Cullin3/KCTD5 induces monoubiquitination of ÎNp63α and impairs its activity.
[No authors listed]
摘要
Potassium channel tetramerization domain containing 5 (KCTD5) was previously documented as a component of the Cullin3-RING ligase (CRL3). It has been reported that KCTD5 can induce enrichment of polyubiquitinated proteins, and KCTD5-based CRL3 destabilizes several proteins. In our present study, we report that KCTD5 may physically interact with ÎNp63α, which is a member of the p53 family. Our further investigation revealed that Cullin3/KCTD5 can induce monoubiquitination of ÎNp63α. Cullin3/KCTD5 downregulates the DNA-binding affinity of ÎNp63α, impairing either its transactivity or its transinhibitory activity. Functionally, Cullin3/KCTD5 abates the proproliferation activity of ÎNp63α. These findings suggest that KCTD5-based CRL3 may mediate monoubiquitination and is a novel regulator of ÎNp63α.
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基因功能
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原始数据
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文献解读
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