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...
| Published in: | Nature Communications |
|---|---|
| Main Authors: | , , , , , , , , , , , |
| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2024-05-01
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| Online Access: | https://doi.org/10.1038/s41467-024-48045-2 |
