| pubmed-article:14604964 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14604964 | lifeskim:mentions | umls-concept:C0077678 | lld:lifeskim |
| pubmed-article:14604964 | lifeskim:mentions | umls-concept:C0205160 | lld:lifeskim |
| pubmed-article:14604964 | lifeskim:mentions | umls-concept:C1155074 | lld:lifeskim |
| pubmed-article:14604964 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:14604964 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:14604964 | pubmed:dateCreated | 2004-2-20 | lld:pubmed |
| pubmed-article:14604964 | pubmed:abstractText | Aggregation of the high-affinity immunoglobulin E (IgE) receptor (FcepsilonRI) on mast cells induces a number of biochemical events, including protein-tyrosine phosphorylation leading to degranulation and multiple cytokine gene transcription. Here, we have demonstrated that a second member of the Cbl family of ubiquitin-protein ligase Cbl-b translocates into the lipid raft after FcepsilonRI engagement. Overexpression of Cbl-b in the lipid raft inhibits FcepsilonRI-mediated degranulation and cytokine gene transcription through the distinct mechanism. A point mutation of Cys373 in the RING finger domain of Cbl-b abrogates the suppression of FcepsilonRI-mediated degranulation but not cytokine gene transcription. The antigen-induced tyrosine phosphorylation of FcepsilonRI, Syk, phospholipase C-gamma (PLC-gamma), activation of c-Jun N-terminal kinase (JNK), extracellular signal regulated kinase (ERK), inhibitor of nuclear factor kappaB kinase (IKK), and Ca++ influx were all suppressed in the cells overexpressing Cbl-b in the lipid raft. In particular, the expression amount of Gab2 protein and thereby its FcepsilonRI-mediated tyrosine phosphorylation were dramatically down-regulated by ubiquitin-protein ligase activity of Cbl-b. These results suggest that Cbl-b is a negative regulator of both Lyn-Syk-LAT and Gab2mediated complementary signaling pathways in FcepsilonRI-mediated mast cell activation. | lld:pubmed |
| pubmed-article:14604964 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14604964 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14604964 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:14604964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14604964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14604964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:14604964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14604964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14604964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14604964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14604964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14604964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14604964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14604964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14604964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14604964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14604964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14604964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14604964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14604964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14604964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14604964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14604964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14604964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14604964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14604964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14604964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14604964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14604964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14604964 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14604964 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14604964 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:14604964 | pubmed:issn | 0006-4971 | lld:pubmed |
| pubmed-article:14604964 | pubmed:author | pubmed-author:YamamuraHiroh... | lld:pubmed |
| pubmed-article:14604964 | pubmed:author | pubmed-author:SadaKiyonaoK | lld:pubmed |
| pubmed-article:14604964 | pubmed:author | pubmed-author:MiahS M... | lld:pubmed |
| pubmed-article:14604964 | pubmed:author | pubmed-author:MaenoKoichiro... | lld:pubmed |
| pubmed-article:14604964 | pubmed:author | pubmed-author:KyoShinkouS | lld:pubmed |
| pubmed-article:14604964 | pubmed:author | pubmed-author:QuXiujuanX | lld:pubmed |
| pubmed-article:14604964 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14604964 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:14604964 | pubmed:volume | 103 | lld:pubmed |
| pubmed-article:14604964 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14604964 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14604964 | pubmed:pagination | 1779-86 | lld:pubmed |
| pubmed-article:14604964 | pubmed:dateRevised | 2011-11-2 | lld:pubmed |
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| pubmed-article:14604964 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:14604964 | pubmed:articleTitle | Negative regulation of FcepsilonRI-mediated mast cell activation by a ubiquitin-protein ligase Cbl-b. | lld:pubmed |
| pubmed-article:14604964 | pubmed:affiliation | Division of Proteomics, Department of Genome Sciences, Kobe University Graduate School of Medicine, Kobe, Japan. | lld:pubmed |
| pubmed-article:14604964 | pubmed:publicationType | Journal Article | lld:pubmed |
