Buchmann Institute for Molecular Life Sciences and Institute of Biochemistry II, Goethe University School of Medicine, Theodor-Stern-Kai 7, 60590 Frankfurt am Main, Germany.
FEBS Lett. 2012 Aug 14;586(17):2705-10. doi: 10.1016/j.febslet.2012.04.053. Epub 2012 May 5.
Ubiquitin-binding modules are constituents of cellular proteins that mediate the effects of ubiquitylation by making transient, non-covalent interactions with ubiquitin molecules. While some ubiquitin-binding modules bind single ubiquitin moieties, others are selective for specific ubiquitin chains of different linkage types and lengths. In recent years, functions of ubiquitin chains that are polymerized through their Lys or N-terminal Met (i.e. linear chains) residues have been linked to a variety of cellular processes. Selectivity of ubiquitin-binding modules for different ubiquitin chain types appears as a key to the distinct regulatory consequences during protein quality control pathways, receptor endocytosis, gene transcription, signaling via the NF-κB pathway, and autophagy.
泛素结合模块是细胞蛋白的组成部分，通过与泛素分子形成短暂的非共价相互作用，介导泛素化的作用。虽然有些泛素结合模块结合单个泛素分子，但其他模块则对不同连接类型和长度的特定泛素链具有选择性。近年来，通过赖氨酸或 N 端甲硫氨酸（即线性链）残基聚合的泛素链的功能已与多种细胞过程相关联。泛素结合模块对不同泛素链类型的选择性似乎是蛋白质质量控制途径、受体内吞、通过 NF-κB 途径的信号转导和自噬中不同调节后果的关键。
