Membrane Protein Targeting to the MVB/Lysosome

被引：45

作者：

Davies, Brian A. ^{[1
]}

Lee, Jacqueline R. E. ^{[1
]}

Oestreich, Andrea J. ^{[1
]}

Katzmann, David J. ^{[1
]}

机构：

[1] Mayo Clin, Coll Med, Dept Biochem & Mol Biol, Rochester, MN 55905 USA

来源：

CHEMICAL REVIEWS | 2009年 / 109卷 / 04期

关键词：

MULTIVESICULAR BODY FORMATION; UBIQUITIN LIGASE RSP5; ESCRT-III PROTEIN; DOA4 DEUBIQUITINATING ENZYME; ENDOSOME-ASSOCIATED COMPLEX; RECEPTOR TYROSINE KINASES; AAA-ATPASE; SORTING COMPLEX; STRUCTURAL BASIS; MIT DOMAIN;

D O I：

10.1021/cr800473s

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

A study was conducted to examine the effect of multivesicular body (MVB) sorting on membrane protein function. MVB sorting reaction within the endocytic pathway showed a cellular mechanism for terminating the function of integral membrane proteins destined for degradation within the lysosome. It was found that MVB sorting recognized a subset of endocytic cargoes and concentrated them into regions within the endosomal membrane. Fusion of the MVB with the lysosome delivered intralumenal vesicles to the hydrolytic environment of the lysosome, where the lipid and protein contents of the vesicles were degraded. The topology of membrane invagination into the endosomal lumen during MVB sorting was found similar to the budding process. The MVB sorting can be used for viral replication and for lysosomal delivery of endocytosed proteins.

引用

页码：1575 / 1586

页数：12

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