Differential requirements for Alix and ESCRT-III in cytokinesis and HIV-1 release.
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.
Mesh Terms:
Calcium-Binding Proteins, Cell Cycle Proteins, Cell Nucleus, Cytokinesis, DNA-Binding Proteins, Endosomal Sorting Complexes Required for Transport, Endosomes, Gene Expression Regulation, Gene Expression Regulation, Viral, HIV-1, HeLa Cells, Humans, Models, Biological, Nuclear Proteins, Protein Binding, Protein Structure, Tertiary, RNA, Small Interfering, Transcription Factors, Vesicular Transport Proteins
Calcium-Binding Proteins, Cell Cycle Proteins, Cell Nucleus, Cytokinesis, DNA-Binding Proteins, Endosomal Sorting Complexes Required for Transport, Endosomes, Gene Expression Regulation, Gene Expression Regulation, Viral, HIV-1, HeLa Cells, Humans, Models, Biological, Nuclear Proteins, Protein Binding, Protein Structure, Tertiary, RNA, Small Interfering, Transcription Factors, Vesicular Transport Proteins
Proc. Natl. Acad. Sci. U.S.A.
Date: Jul. 29, 2008
PubMed ID: 18641129
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