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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
9
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pubmed:dateCreated |
2001-8-29
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pubmed:abstractText |
Cbl-b, a ring-type E3 ubiquitin protein ligase, is implicated in setting the threshold of T lymphocyte activation. The p85 regulatory subunit of phosphatidylinositol 3 kinase (PI3K) was identified as a substrate for Cbl-b. We have shown that Cbl-b negatively regulated p85 in a proteolysis-independent manner. Cbl-b is involved in the recruitment of p85 to CD28 and T cell antigen receptor zeta through its E3 ubiquitin ligase activity. The enhanced activation of Cbl-b(-/-) T cells was suppressed by the inhibition of PI3K. The results suggest a proteolysis-independent function for Cbl-b in the modification of protein recruitment.
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pubmed:grant |
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD28,
http://linkedlifedata.com/resource/pubmed/chemical/CBLB protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cblb protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-cbl,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, T-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitins,
http://linkedlifedata.com/resource/pubmed/chemical/antigen T cell receptor, zeta chain
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1529-2908
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
870-5
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:11526404-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:11526404-Animals,
pubmed-meshheading:11526404-Antigens, CD28,
pubmed-meshheading:11526404-Carrier Proteins,
pubmed-meshheading:11526404-Cells, Cultured,
pubmed-meshheading:11526404-Humans,
pubmed-meshheading:11526404-Jurkat Cells,
pubmed-meshheading:11526404-Lymphocyte Activation,
pubmed-meshheading:11526404-Membrane Proteins,
pubmed-meshheading:11526404-Mice,
pubmed-meshheading:11526404-Mice, Inbred C57BL,
pubmed-meshheading:11526404-Mice, Knockout,
pubmed-meshheading:11526404-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:11526404-Phosphoproteins,
pubmed-meshheading:11526404-Protein Transport,
pubmed-meshheading:11526404-Proto-Oncogene Proteins c-cbl,
pubmed-meshheading:11526404-Receptors, Antigen, T-Cell,
pubmed-meshheading:11526404-T-Lymphocytes,
pubmed-meshheading:11526404-Ubiquitin-Protein Ligases,
pubmed-meshheading:11526404-Ubiquitins
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pubmed:year |
2001
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pubmed:articleTitle |
Proteolysis-independent regulation of PI3K by Cbl-b-mediated ubiquitination in T cells.
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pubmed:affiliation |
Division of Cell Biology, La Jolla Institute for Allergy and Immunology, 10355 Science Center Drive, San Diego, CA 92121, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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