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

Research output: Contribution to journalArticle

Original languageEnglish
Pages (from-to)10541-6
Number of pages6
JournalProceedings of National Academy of Sciences USA
Volume105
Issue number30
DOIs
Publication statusPublished - 29 Jul 2008

King's Authors

Abstract

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 Tsg101. 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.

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