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通过 UBA 结构域泛素化调节 SQSTM1/p62 及其在疾病中的作用。

Regulation of SQSTM1/p62 via UBA domain ubiquitination and its role in disease.

机构信息

a Department of Neurology , Washington University School of Medicine , St. Louis , MO , USA.

出版信息

Autophagy. 2017 Sep 2;13(9):1615-1616. doi: 10.1080/15548627.2017.1339845. Epub 2017 Aug 16.

Abstract

Macroautophagy/autophagy can be a selective degradative process via the utilization of various autophagic receptor proteins. Autophagic receptors selectively recognize ubiquitinated cargoes and deliver them to phagophores, the precursors to autophagosomes, for their degradation. For example, SQSTM1/p62 directly binds to ubiquitinated protein aggregates via its UBA domain and sequesters them into inclusion bodies via its PB1 domain. SQSTM1also interacts with phagophores via its LC3-interacting (LIR) motif. However, a regulatory mechanism for autophagic receptors is not yet understood.

摘要

巨自噬/自噬可以是一种通过利用各种自噬受体蛋白的选择性降解过程。自噬受体选择性地识别泛素化的货物,并将其递送至吞噬体(自噬体的前体)进行降解。例如,SQSTM1/p62 通过其 UBA 结构域直接与泛素化蛋白聚集体结合,并通过其 PB1 结构域将其隔离到包含体中。SQSTM1 还通过其 LC3 相互作用(LIR)基序与吞噬体相互作用。然而,自噬受体的调控机制尚不清楚。

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