Differential requirements for Alix and ESCRT-III in cytokinesis and HIV-1 release

被引:174
作者
Carlton, Jez G. [1 ]
Agromayor, Monica [1 ]
Martin-Serrano, Juan [1 ]
机构
[1] Kings Coll London, Sch Med, Dept Infect Dis, London SE1 9RT, England
基金
英国医学研究理事会;
关键词
late domain; viral budding; Class E VPS; L-domain; cell division;
D O I
10.1073/pnas.0802008105
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
The ESCRT machinery functions in topologically equivalent membrane fission events, namely multivesicular body formation, the terminal stages of cytokinesis and HIV-1 release. Here, we show that the ESCRT-III-binding protein Alix is recruited to the midbody of dividing cells through binding Cep55 via an evolutionarily conserved peptide. Disruption of Cep55/Alix/ESCRT-III interactions causes formation of aberrant midbodies and cytokinetic failure, demonstrating an essential role for these proteins in midbody morphology and cell division. We also show that the C terminus of Alix encodes a multimerization activity that is essential for its function in Alix-dependent HIV-1 release and for interaction with Tsg 101. Last, we demonstrate that overexpression of Chmp4b and Chmp4c differentially inhibits HIV-1 release and cytokinesis, suggesting possible reasons for gene expansion within the mammalian Class E VPS pathway.
引用
收藏
页码:10541 / 10546
页数:6
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