Buchberger Alexander
Dept of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18a, D-82152 Martinsried, Germany.
Trends Cell Biol. 2002 May;12(5):216-21. doi: 10.1016/s0962-8924(02)02269-9.
Ubiquitination is a versatile tool of eukaryotic cells for controlling the stability, function and subcellular localization of proteins. The variety of cellular processes regulated by ubiquitination demands high substrate specificity of the ubiquitination machinery as well as the existence of diverse downstream effector proteins interacting with ubiquitinated substrates. Most of these cellular effectors are characterized by a modular composition of ubiquitin-binding motifs and further domains mediating specific functions. Here, I give an overview of important ubiquitin-related protein motifs, including the UBA, UIM, UBD and UBX domains, and propose a model for the role of subclasses of UBA-domain-containing proteins in ubiquitin-mediated proteolysis.
泛素化是真核细胞用于控制蛋白质稳定性、功能和亚细胞定位的一种多功能工具。由泛素化调节的各种细胞过程需要泛素化机制具有高底物特异性,以及存在与泛素化底物相互作用的多种下游效应蛋白。这些细胞效应蛋白中的大多数具有泛素结合基序和介导特定功能的其他结构域的模块化组成。在这里,我概述了重要的泛素相关蛋白基序,包括UBA、UIM、UBD和UBX结构域,并提出了一个关于含UBA结构域蛋白亚类在泛素介导的蛋白水解中作用的模型。