Williams Roger L, Urbé Sylvie
MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, UK.
Nat Rev Mol Cell Biol. 2007 May;8(5):355-68. doi: 10.1038/nrm2162.
The past two years have seen an explosion in the structural understanding of the endosomal sorting complex required for transport (ESCRT) machinery that facilitates the trafficking of ubiquitylated proteins from endosomes to lysosomes via multivesicular bodies (MVBs). A common organization of all ESCRTs is a rigid core attached to flexibly connected modules that recognize other components of the MVB pathway. Several previously unsuspected key links between multiple ESCRT subunits, phospholipids and ubiquitin have now been elucidated, which, together with the detailed morphological analyses of ESCRT-depletion phenotypes, provide new insights into the mechanism of MVB biogenesis.
在过去两年中，对转运所需内体分选复合物（ESCRT）机制的结构理解有了突飞猛进的发展。ESCRT机制通过多泡体（MVB）促进泛素化蛋白从内体向溶酶体的运输。所有ESCRT的一个共同组织形式是一个刚性核心连接到灵活连接的模块，这些模块识别MVB途径的其他成分。现在已经阐明了多个ESCRT亚基、磷脂和泛素之间一些先前未被怀疑的关键联系，这些联系与对ESCRT缺失表型的详细形态学分析一起，为MVB生物发生机制提供了新的见解。
