A conserved N-terminal motif of CUL3 contributes to assembly and E3 ligase activity of CRL3KLHL22

Abstract The CUL3-RING E3 ubiquitin ligases (CRL3s) play an essential role in response to extracellular nutrition and stress stimuli. The ubiquitin ligase function of CRL3s is activated through dimerization. However, how and why such a dimeric assembly is required for its ligase activity remains elu...

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Bibliographic Details
Published in:Nature Communications
Main Authors: Weize Wang, Ling Liang, Zonglin Dai, Peng Zuo, Shang Yu, Yishuo Lu, Dian Ding, Hongyi Chen, Hui Shan, Yan Jin, Youdong Mao, Yuxin Yin
Format: Article
Language:English
Published: Nature Portfolio 2024-05-01
Online Access:https://doi.org/10.1038/s41467-024-48045-2