Structural insights into SMCR8 C-degron recognition by FEM1B

被引：11
|
作者：
Zhao, Shidong [1 ,2 ]
Ru, Wenwen [1 ,2 ]
Chen, Xinyan [1 ,2 ]
Liao, Shanhui [1 ,2 ]
Zhu, Zhongliang [1 ,2 ]
Zhang, Jiahai [1 ,2 ]
Xu, Chao [1 ,2 ]
机构：
[1] Univ Sci & Technol China, Hefei Natl Lab Phys Sci Microscale, MOE Key Lab Membraneless Organelles & Cellular Dy, Hefei 230027, Peoples R China
[2] Univ Sci & Technol China, Sch Life Sci, Hefei 230027, Peoples R China
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2021年 / 557卷
基金：
中国国家自然科学基金;
关键词：
Ubiquitination; Protein degradation; Degron; Cullin-RING E3 ligase; E3 UBIQUITIN LIGASES; PROTEIN; DEGRADATION;
D O I：
10.1016/j.bbrc.2021.04.046
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
C-degrons play critical roles in targeting the receptor proteins of Cullin-RING E3 ligase complexes to initiate protein degradation. FEM1 proteins, including FEM1A, FEM1B, and FEM1C, act as the receptors to specifically recognize Arg/C-degrons to enable CRL2-mediated protein turnover. Very few substrates have been identified for FEM1B, except CDK5R1. We found that CRL2(FEM1B) also recognizes the C-degron of an SMCR8 isoform, and uncovered the recognition of SMCR8 by FEM1B through presenting the structure of FEM1B bound to SMCR8. Our work provides insights into the role of CRL2(FEM1B) in regulating the lifetime of SMCR8, a critical autophagy regulator. (C) 2021 Elsevier Inc. All rights reserved.
引用
收藏
页码：236 / 239
页数：4
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