rdf:type |
|
lifeskim:mentions |
umls-concept:C0004083,
umls-concept:C0019704,
umls-concept:C0085828,
umls-concept:C0205250,
umls-concept:C1422036,
umls-concept:C1511545,
umls-concept:C1511625,
umls-concept:C1514562,
umls-concept:C1707271,
umls-concept:C1749488,
umls-concept:C1947976,
umls-concept:C2346841
|
pubmed:issue |
6
|
pubmed:dateCreated |
2001-3-6
|
pubmed:abstractText |
Short amino acid sequences in the cytosolic domains of transmembrane proteins are recognized by specialized adaptor [corrected] proteins which are part of coated vesicles utilized to transport membrane proteins between the trans-Golgi network (TGN) and the plasma membrane (forward and backward). Previously, we and others reported that the membrane-proximal tyrosine residues Y712 (human immunodeficiency virus [HIV]) and Y721 (simian immunodeficiency virus [SIV]) in the envelope glycoprotein (Env) of the primate lentiviruses are crucial for the association of Env with clathrin-associated adaptor [corrected] complex AP-2. The same tyrosine-based endocytosis motifs in the cytosolic domains (EnvCD) of transmembrane gp41 of HIV type 1 (HIV-1) and SIV, respectively, were also shown to modulate the interaction with TGN- and endosome-based clathrin-associated complex AP-1. Our findings suggested that EnvCD binding to AP-1, unlike the association of EnvCD with AP-2, is dependent largely on residues other than Y712 and Y721. Here, we tested if motifs downstream of Y712 affect HIV-1 EnvCD-AP-1 binding and Env trafficking. Mutational analysis revealed that the C-terminal leucine-based motif in Env was crucial for the recruitment of AP-1 in vitro and in Env-expressing cells. In addition to affecting Env-AP-1 association, mutations at the C terminus of Env also altered the subcellular localization of Env, suggesting that proper post-Golgi routing of Env depends on its recruitment of AP-1. Finally, the C-terminal dileucine was shown to assist the membrane-proximal Y712 motif in restricting the cell surface expression of Env.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11222723,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11222723-10075724,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11222723-10233963,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11222723-10338135,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11222723-10352010,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11222723-10472183,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/11222723-10535737,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11222723-10747937,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/11222723-11208139,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/11222723-9890983
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pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
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pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
0022-538X
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pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
75
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
2982-92
|
pubmed:dateRevised |
2009-11-18
|
pubmed:meshHeading |
pubmed-meshheading:11222723-Adaptor Protein Complex delta Subunits,
pubmed-meshheading:11222723-Amino Acid Motifs,
pubmed-meshheading:11222723-Amino Acid Sequence,
pubmed-meshheading:11222723-Gene Expression Regulation, Viral,
pubmed-meshheading:11222723-Gene Products, env,
pubmed-meshheading:11222723-Genes, env,
pubmed-meshheading:11222723-HIV-1,
pubmed-meshheading:11222723-HeLa Cells,
pubmed-meshheading:11222723-Humans,
pubmed-meshheading:11222723-Leucine,
pubmed-meshheading:11222723-Membrane Proteins,
pubmed-meshheading:11222723-Molecular Sequence Data,
pubmed-meshheading:11222723-Mutation,
pubmed-meshheading:11222723-Signal Transduction,
pubmed-meshheading:11222723-Subcellular Fractions,
pubmed-meshheading:11222723-Transfection
|
pubmed:year |
2001
|
pubmed:articleTitle |
The highly conserved C-terminal dileucine motif in the cytosolic domain of the human immunodeficiency virus type 1 envelope glycoprotein is critical for its association with the AP-1 clathrin adaptor [correction of adapter].
|
pubmed:affiliation |
Institute of Microbiology, University of Lausanne, CH-1011 Lausanne, Switzerland.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|