpressing TRPC6-GFP. TRPC6 was seen to bind to TRPC3, TRPC7, and PLCy2, interactions that have been described previously.49,50 Novel interactions with calpain 2 and caldesmon-1 were identified. Podocytes expressing the GFP protein only were used as a control. (B) Interactions reported by proteomics were confirmed in TRPC6 KO cells expressing WT TRPC6-GFP (T6K+WT) by coimmunoprecipitation (TRAP lane). Control agarose beads were used to demonstrate that immunoprecipitation was specific to TRPC6 (control lane). Additional interactions with calpain 1 and ERK 1/2 were also identified. On the basis of the proteomics results, the phosphorylation and/or cleavage states of FAK, talin-1, caldesmon-1, and ERK 1/2 were ascertained through western blotting. (C) T6K had increased FAK phosphorylation at Tyr 397 and decreased ERK phosphorylation compared with control and T6K+WT cells. (D) Cleavage of FAK, talin-1, and caldesmon-1 was decreased in T6K cells compared with controls. For densitometry see Supplemental Figure 3. Con, control; TRAP, GFP-TRAP associated pull-down.
    Caldesmon 1 Cell Signaling Technology, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    1) Product Images from "TRPC6 Binds to and Activates Calpain, Independent of Its Channel Activity, and Regulates Podocyte Cytoskeleton, Cell Adhesion, and Motility"

    Article Title: TRPC6 Binds to and Activates Calpain, Independent of Its Channel Activity, and Regulates Podocyte Cytoskeleton, Cell Adhesion, and Motility

    Journal: Journal of the American Society of Nephrology : JASN

    doi: 10.1681/ASN.2018070729

    Calpain 1, calpain 2, caldesmon-1 and ERK 1/2 are novel TRPC6 binding partners. (A) Table of proteomics results of TRPC6-binding partners from WT human podocytes overexpressing TRPC6-GFP. TRPC6 was seen to bind to TRPC3, TRPC7, and PLCy2, interactions that have been described previously.49,50 Novel interactions with calpain 2 and caldesmon-1 were identified. Podocytes expressing the GFP protein only were used as a control. (B) Interactions reported by proteomics were confirmed in TRPC6 KO cells expressing WT TRPC6-GFP (T6K+WT) by coimmunoprecipitation (TRAP lane). Control agarose beads were used to demonstrate that immunoprecipitation was specific to TRPC6 (control lane). Additional interactions with calpain 1 and ERK 1/2 were also identified. On the basis of the proteomics results, the phosphorylation and/or cleavage states of FAK, talin-1, caldesmon-1, and ERK 1/2 were ascertained through western blotting. (C) T6K had increased FAK phosphorylation at Tyr 397 and decreased ERK phosphorylation compared with control and T6K+WT cells. (D) Cleavage of FAK, talin-1, and caldesmon-1 was decreased in T6K cells compared with controls. For densitometry see Supplemental Figure 3. Con, control; TRAP, GFP-TRAP associated pull-down.
    Figure Legend Snippet: Calpain 1, calpain 2, caldesmon-1 and ERK 1/2 are novel TRPC6 binding partners. (A) Table of proteomics results of TRPC6-binding partners from WT human podocytes overexpressing TRPC6-GFP. TRPC6 was seen to bind to TRPC3, TRPC7, and PLCy2, interactions that have been described previously.49,50 Novel interactions with calpain 2 and caldesmon-1 were identified. Podocytes expressing the GFP protein only were used as a control. (B) Interactions reported by proteomics were confirmed in TRPC6 KO cells expressing WT TRPC6-GFP (T6K+WT) by coimmunoprecipitation (TRAP lane). Control agarose beads were used to demonstrate that immunoprecipitation was specific to TRPC6 (control lane). Additional interactions with calpain 1 and ERK 1/2 were also identified. On the basis of the proteomics results, the phosphorylation and/or cleavage states of FAK, talin-1, caldesmon-1, and ERK 1/2 were ascertained through western blotting. (C) T6K had increased FAK phosphorylation at Tyr 397 and decreased ERK phosphorylation compared with control and T6K+WT cells. (D) Cleavage of FAK, talin-1, and caldesmon-1 was decreased in T6K cells compared with controls. For densitometry see Supplemental Figure 3. Con, control; TRAP, GFP-TRAP associated pull-down.

    Techniques Used: Binding Assay, Expressing, Immunoprecipitation, Western Blot

    Proposed role of the calpain-TRPC6 interaction in podocytes. (A) WT TRPC6 binds to, and acts as a structural scaffold at the membrane for, caldesmon-1 (cald1), ERK 1/2, and calpain. This keeps calpain localized just below the membrane where it can easily cleave its targets talin-1, FAK, and caldesmon-1. (B) In the absence of TRPC6 there is no calcium influx to the cell and calpain is also not localized to the membrane. This means that there is no cleavage of talin-1, FAK, or caldesmon-1. (C) The disease-causing mutant TRPC6 K874* has a truncation at its C terminus. Calpain no longer binds to this form of TRPC6 and is mislocalized. The mutant allows the same calcium influx as WT TRPC6. There is no cleavage of caldesmon-1, talin-1, or FAK. This suggests that the localization of calpain to the membrane is important in its function in the podocyte.
    Figure Legend Snippet: Proposed role of the calpain-TRPC6 interaction in podocytes. (A) WT TRPC6 binds to, and acts as a structural scaffold at the membrane for, caldesmon-1 (cald1), ERK 1/2, and calpain. This keeps calpain localized just below the membrane where it can easily cleave its targets talin-1, FAK, and caldesmon-1. (B) In the absence of TRPC6 there is no calcium influx to the cell and calpain is also not localized to the membrane. This means that there is no cleavage of talin-1, FAK, or caldesmon-1. (C) The disease-causing mutant TRPC6 K874* has a truncation at its C terminus. Calpain no longer binds to this form of TRPC6 and is mislocalized. The mutant allows the same calcium influx as WT TRPC6. There is no cleavage of caldesmon-1, talin-1, or FAK. This suggests that the localization of calpain to the membrane is important in its function in the podocyte.

    Techniques Used: Mutagenesis

    Antibodies Used
    Figure Legend Snippet: Antibodies Used

    Techniques Used:

    caldesmon 1 cell signaling technology  (Cell Signaling Technology Inc)


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    Cell Signaling Technology Inc caldesmon 1 cell signaling technology
    Calpain 1, calpain 2, <t>caldesmon-1</t> and ERK 1/2 are novel TRPC6 binding partners. (A) Table of proteomics results of TRPC6-binding partners from WT human podocytes overexpressing TRPC6-GFP. TRPC6 was seen to bind to TRPC3, TRPC7, and PLCy2, interactions that have been described previously.49,50 Novel interactions with calpain 2 and caldesmon-1 were identified. Podocytes expressing the GFP protein only were used as a control. (B) Interactions reported by proteomics were confirmed in TRPC6 KO cells expressing WT TRPC6-GFP (T6K+WT) by coimmunoprecipitation (TRAP lane). Control agarose beads were used to demonstrate that immunoprecipitation was specific to TRPC6 (control lane). Additional interactions with calpain 1 and ERK 1/2 were also identified. On the basis of the proteomics results, the phosphorylation and/or cleavage states of FAK, talin-1, caldesmon-1, and ERK 1/2 were ascertained through western blotting. (C) T6K had increased FAK phosphorylation at Tyr 397 and decreased ERK phosphorylation compared with control and T6K+WT cells. (D) Cleavage of FAK, talin-1, and caldesmon-1 was decreased in T6K cells compared with controls. For densitometry see Supplemental Figure 3. Con, control; TRAP, GFP-TRAP associated pull-down.
    Caldesmon 1 Cell Signaling Technology, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 92 stars, based on 1 article reviews
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    caldesmon 1 cell signaling technology - by Bioz Stars, 2023-03
    92/100 stars

    Images

    1) Product Images from "TRPC6 Binds to and Activates Calpain, Independent of Its Channel Activity, and Regulates Podocyte Cytoskeleton, Cell Adhesion, and Motility"

    Article Title: TRPC6 Binds to and Activates Calpain, Independent of Its Channel Activity, and Regulates Podocyte Cytoskeleton, Cell Adhesion, and Motility

    Journal: Journal of the American Society of Nephrology : JASN

    doi: 10.1681/ASN.2018070729

    Calpain 1, calpain 2, caldesmon-1 and ERK 1/2 are novel TRPC6 binding partners. (A) Table of proteomics results of TRPC6-binding partners from WT human podocytes overexpressing TRPC6-GFP. TRPC6 was seen to bind to TRPC3, TRPC7, and PLCy2, interactions that have been described previously.49,50 Novel interactions with calpain 2 and caldesmon-1 were identified. Podocytes expressing the GFP protein only were used as a control. (B) Interactions reported by proteomics were confirmed in TRPC6 KO cells expressing WT TRPC6-GFP (T6K+WT) by coimmunoprecipitation (TRAP lane). Control agarose beads were used to demonstrate that immunoprecipitation was specific to TRPC6 (control lane). Additional interactions with calpain 1 and ERK 1/2 were also identified. On the basis of the proteomics results, the phosphorylation and/or cleavage states of FAK, talin-1, caldesmon-1, and ERK 1/2 were ascertained through western blotting. (C) T6K had increased FAK phosphorylation at Tyr 397 and decreased ERK phosphorylation compared with control and T6K+WT cells. (D) Cleavage of FAK, talin-1, and caldesmon-1 was decreased in T6K cells compared with controls. For densitometry see Supplemental Figure 3. Con, control; TRAP, GFP-TRAP associated pull-down.
    Figure Legend Snippet: Calpain 1, calpain 2, caldesmon-1 and ERK 1/2 are novel TRPC6 binding partners. (A) Table of proteomics results of TRPC6-binding partners from WT human podocytes overexpressing TRPC6-GFP. TRPC6 was seen to bind to TRPC3, TRPC7, and PLCy2, interactions that have been described previously.49,50 Novel interactions with calpain 2 and caldesmon-1 were identified. Podocytes expressing the GFP protein only were used as a control. (B) Interactions reported by proteomics were confirmed in TRPC6 KO cells expressing WT TRPC6-GFP (T6K+WT) by coimmunoprecipitation (TRAP lane). Control agarose beads were used to demonstrate that immunoprecipitation was specific to TRPC6 (control lane). Additional interactions with calpain 1 and ERK 1/2 were also identified. On the basis of the proteomics results, the phosphorylation and/or cleavage states of FAK, talin-1, caldesmon-1, and ERK 1/2 were ascertained through western blotting. (C) T6K had increased FAK phosphorylation at Tyr 397 and decreased ERK phosphorylation compared with control and T6K+WT cells. (D) Cleavage of FAK, talin-1, and caldesmon-1 was decreased in T6K cells compared with controls. For densitometry see Supplemental Figure 3. Con, control; TRAP, GFP-TRAP associated pull-down.

    Techniques Used: Binding Assay, Expressing, Immunoprecipitation, Western Blot

    Proposed role of the calpain-TRPC6 interaction in podocytes. (A) WT TRPC6 binds to, and acts as a structural scaffold at the membrane for, caldesmon-1 (cald1), ERK 1/2, and calpain. This keeps calpain localized just below the membrane where it can easily cleave its targets talin-1, FAK, and caldesmon-1. (B) In the absence of TRPC6 there is no calcium influx to the cell and calpain is also not localized to the membrane. This means that there is no cleavage of talin-1, FAK, or caldesmon-1. (C) The disease-causing mutant TRPC6 K874* has a truncation at its C terminus. Calpain no longer binds to this form of TRPC6 and is mislocalized. The mutant allows the same calcium influx as WT TRPC6. There is no cleavage of caldesmon-1, talin-1, or FAK. This suggests that the localization of calpain to the membrane is important in its function in the podocyte.
    Figure Legend Snippet: Proposed role of the calpain-TRPC6 interaction in podocytes. (A) WT TRPC6 binds to, and acts as a structural scaffold at the membrane for, caldesmon-1 (cald1), ERK 1/2, and calpain. This keeps calpain localized just below the membrane where it can easily cleave its targets talin-1, FAK, and caldesmon-1. (B) In the absence of TRPC6 there is no calcium influx to the cell and calpain is also not localized to the membrane. This means that there is no cleavage of talin-1, FAK, or caldesmon-1. (C) The disease-causing mutant TRPC6 K874* has a truncation at its C terminus. Calpain no longer binds to this form of TRPC6 and is mislocalized. The mutant allows the same calcium influx as WT TRPC6. There is no cleavage of caldesmon-1, talin-1, or FAK. This suggests that the localization of calpain to the membrane is important in its function in the podocyte.

    Techniques Used: Mutagenesis

    Antibodies Used
    Figure Legend Snippet: Antibodies Used

    Techniques Used:

    caldesmon 1 cell signaling technology  (Cell Signaling Technology Inc)


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    Structured Review

    Cell Signaling Technology Inc caldesmon 1 cell signaling technology
    Calpain 1, calpain 2, <t>caldesmon-1</t> and ERK 1/2 are novel TRPC6 binding partners. (A) Table of proteomics results of TRPC6-binding partners from WT human podocytes overexpressing TRPC6-GFP. TRPC6 was seen to bind to TRPC3, TRPC7, and PLCy2, interactions that have been described previously.49,50 Novel interactions with calpain 2 and caldesmon-1 were identified. Podocytes expressing the GFP protein only were used as a control. (B) Interactions reported by proteomics were confirmed in TRPC6 KO cells expressing WT TRPC6-GFP (T6K+WT) by coimmunoprecipitation (TRAP lane). Control agarose beads were used to demonstrate that immunoprecipitation was specific to TRPC6 (control lane). Additional interactions with calpain 1 and ERK 1/2 were also identified. On the basis of the proteomics results, the phosphorylation and/or cleavage states of FAK, talin-1, caldesmon-1, and ERK 1/2 were ascertained through western blotting. (C) T6K had increased FAK phosphorylation at Tyr 397 and decreased ERK phosphorylation compared with control and T6K+WT cells. (D) Cleavage of FAK, talin-1, and caldesmon-1 was decreased in T6K cells compared with controls. For densitometry see Supplemental Figure 3. Con, control; TRAP, GFP-TRAP associated pull-down.
    Caldesmon 1 Cell Signaling Technology, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/caldesmon 1 cell signaling technology/product/Cell Signaling Technology Inc
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    caldesmon 1 cell signaling technology - by Bioz Stars, 2023-03
    92/100 stars

    Images

    1) Product Images from "TRPC6 Binds to and Activates Calpain, Independent of Its Channel Activity, and Regulates Podocyte Cytoskeleton, Cell Adhesion, and Motility"

    Article Title: TRPC6 Binds to and Activates Calpain, Independent of Its Channel Activity, and Regulates Podocyte Cytoskeleton, Cell Adhesion, and Motility

    Journal: Journal of the American Society of Nephrology : JASN

    doi: 10.1681/ASN.2018070729

    Calpain 1, calpain 2, caldesmon-1 and ERK 1/2 are novel TRPC6 binding partners. (A) Table of proteomics results of TRPC6-binding partners from WT human podocytes overexpressing TRPC6-GFP. TRPC6 was seen to bind to TRPC3, TRPC7, and PLCy2, interactions that have been described previously.49,50 Novel interactions with calpain 2 and caldesmon-1 were identified. Podocytes expressing the GFP protein only were used as a control. (B) Interactions reported by proteomics were confirmed in TRPC6 KO cells expressing WT TRPC6-GFP (T6K+WT) by coimmunoprecipitation (TRAP lane). Control agarose beads were used to demonstrate that immunoprecipitation was specific to TRPC6 (control lane). Additional interactions with calpain 1 and ERK 1/2 were also identified. On the basis of the proteomics results, the phosphorylation and/or cleavage states of FAK, talin-1, caldesmon-1, and ERK 1/2 were ascertained through western blotting. (C) T6K had increased FAK phosphorylation at Tyr 397 and decreased ERK phosphorylation compared with control and T6K+WT cells. (D) Cleavage of FAK, talin-1, and caldesmon-1 was decreased in T6K cells compared with controls. For densitometry see Supplemental Figure 3. Con, control; TRAP, GFP-TRAP associated pull-down.
    Figure Legend Snippet: Calpain 1, calpain 2, caldesmon-1 and ERK 1/2 are novel TRPC6 binding partners. (A) Table of proteomics results of TRPC6-binding partners from WT human podocytes overexpressing TRPC6-GFP. TRPC6 was seen to bind to TRPC3, TRPC7, and PLCy2, interactions that have been described previously.49,50 Novel interactions with calpain 2 and caldesmon-1 were identified. Podocytes expressing the GFP protein only were used as a control. (B) Interactions reported by proteomics were confirmed in TRPC6 KO cells expressing WT TRPC6-GFP (T6K+WT) by coimmunoprecipitation (TRAP lane). Control agarose beads were used to demonstrate that immunoprecipitation was specific to TRPC6 (control lane). Additional interactions with calpain 1 and ERK 1/2 were also identified. On the basis of the proteomics results, the phosphorylation and/or cleavage states of FAK, talin-1, caldesmon-1, and ERK 1/2 were ascertained through western blotting. (C) T6K had increased FAK phosphorylation at Tyr 397 and decreased ERK phosphorylation compared with control and T6K+WT cells. (D) Cleavage of FAK, talin-1, and caldesmon-1 was decreased in T6K cells compared with controls. For densitometry see Supplemental Figure 3. Con, control; TRAP, GFP-TRAP associated pull-down.

    Techniques Used: Binding Assay, Expressing, Immunoprecipitation, Western Blot

    Proposed role of the calpain-TRPC6 interaction in podocytes. (A) WT TRPC6 binds to, and acts as a structural scaffold at the membrane for, caldesmon-1 (cald1), ERK 1/2, and calpain. This keeps calpain localized just below the membrane where it can easily cleave its targets talin-1, FAK, and caldesmon-1. (B) In the absence of TRPC6 there is no calcium influx to the cell and calpain is also not localized to the membrane. This means that there is no cleavage of talin-1, FAK, or caldesmon-1. (C) The disease-causing mutant TRPC6 K874* has a truncation at its C terminus. Calpain no longer binds to this form of TRPC6 and is mislocalized. The mutant allows the same calcium influx as WT TRPC6. There is no cleavage of caldesmon-1, talin-1, or FAK. This suggests that the localization of calpain to the membrane is important in its function in the podocyte.
    Figure Legend Snippet: Proposed role of the calpain-TRPC6 interaction in podocytes. (A) WT TRPC6 binds to, and acts as a structural scaffold at the membrane for, caldesmon-1 (cald1), ERK 1/2, and calpain. This keeps calpain localized just below the membrane where it can easily cleave its targets talin-1, FAK, and caldesmon-1. (B) In the absence of TRPC6 there is no calcium influx to the cell and calpain is also not localized to the membrane. This means that there is no cleavage of talin-1, FAK, or caldesmon-1. (C) The disease-causing mutant TRPC6 K874* has a truncation at its C terminus. Calpain no longer binds to this form of TRPC6 and is mislocalized. The mutant allows the same calcium influx as WT TRPC6. There is no cleavage of caldesmon-1, talin-1, or FAK. This suggests that the localization of calpain to the membrane is important in its function in the podocyte.

    Techniques Used: Mutagenesis

    Antibodies Used
    Figure Legend Snippet: Antibodies Used

    Techniques Used:

    caldesmon 1 cell signaling technology  (Cell Signaling Technology Inc)


    Bioz Verified Symbol Cell Signaling Technology Inc is a verified supplier
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    Cell Signaling Technology Inc caldesmon 1 cell signaling technology
    Caldesmon 1 Cell Signaling Technology, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/caldesmon 1 cell signaling technology/product/Cell Signaling Technology Inc
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    caldesmon 1 cell signaling technology - by Bioz Stars, 2023-03
    92/100 stars

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    Cell Signaling Technology Inc caldesmon 1 cell signaling technology
    Calpain 1, calpain 2, <t>caldesmon-1</t> and ERK 1/2 are novel TRPC6 binding partners. (A) Table of proteomics results of TRPC6-binding partners from WT human podocytes overexpressing TRPC6-GFP. TRPC6 was seen to bind to TRPC3, TRPC7, and PLCy2, interactions that have been described previously.49,50 Novel interactions with calpain 2 and caldesmon-1 were identified. Podocytes expressing the GFP protein only were used as a control. (B) Interactions reported by proteomics were confirmed in TRPC6 KO cells expressing WT TRPC6-GFP (T6K+WT) by coimmunoprecipitation (TRAP lane). Control agarose beads were used to demonstrate that immunoprecipitation was specific to TRPC6 (control lane). Additional interactions with calpain 1 and ERK 1/2 were also identified. On the basis of the proteomics results, the phosphorylation and/or cleavage states of FAK, talin-1, caldesmon-1, and ERK 1/2 were ascertained through western blotting. (C) T6K had increased FAK phosphorylation at Tyr 397 and decreased ERK phosphorylation compared with control and T6K+WT cells. (D) Cleavage of FAK, talin-1, and caldesmon-1 was decreased in T6K cells compared with controls. For densitometry see Supplemental Figure 3. Con, control; TRAP, GFP-TRAP associated pull-down.
    Caldesmon 1 Cell Signaling Technology, supplied by Cell Signaling Technology Inc, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/caldesmon 1 cell signaling technology/product/Cell Signaling Technology Inc
    Average 92 stars, based on 1 article reviews
    Price from $9.99 to $1999.99
    caldesmon 1 cell signaling technology - by Bioz Stars, 2023-03
    92/100 stars
    		  Buy from Supplier

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    Calpain 1, calpain 2, caldesmon-1 and ERK 1/2 are novel TRPC6 binding partners. (A) Table of proteomics results of TRPC6-binding partners from WT human podocytes overexpressing TRPC6-GFP. TRPC6 was seen to bind to TRPC3, TRPC7, and PLCy2, interactions that have been described previously.49,50 Novel interactions with calpain 2 and caldesmon-1 were identified. Podocytes expressing the GFP protein only were used as a control. (B) Interactions reported by proteomics were confirmed in TRPC6 KO cells expressing WT TRPC6-GFP (T6K+WT) by coimmunoprecipitation (TRAP lane). Control agarose beads were used to demonstrate that immunoprecipitation was specific to TRPC6 (control lane). Additional interactions with calpain 1 and ERK 1/2 were also identified. On the basis of the proteomics results, the phosphorylation and/or cleavage states of FAK, talin-1, caldesmon-1, and ERK 1/2 were ascertained through western blotting. (C) T6K had increased FAK phosphorylation at Tyr 397 and decreased ERK phosphorylation compared with control and T6K+WT cells. (D) Cleavage of FAK, talin-1, and caldesmon-1 was decreased in T6K cells compared with controls. For densitometry see Supplemental Figure 3. Con, control; TRAP, GFP-TRAP associated pull-down.

    Journal: Journal of the American Society of Nephrology : JASN

    Article Title: TRPC6 Binds to and Activates Calpain, Independent of Its Channel Activity, and Regulates Podocyte Cytoskeleton, Cell Adhesion, and Motility

    doi: 10.1681/ASN.2018070729

    Figure Lengend Snippet: Calpain 1, calpain 2, caldesmon-1 and ERK 1/2 are novel TRPC6 binding partners. (A) Table of proteomics results of TRPC6-binding partners from WT human podocytes overexpressing TRPC6-GFP. TRPC6 was seen to bind to TRPC3, TRPC7, and PLCy2, interactions that have been described previously.49,50 Novel interactions with calpain 2 and caldesmon-1 were identified. Podocytes expressing the GFP protein only were used as a control. (B) Interactions reported by proteomics were confirmed in TRPC6 KO cells expressing WT TRPC6-GFP (T6K+WT) by coimmunoprecipitation (TRAP lane). Control agarose beads were used to demonstrate that immunoprecipitation was specific to TRPC6 (control lane). Additional interactions with calpain 1 and ERK 1/2 were also identified. On the basis of the proteomics results, the phosphorylation and/or cleavage states of FAK, talin-1, caldesmon-1, and ERK 1/2 were ascertained through western blotting. (C) T6K had increased FAK phosphorylation at Tyr 397 and decreased ERK phosphorylation compared with control and T6K+WT cells. (D) Cleavage of FAK, talin-1, and caldesmon-1 was decreased in T6K cells compared with controls. For densitometry see Supplemental Figure 3. Con, control; TRAP, GFP-TRAP associated pull-down.

    Article Snippet: 25 – 27 Antibody Supplier and Catalog Number TRPC6 Cell Signaling Technology #16716 Caldesmon-1 Cell Signaling Technology #2980 Calpain 1 Cell Signaling Technology #2556 Calpain 2 Cell Signaling Technology #2539S Calpain 1 Abcam #ab28258 Talin-1 Cell Signaling Technology #4021 Phospho-p44/p42 (ERK1/2) Cell Signaling Technology #4370S FAK Cell Signaling Technology #3285S Phospho-FAK (Tyr397) Cell Signaling Technology #8556S Synaptopodin Santa Cruz #sc-515842 WT1 Cell Signaling technology #13580 Podocin Abcam #ab50339 CD2AP Cell Signaling #5478 Nephrin Acris #BP5030 GFP Sigma #11814460001 CD99 Kind gift from Professor George Banting University of Bristol.

    Techniques: Binding Assay, Expressing, Immunoprecipitation, Western Blot

    Proposed role of the calpain-TRPC6 interaction in podocytes. (A) WT TRPC6 binds to, and acts as a structural scaffold at the membrane for, caldesmon-1 (cald1), ERK 1/2, and calpain. This keeps calpain localized just below the membrane where it can easily cleave its targets talin-1, FAK, and caldesmon-1. (B) In the absence of TRPC6 there is no calcium influx to the cell and calpain is also not localized to the membrane. This means that there is no cleavage of talin-1, FAK, or caldesmon-1. (C) The disease-causing mutant TRPC6 K874* has a truncation at its C terminus. Calpain no longer binds to this form of TRPC6 and is mislocalized. The mutant allows the same calcium influx as WT TRPC6. There is no cleavage of caldesmon-1, talin-1, or FAK. This suggests that the localization of calpain to the membrane is important in its function in the podocyte.

    Journal: Journal of the American Society of Nephrology : JASN

    Article Title: TRPC6 Binds to and Activates Calpain, Independent of Its Channel Activity, and Regulates Podocyte Cytoskeleton, Cell Adhesion, and Motility

    doi: 10.1681/ASN.2018070729

    Figure Lengend Snippet: Proposed role of the calpain-TRPC6 interaction in podocytes. (A) WT TRPC6 binds to, and acts as a structural scaffold at the membrane for, caldesmon-1 (cald1), ERK 1/2, and calpain. This keeps calpain localized just below the membrane where it can easily cleave its targets talin-1, FAK, and caldesmon-1. (B) In the absence of TRPC6 there is no calcium influx to the cell and calpain is also not localized to the membrane. This means that there is no cleavage of talin-1, FAK, or caldesmon-1. (C) The disease-causing mutant TRPC6 K874* has a truncation at its C terminus. Calpain no longer binds to this form of TRPC6 and is mislocalized. The mutant allows the same calcium influx as WT TRPC6. There is no cleavage of caldesmon-1, talin-1, or FAK. This suggests that the localization of calpain to the membrane is important in its function in the podocyte.

    Article Snippet: 25 – 27 Antibody Supplier and Catalog Number TRPC6 Cell Signaling Technology #16716 Caldesmon-1 Cell Signaling Technology #2980 Calpain 1 Cell Signaling Technology #2556 Calpain 2 Cell Signaling Technology #2539S Calpain 1 Abcam #ab28258 Talin-1 Cell Signaling Technology #4021 Phospho-p44/p42 (ERK1/2) Cell Signaling Technology #4370S FAK Cell Signaling Technology #3285S Phospho-FAK (Tyr397) Cell Signaling Technology #8556S Synaptopodin Santa Cruz #sc-515842 WT1 Cell Signaling technology #13580 Podocin Abcam #ab50339 CD2AP Cell Signaling #5478 Nephrin Acris #BP5030 GFP Sigma #11814460001 CD99 Kind gift from Professor George Banting University of Bristol.

    Techniques: Mutagenesis

    Antibodies Used

    Journal: Journal of the American Society of Nephrology : JASN

    Article Title: TRPC6 Binds to and Activates Calpain, Independent of Its Channel Activity, and Regulates Podocyte Cytoskeleton, Cell Adhesion, and Motility

    doi: 10.1681/ASN.2018070729

    Figure Lengend Snippet: Antibodies Used

    Article Snippet: 25 – 27 Antibody Supplier and Catalog Number TRPC6 Cell Signaling Technology #16716 Caldesmon-1 Cell Signaling Technology #2980 Calpain 1 Cell Signaling Technology #2556 Calpain 2 Cell Signaling Technology #2539S Calpain 1 Abcam #ab28258 Talin-1 Cell Signaling Technology #4021 Phospho-p44/p42 (ERK1/2) Cell Signaling Technology #4370S FAK Cell Signaling Technology #3285S Phospho-FAK (Tyr397) Cell Signaling Technology #8556S Synaptopodin Santa Cruz #sc-515842 WT1 Cell Signaling technology #13580 Podocin Abcam #ab50339 CD2AP Cell Signaling #5478 Nephrin Acris #BP5030 GFP Sigma #11814460001 CD99 Kind gift from Professor George Banting University of Bristol.

    Techniques: