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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
16
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pubmed:dateCreated |
1992-9-15
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pubmed:abstractText |
CD4 is a cell surface glycoprotein expressed by a subset of T lymphocytes and functions to enhance T-cell activation. CD4 is noncovalently associated via the cytoplasmic domain with the protein-tyrosine kinase p56lck, a member of the src protein-tyrosine kinase family. Upon activation of protein kinase C by phorbol ester, CD4 is phosphorylated on cytoplasmic serine residues and internalized from the cell surface, and disruption of the CD4-p56lck complex occurs. The exact relationship between these events is likely to be functionally significant, as cytoplasmic-domain serine phosphorylation and internalization have been shown to regulate the function of receptors that possess intrinsic protein-tyrosine kinase activity. Here we demonstrate that p56lck slows the rate of phorbol 12-myristate 13-acetate-induced internalization of CD4 in a manner that depends on a physical association between p56lck and CD4. This decreased rate is due at least in part to a requirement for disruption of the CD4-p56lck complex prior to internalization of CD4. Furthermore, disruption of the CD4-p56lck complex appears to depend on the integrity of the cytoplasmic-domain serine at position 408, probably due to a requirement for phosphorylation.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-1373141,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-1532002,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-1671341,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-1674746,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-1850281,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-1900077,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-2105883,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-2107025,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-2109184,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-2158859,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-2204623,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-2344614,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-2369920,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-2455897,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-2582490,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-2722808,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-2783435,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-2783943,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-2784463,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-2787934,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-2790960,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-2823150,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-2946683,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-2957374,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-2961801,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-3037388,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-3081813,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-3100638,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-3116077,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-3259970,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-3262426,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-3312193,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-3316198,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-3498122,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1502168-3499230
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
89
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7566-70
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pubmed:dateRevised |
2010-9-7
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pubmed:meshHeading |
pubmed-meshheading:1502168-Antigens, CD,
pubmed-meshheading:1502168-Antigens, CD4,
pubmed-meshheading:1502168-Antigens, CD8,
pubmed-meshheading:1502168-Cell Membrane,
pubmed-meshheading:1502168-Cloning, Molecular,
pubmed-meshheading:1502168-Fluorescent Antibody Technique,
pubmed-meshheading:1502168-HeLa Cells,
pubmed-meshheading:1502168-Humans,
pubmed-meshheading:1502168-Kinetics,
pubmed-meshheading:1502168-Lymphocyte Specific Protein Tyrosine Kinase p56(lck),
pubmed-meshheading:1502168-Lymphocytes,
pubmed-meshheading:1502168-Plasmids,
pubmed-meshheading:1502168-Protein-Tyrosine Kinases,
pubmed-meshheading:1502168-Tetradecanoylphorbol Acetate
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pubmed:year |
1992
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pubmed:articleTitle |
Disruption of the CD4-p56lck complex is required for rapid internalization of CD4.
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pubmed:affiliation |
Division of Pediatric Oncology, Dana-Farber Cancer Institute, Boston, Ma.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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