Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2022 Oct 20;44(5):931–939. doi: 10.1038/s41401-022-01007-0

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s), under exclusive licence to Shanghai Institute of Materia Medica, Chinese Academy of Sciences and Chinese Pharmacological Society 2022, Springer Nature or its licensor holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.

PMC Copyright notice

Fig. 1 — a Schematic representation of KLHLs structure. KLHLs consist of BTB/POZ domain, BACK domain and Kelch domain. The BTB/POZ domain is essential for dimerization and contributes to CUL3 interaction. The Kelch domain is comprised of six identical motif repeats and mediates specific substrates recruitment. The BACK domain is served as a linker connecting two domains. b The biological process involved in KLHLs regulation. The KLHLs and CUL3 are both dimerized and form CUL3-KLHL complex to identify substrates. The complex then recruits the E2 enzyme when bound to RBX1 and NEDD8, and jointly transfers ubiquitin onto substrates for subsequent proteasome-mediated degradation.