IndraLab

Statements

STUB1 binds KCNA5. 12 / 12
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"Effects of Hsc70 on Kv1.5 were similar to CHIP by altering interaction of CHIP with Kv1.5 protein."
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"The function of CHIP in Kv1.5 protein regulation was first suggested by immunoprecipitation studies that showed interaction of CHIP with Kv1.5 proteins ( Fig. 1 A)."
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"First, to examine whether the E3 ligase CHIP interacts with Kv1.5 protein, we introduced Kv1.5-FLAG and myc-CHIP WT into HEK 293 cells."
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"Myc-CHIP ∆TPR also showed decreased interaction with Kv1.5 ( Fig. 5 B), reflecting that the interaction of CHIP with Kv1.5 is Hsc70 dependent."
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"Cooperation of STUB1 and HSC70 may lead to enhanced ubiquitination of genes, for example, HSC70 is required for STUB1 to form a complex with Kv1.5 proteins [36] ."
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"Overexpression of Hsc70 intensified, but knockdown of Hsc70 diminished, the interaction of CHIP with Kv1.5 proteins ( Fig. 7 A)."
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No evidence text available
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"The interaction of CHIP with Kv1.5 was enhanced by overexpressed Hsc70 but depressed by siRNA against Hsc70 ( Fig. 6 B, bottom), indicating that Hsc70 is indispensable for the CHIP activity."
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"Knockdown of Hsc70 diminished interaction of Kv1.5 with CHIP ( Fig. 6 B), indicating that CHIP requires Hsc70 to form a complex with Kv1.5 proteins."
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"Immunoprecipitation showed that CHIP formed complexes with Kv1.5 proteins and heat shock cognate protein 70 (Hsc70)."
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"Our findings presented evidence that Kv1.5 is a substrate of CHIP, and that CHIP associates with Kv1.5 proteins to depress their expression and channel function."
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No evidence text available
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