Cullin3/KCTD5 induces monoubiquitination of ΔNp63α and impairs its activity

FEBS Letters
Hanbing HeChenghua Li

Abstract

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 ΔNp63α, which is a member of the p53 family. Our further investigation revealed that Cullin3/KCTD5 can induce monoubiquitination of ΔNp63α. Cullin3/KCTD5 downregulates the DNA-binding affinity of ΔNp63α, impairing either its transactivity or its transinhibitory activity. Functionally, Cullin3/KCTD5 abates the proproliferation activity of ΔNp63α. These findings suggest that KCTD5-based CRL3 may mediate monoubiquitination and is a novel regulator of ΔNp63α.

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Citations

Apr 18, 2020·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·José RivasOscar Cerda
Feb 7, 2021·FEBS Open Bio·Xueying FanChenghua Li
Feb 28, 2021·The Journal of Pathology·Zuzana PokornáPhilip J Coates

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