基于 N-聚糖的内质网分子伴侣与蛋白质质量控制系统：钙连蛋白结合循环
N-Glycan-based ER Molecular Chaperone and Protein Quality Control System: The Calnexin Binding Cycle.
作者信息
Lamriben Lydia, Graham Jill B, Adams Benjamin M, Hebert Daniel N
机构信息
Department of Biochemistry and Molecular Biology, Program in Molecular and Cellular Biology, University of Massachusetts, Amherst, MA, 01003, USA.
出版信息
Traffic. 2016 Apr;17(4):308-26. doi: 10.1111/tra.12358. Epub 2016 Jan 10.
Abstract
Helenius and colleagues proposed over 20-years ago a paradigm-shifting model for how chaperone binding in the endoplasmic reticulum was mediated and controlled for a new type of molecular chaperone- the carbohydrate-binding chaperones, calnexin and calreticulin. While the originally established basics for this lectin chaperone binding cycle holds true today, there has been a number of important advances that have expanded our understanding of its mechanisms of action, role in protein homeostasis, and its connection to disease states that are highlighted in this review.
摘要
20多年前，海伦纽斯及其同事提出了一种范式转变模型，用于解释内质网中伴侣蛋白结合是如何介导和控制一种新型分子伴侣——碳水化合物结合伴侣蛋白钙连蛋白和钙网蛋白的。虽然最初确立的这种凝集素伴侣蛋白结合循环的基本原理至今仍然适用，但在其作用机制、在蛋白质稳态中的作用以及与疾病状态的联系方面，已经有了许多重要进展，本综述将重点介绍这些进展。
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