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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2003-9-24
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pubmed:abstractText |
HIV-1 and other retroviruses exit infected cells by budding from the plasma membrane, a process requiring membrane fission. The primary late assembly (L) domain in the p6 region of HIV-1 Gag mediates the detachment of the virion by recruiting host Tsg101, a component of the class E vacuolar protein sorting (Vps) machinery. We now show that HIV Gag p6 contains a second region involved in L domain function that binds AIP1, a homolog of the yeast class E Vps protein Bro1. Further, AIP1 interacts with Tsg101 and homologs of a subunit of the yeast class E Vps protein complex ESCRT-III. AIP1 also binds to the L domain in EIAV p9, and this binding correlates perfectly with L domain function. These observations identify AIP1 as a component of the viral budding machinery, which serves to link a distinct region in the L domain of HIV-1 p6 and EIAV p9 to ESCRT-III.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/CHMP1A protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Endosomal Sorting Complexes...,
http://linkedlifedata.com/resource/pubmed/chemical/Gene Products, gag,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Tsg101 protein,
http://linkedlifedata.com/resource/pubmed/chemical/VPS4 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/actin interacting protein 1,
http://linkedlifedata.com/resource/pubmed/chemical/gag Gene Products, Human...,
http://linkedlifedata.com/resource/pubmed/chemical/p6 gag protein, Human...
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
19
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pubmed:volume |
114
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
689-99
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pubmed:dateRevised |
2009-12-18
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pubmed:meshHeading |
pubmed-meshheading:14505569-Adenosine Triphosphatases,
pubmed-meshheading:14505569-Binding Sites,
pubmed-meshheading:14505569-Cell Membrane,
pubmed-meshheading:14505569-DNA-Binding Proteins,
pubmed-meshheading:14505569-Endosomal Sorting Complexes Required for Transport,
pubmed-meshheading:14505569-Gene Products, gag,
pubmed-meshheading:14505569-HIV-1,
pubmed-meshheading:14505569-HeLa Cells,
pubmed-meshheading:14505569-Humans,
pubmed-meshheading:14505569-Infectious Anemia Virus, Equine,
pubmed-meshheading:14505569-Microfilament Proteins,
pubmed-meshheading:14505569-Microscopy, Electron,
pubmed-meshheading:14505569-Nuclear Proteins,
pubmed-meshheading:14505569-Protein Binding,
pubmed-meshheading:14505569-Protein Structure, Tertiary,
pubmed-meshheading:14505569-Recombinant Fusion Proteins,
pubmed-meshheading:14505569-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:14505569-Simian immunodeficiency virus,
pubmed-meshheading:14505569-Transcription Factors,
pubmed-meshheading:14505569-Virus Shedding,
pubmed-meshheading:14505569-gag Gene Products, Human Immunodeficiency Virus
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pubmed:year |
2003
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pubmed:articleTitle |
AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding.
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pubmed:affiliation |
Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute and Department of Pathology, Harvard Medical School, Boston, MA 02115, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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