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泛素化机制在内质网蛋白错位与降解中的作用。

The role of the ubiquitination machinery in dislocation and degradation of endoplasmic reticulum proteins.

作者信息

Kikkert M, Hassink G, Wiertz E

机构信息

Department of Medical Microbiology, Leiden University Medical Center (LUMC), Albinusdreef 2, 2333 ZA Leiden, The Netherlands.

出版信息

Curr Top Microbiol Immunol. 2005;300:57-93. doi: 10.1007/3-540-28007-3_4.

Abstract

Ubiquitination is essential for the dislocation and degradation of proteins from the endoplasmic reticulum (ER). How exactly this is regulated is unknown at present. This review provides an overview of ubiquitin-conjugating enzymes (E2s) and ubiquitin ligases (E3s) with a role in the degradation of ER proteins. Their structure and functions are described, as well as their mutual interactions. Substrate specificity and functional redundancy of E3 ligases are discussed, and other components of the ER degradation machinery that may associate with the ubiquitination system are reviewed.

摘要

泛素化对于内质网(ER)中蛋白质的错位和降解至关重要。目前尚不清楚其具体调控方式。本综述概述了在内质网蛋白质降解中起作用的泛素结合酶(E2s)和泛素连接酶(E3s)。描述了它们的结构和功能,以及它们之间的相互作用。讨论了E3连接酶的底物特异性和功能冗余,并综述了可能与泛素化系统相关的内质网降解机制的其他组分。

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