Linked Life Data

17140399

Source:http://linkedlifedata.com/resource/pubmed/id/17140399

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2007-1-18
pubmed:abstractText
The HIV-1 Nef protein perturbs the trafficking of membrane proteins such as CD4 by interacting with clathrin-adaptor complexes. We previously reported that Nef alters early/recycling endosomes, but its role at the plasma membrane is poorly documented. Here, we used total internal reflection fluorescence microscopy, which restricts the analysis to a approximately 100 nm region of the adherent surface of the cells, to focus on the dynamic of Nef at the plasma membrane relative to that of clathrin. Nef colocalized both with clathrin spots (CS) that remained static at the cell surface, corresponding to clathrin-coated pits (CCPs), and with approximately 50% of CS that disappeared from the cell surface, corresponding to forming clathrin-coated vesicles (CCVs). The colocalization of Nef with clathrin required the di-leucine motif essential for Nef binding to AP complexes and was independent of CD4 expression. Furthermore, analysis of Nef mutants showed that the capacity of Nef to induce internalization and downregulation of CD4 in T lymphocytes correlated with its localization into CCPs. In conclusion, this analysis shows that Nef is recruited into CCPs and into forming CCVs at the plasma membrane, in agreement with a model in which Nef uses the clathrin-mediated endocytic pathway to induce internalization of some membrane proteins from the surface of HIV-1-infected T cells.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1398-9219
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
61-76
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:17140399-Amino Acid Motifs, pubmed-meshheading:17140399-Antigens, CD4, pubmed-meshheading:17140399-Binding Sites, pubmed-meshheading:17140399-Biological Transport, Active, pubmed-meshheading:17140399-CD4-Positive T-Lymphocytes, pubmed-meshheading:17140399-Cell Membrane, pubmed-meshheading:17140399-Clathrin, pubmed-meshheading:17140399-Coated Pits, Cell-Membrane, pubmed-meshheading:17140399-Endocytosis, pubmed-meshheading:17140399-Gene Products, nef, pubmed-meshheading:17140399-Green Fluorescent Proteins, pubmed-meshheading:17140399-HIV-1, pubmed-meshheading:17140399-HeLa Cells, pubmed-meshheading:17140399-Humans, pubmed-meshheading:17140399-Microscopy, Fluorescence, pubmed-meshheading:17140399-Recombinant Fusion Proteins, pubmed-meshheading:17140399-nef Gene Products, Human Immunodeficiency Virus
pubmed:year
2007
pubmed:articleTitle
Dynamic interaction of HIV-1 Nef with the clathrin-mediated endocytic pathway at the plasma membrane.
pubmed:affiliation
Institut Cochin, Département Maladies Infectieuses, Paris F-75014, France.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural