Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2005-3-14
pubmed:abstractText
We examined the function of LIP5 in mammalian cells, because the yeast homologue Vta1p was recently identified as a protein required for multivesicular body (MVB) formation. LIP5 is predominantly a cytosolic protein. Depletion of LIP5 by small inhibitory RNA (siRNA) does not affect the distribution or morphology of early endosomes, lysosomes, or Golgi but does reduce the degradation of internalized epidermal growth factor receptor (EGFR), with EGFR accumulating in intracellular vesicles. Depletion of LIP5 by siRNA also decreases human immunodeficiency virus type 1 (HIV-1) budding by 70%. We identify CHMP5 as a LIP5-binding protein and show that CHMP5 is primarily cytosolic. Depletion of CHMP5 by siRNA does not affect the distribution or morphology of early endosomes, lysosomes, or Golgi but does result in reduced degradation of the EGFR similar to silencing of LIP5. Surprisingly, CHMP5 depletion results in an increase in the release of infectious HIV-1 particles. Overexpression of CHMP5 with a large carboxyl-terminal epitope affects the distribution of both early and late endocytic compartments, whereas overexpression of LIP5 does not alter the endocytic pathway. Comparison of overexpression and siRNA phenotypes suggests that the roles of these proteins in MVB formation may be more specifically addressed using RNA interference and that both LIP5 and CHMP5 function in MVB sorting, whereas only LIP5 is required for HIV release.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
280
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10548-55
pubmed:dateRevised
2010-9-13
pubmed:meshHeading
pubmed-meshheading:15644320-Animals, pubmed-meshheading:15644320-Blotting, Western, pubmed-meshheading:15644320-COS Cells, pubmed-meshheading:15644320-Carrier Proteins, pubmed-meshheading:15644320-Cell Line, pubmed-meshheading:15644320-Cloning, Molecular, pubmed-meshheading:15644320-Cytosol, pubmed-meshheading:15644320-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:15644320-Endocytosis, pubmed-meshheading:15644320-Endosomal Sorting Complexes Required for Transport, pubmed-meshheading:15644320-Endosomes, pubmed-meshheading:15644320-Epitopes, pubmed-meshheading:15644320-Fibroblasts, pubmed-meshheading:15644320-Golgi Apparatus, pubmed-meshheading:15644320-Green Fluorescent Proteins, pubmed-meshheading:15644320-HIV-1, pubmed-meshheading:15644320-HeLa Cells, pubmed-meshheading:15644320-Humans, pubmed-meshheading:15644320-Lysosomes, pubmed-meshheading:15644320-Mass Spectrometry, pubmed-meshheading:15644320-Mice, pubmed-meshheading:15644320-Microscopy, Confocal, pubmed-meshheading:15644320-Phenotype, pubmed-meshheading:15644320-RNA, Small Interfering, pubmed-meshheading:15644320-RNA Interference, pubmed-meshheading:15644320-Time Factors, pubmed-meshheading:15644320-Transfection
pubmed:year
2005
pubmed:articleTitle
The role of LIP5 and CHMP5 in multivesicular body formation and HIV-1 budding in mammalian cells.
pubmed:affiliation
University of Utah Health Sciences Center, Department of Pathology, Salt Lake City, Utah 84132, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.