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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2004-7-15
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pubmed:abstractText |
Lipid rafts are detergent-insoluble membrane domains that play a key role in signal transduction by the T-cell antigen receptor. Proteome analysis revealed the presence of amidosulfobetaine-soluble signal transducing, integral membrane, cytoskeletal, heat shock, and GTP-binding proteins in rafts prepared from Jurkat cells. Several of these proteins were recruited to rafts by CD3/CD28 costimulation. Of particular interest is the inducible association of activated IkappaB kinase complexes with raft vesicles that could be captured with anti-flotillin-1 antibodies. Following amidosulfobetaine solubilization, flotillin-beta and IKKbeta underwent reciprocal co-immunoprecipitation. Treatment of Jurkat cells with methyl-beta-cyclodextrin disrupted the assembly and activation of this raft complex and also interfered in CD3/ CD28-induced activation of a NF-kappaB response element in the IL-2 promoter.
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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/Antigens, CD28,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD3,
http://linkedlifedata.com/resource/pubmed/chemical/CHUK protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/I-kappa B Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/IKBKB protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/IKBKE protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-2,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteome,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Cyclodextrins,
http://linkedlifedata.com/resource/pubmed/chemical/flotillins,
http://linkedlifedata.com/resource/pubmed/chemical/methyl-beta-cyclodextrin
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pubmed:status |
MEDLINE
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pubmed:issn |
1535-3893
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
445-54
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:15253425-Antigens, CD28,
pubmed-meshheading:15253425-Antigens, CD3,
pubmed-meshheading:15253425-Cell Membrane,
pubmed-meshheading:15253425-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:15253425-Humans,
pubmed-meshheading:15253425-I-kappa B Kinase,
pubmed-meshheading:15253425-Immunoprecipitation,
pubmed-meshheading:15253425-Interleukin-2,
pubmed-meshheading:15253425-Jurkat Cells,
pubmed-meshheading:15253425-Membrane Microdomains,
pubmed-meshheading:15253425-Membrane Proteins,
pubmed-meshheading:15253425-Promoter Regions, Genetic,
pubmed-meshheading:15253425-Protein-Serine-Threonine Kinases,
pubmed-meshheading:15253425-Proteome,
pubmed-meshheading:15253425-Signal Transduction,
pubmed-meshheading:15253425-beta-Cyclodextrins
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pubmed:articleTitle |
Proteome analysis of lipid rafts in Jurkat cells characterizes a raft subset that is involved in NF-kappaB activation.
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pubmed:affiliation |
Division of Clinical Immunology and Allergy, Department of Medicine, The Pasarow Mass Spectrometry Laboratory, University of California, Los Angeles, California 90095, USA.
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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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