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通过可逆泛素化控制内吞运输和信号转导。

Governance of endocytic trafficking and signaling by reversible ubiquitylation.

机构信息

Physiological Laboratory, Institute for Translational Research, University of Liverpool, Crown Street, L69 3BX Liverpool, UK.

出版信息

Dev Cell. 2012 Sep 11;23(3):457-67. doi: 10.1016/j.devcel.2012.08.011.

Abstract

The endosomal pathway provides a major platform for ubiquitin-modifying enzymes, which act upon membrane-associated proteins in transit. Ubiquitylated cargo proteins are recognized by ubiquitin-binding domains inherent to key adaptor proteins at the plasma membrane and sorting endosome. A balance between ubiquitylation and deubiquitylation activities may govern the efficiency of recycling from endosomes to the plasma membrane versus lysosomal sorting through the multivesicular body pathway. We discuss the current knowledge of the properties of adaptors and ubiquitin-modifying proteins and their effects upon the trafficking and signaling of receptors and ligands associated with pathways fundamental to development.

摘要

内体途径为泛素修饰酶提供了一个主要平台,这些酶作用于运输过程中膜相关的蛋白质。泛素化的货物蛋白被质膜和分选内体固有到关键衔接蛋白的泛素结合结构域所识别。泛素化和去泛素化活性之间的平衡可能控制从内体到质膜的再循环效率与通过多泡体途径到溶酶体的分拣效率之比。我们讨论了衔接蛋白和泛素修饰蛋白的特性及其对与发育相关的基本途径的受体和配体的运输和信号转导的影响的现有知识。

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