Diversity of structure and function in Cullin E3 ligases

被引：6

作者：

Lin, Calvin P. ^{[1
]}

Komives, Elizabeth A. ^{[1
]}

机构：

[1] Univ Calif San Diego, Dept Chem & Biochem, San Diego, CA 92161 USA

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 2024年 / 88卷

基金：

美国国家科学基金会;

关键词：

UBIQUITIN; MECHANISM; UBIQUITYLATION; INSIGHTS;

D O I：

10.1016/j.sbi.2024.102879

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：

The cellular process by which the protein ubiquitin (Ub) is covalently attached to a protein substrate involves Ub actitogether with a large variety of E3 ligases that impart substrate specificity. The largest family of E3s is the Cullin-RING ligase (CRL) family which utilizes a wide variety of substrate receptors, adapter proteins, and cooperating ligases. Cr yoelectron microscopy (cryoEM) has revealed a wide variety of structures which suggest how Ub transfer occurs. Hydrogen deuterium exchange mass spectrometry (HDXMS) has revealed the role of dynamics and expanded our knowledge of how covalent NEDD8 modification (neddylation) activates the CRLs, particularly by facilitating cooperation with additional RING-between-RING ligases to transfer Ub.

引用

页数：7

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