Linked Life Data

21394086

Source:http://linkedlifedata.com/resource/pubmed/id/21394086

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2011-4-4
pubmed:abstractText
HIV (human immunodeficiency virus) diverts the cellular ESCRT (endosomal sorting complex required for transport) machinery to promote virion release from infected cells. The ESCRT consists of four heteromeric complexes (ESCRT-0 to ESCRT-III), which mediate different membrane abscission processes, most importantly formation of intralumenal vesicles at multivesicular bodies. The ATPase VPS4 (vacuolar protein sorting 4) acts at a late stage of ESCRT function, providing energy for ESCRT dissociation. Recruitment of ESCRT by late-domain motifs in the viral Gag polyprotein and a role of ESCRT in HIV release are firmly established, but the order of events, their kinetics and the mechanism of action of individual ESCRT components in HIV budding are unclear at present. Using live-cell imaging, we show late-domain-dependent recruitment of VPS4A to nascent HIV particles at the host cell plasma membrane. Recruitment of VPS4A was transient, resulting in a single or a few bursts of at least two to five VPS4 dodecamers assembling at HIV budding sites. Bursts lasted for ?35 s and appeared with variable delay before particle release. These results indicate that VPS4A has a direct role in membrane scission leading to HIV-1 release.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1476-4679
pubmed:author
pubmed:copyrightInfo
© 2011 Macmillan Publishers Limited. All rights reserved
pubmed:issnType
Electronic
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
469-74
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Live-cell visualization of dynamics of HIV budding site interactions with an ESCRT component.
pubmed:affiliation
Physical Chemistry, Department of Chemistry and Biochemistry, Munich Center for Integrated Protein Science (CiPSM) and Center for NanoScience, Ludwig-Maximilians-Universität München, Butenandtstrasse 11, 81377 Munich, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't