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网格蛋白和衔接蛋白。

Clathrin and adaptors.

作者信息

Hirst J, Robinson M S

机构信息

Department of Clinical Biochemistry, University of Cambridge, Addenbrooke's Hospital, Hills Road, Cambridge CB2 2QR, UK.

出版信息

Biochim Biophys Acta. 1998 Aug 14;1404(1-2):173-93. doi: 10.1016/s0167-4889(98)00056-1.

Abstract

Clathrin and adaptors are components of clathrin-coated pits and vesicles. The AP-1 adaptor complex is associated with clathrin-coated vesicles budding from the TGN, while the AP-2 adaptor complex is associated with clathrin-coated vesicles budding from the plasma membrane. The clathrin forms a polyhedral lattice and is believed to be the driving force behind membrane invagination leading to vesicle budding. The adaptors attach the clathrin to the membrane and also interact with the cytoplasmic domains of selected transmembrane proteins, causing these proteins to become concentrated in clathrin-coated vesicles. Clathrin-coated vesicles budding from the TGN have been implicated in the sorting of newly synthesised lysosomal enzymes, while clathrin-coated vesicles budding from the plasma membrane facilitate the receptor-mediated endocytosis of ligands, such as low density lipoproteins and transferrin. A novel adaptor-related complex, AP-3, has recently been identified, which is recruited onto membranes of the TGN and a more peripheral compartment but does not appear to be associated with clathrin. Genetic studies indicate that AP-3 plays a role in the sorting of proteins to lysosomes and lysosome-related organelles.

摘要

网格蛋白和衔接蛋白是网格蛋白包被小窝和小泡的组成成分。AP-1衔接蛋白复合体与从反式高尔基体网络出芽的网格蛋白包被小泡相关,而AP-2衔接蛋白复合体与从质膜出芽的网格蛋白包被小泡相关。网格蛋白形成多面体晶格,被认为是导致小泡出芽的膜内陷背后的驱动力。衔接蛋白将网格蛋白连接到膜上,还与选定跨膜蛋白的胞质结构域相互作用,使这些蛋白在网格蛋白包被小泡中富集。从反式高尔基体网络出芽的网格蛋白包被小泡与新合成的溶酶体酶的分选有关,而从质膜出芽的网格蛋白包被小泡促进受体介导的配体(如低密度脂蛋白和转铁蛋白)的内吞作用。最近鉴定出一种新型的衔接蛋白相关复合体AP-3,它被募集到反式高尔基体网络和一个更外周区室的膜上,但似乎不与网格蛋白相关。遗传学研究表明,AP-3在蛋白质分选中对溶酶体和溶酶体相关细胞器起作用。

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