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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
32
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pubmed:dateCreated |
2001-8-6
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pubmed:abstractText |
Tumor necrosis factor (TNF)-related activation-induced cytokine (TRANCE) is a TNF family member essential for osteoclast differentiation, and it induces the activation and survival of osteoclasts and mature dendritic cells. We recently demonstrated that TRANCE activates Akt via a mechanism involving TRANCE receptor (TRANCE-R)/RANK, TRAF6, and c-Src. Here, we show that TRANCE-R and CD40 recruit TRAF6, Cbl family-scaffolding proteins, and the phospholipid kinase phosphatidylinositol 3-kinase in a ligand-dependent manner. The recruitment of Cbl-b and c-Cbl to TRANCE-R is dependent upon the activity of Src-family kinases. TRANCE and CD40L-mediated Akt activation is defective in Cbl-b -/- dendritic cells, and CD40L-mediated Akt activation is defective in c-Cbl -/- B cells. These findings implicate Cbl family proteins as not only negative regulators of signaling but as positive modulators of TNF receptor superfamily signaling as well.
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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/AKT1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Adaptor Proteins, Signal Transducing,
http://linkedlifedata.com/resource/pubmed/chemical/CBL protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CBLB protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/CD40 Ligand,
http://linkedlifedata.com/resource/pubmed/chemical/CSK tyrosine-protein kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cbl protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Cblb protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositol 3-Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Tyrosine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-akt,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-cbl,
http://linkedlifedata.com/resource/pubmed/chemical/RANK Ligand,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor Activator of Nuclear...,
http://linkedlifedata.com/resource/pubmed/chemical/TNFRSF11A protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/TNFSF11 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Tnfrsf11a protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Tnfsf11 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
30011-7
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pubmed:dateRevised |
2011-11-2
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pubmed:meshHeading |
pubmed-meshheading:11406619-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:11406619-Amino Acid Sequence,
pubmed-meshheading:11406619-Animals,
pubmed-meshheading:11406619-CD40 Ligand,
pubmed-meshheading:11406619-Carrier Proteins,
pubmed-meshheading:11406619-Cell Line,
pubmed-meshheading:11406619-Cell Survival,
pubmed-meshheading:11406619-Cells, Cultured,
pubmed-meshheading:11406619-Dendritic Cells,
pubmed-meshheading:11406619-Enzyme Activation,
pubmed-meshheading:11406619-Humans,
pubmed-meshheading:11406619-Kinetics,
pubmed-meshheading:11406619-Ligands,
pubmed-meshheading:11406619-Membrane Glycoproteins,
pubmed-meshheading:11406619-Mice,
pubmed-meshheading:11406619-Models, Biological,
pubmed-meshheading:11406619-Molecular Sequence Data,
pubmed-meshheading:11406619-Osteoclasts,
pubmed-meshheading:11406619-Phosphatidylinositol 3-Kinases,
pubmed-meshheading:11406619-Phosphoproteins,
pubmed-meshheading:11406619-Phosphorylation,
pubmed-meshheading:11406619-Plasmids,
pubmed-meshheading:11406619-Precipitin Tests,
pubmed-meshheading:11406619-Protein Binding,
pubmed-meshheading:11406619-Protein-Serine-Threonine Kinases,
pubmed-meshheading:11406619-Protein-Tyrosine Kinases,
pubmed-meshheading:11406619-Proto-Oncogene Proteins,
pubmed-meshheading:11406619-Proto-Oncogene Proteins c-akt,
pubmed-meshheading:11406619-Proto-Oncogene Proteins c-cbl,
pubmed-meshheading:11406619-RANK Ligand,
pubmed-meshheading:11406619-Receptor Activator of Nuclear Factor-kappa B,
pubmed-meshheading:11406619-Sequence Homology, Amino Acid,
pubmed-meshheading:11406619-Signal Transduction,
pubmed-meshheading:11406619-Transfection,
pubmed-meshheading:11406619-Ubiquitin-Protein Ligases
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pubmed:year |
2001
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pubmed:articleTitle |
A positive regulatory role for Cbl family proteins in tumor necrosis factor-related activation-induced cytokine (trance) and CD40L-mediated Akt activation.
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pubmed:affiliation |
Laboratory of Immunology and Howard Hughes Medical Institute, The Rockefeller University, New York, New York 10021, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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