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• W2149579871 endingPage "7691" @default.
• W2149579871 startingPage "7687" @default.
• W2149579871 abstract "The ESCRT pathway facilitates membrane fission events during enveloped virus budding, multivesicular body formation, and cytokinesis. To promote HIV budding and cytokinesis, the ALIX protein must bind and recruit CHMP4 subunits of the ESCRT-III complex, which in turn participate in essential membrane remodeling functions. Here, we report that the Bro1 domain of ALIX binds specifically to C-terminal residues of the human CHMP4 proteins (CHMP4A-C). Crystal structures of the complexes reveal that the CHMP4 C-terminal peptides form amphipathic helices that bind across the conserved concave surface of ALIX(Bro1). ALIX-dependent HIV-1 budding is blocked by mutations in exposed ALIX(Bro1) residues that help contribute to the binding sites for three essential hydrophobic residues that are displayed on one side of the CHMP4 recognition helix (M/L/IxxLxxW). The homologous CHMP1-3 classes of ESCRT-III proteins also have C-terminal amphipathic helices, but, in those cases, the three hydrophobic residues are arrayed with L/I/MxxxLxxL spacing. Thus, the distinct patterns of hydrophobic residues provide a code that allows the different ESCRT-III subunits to bind different ESCRT pathway partners, with CHMP1-3 proteins binding MIT domain-containing proteins, such as VPS4 and Vta1/LIP5, and CHMP4 proteins binding Bro1 domain-containing proteins, such as ALIX." @default.
• W2149579871 created "2016-06-24" @default.
• W2149579871 creator A5008539422 @default.
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• W2149579871 creator A5020944188 @default.
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• W2149579871 creator A5086715753 @default.
• W2149579871 date "2008-06-03" @default.
• W2149579871 modified "2023-09-29" @default.
• W2149579871 title "ALIX-CHMP4 interactions in the human ESCRT pathway" @default.
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• W2149579871 doi "https://doi.org/10.1073/pnas.0801567105" @default.
• W2149579871 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2409388" @default.
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