| pubmed-article:12771181 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12771181 | lifeskim:mentions | umls-concept:C0004561 | lld:lifeskim |
| pubmed-article:12771181 | lifeskim:mentions | umls-concept:C0034789 | lld:lifeskim |
| pubmed-article:12771181 | lifeskim:mentions | umls-concept:C0033681 | lld:lifeskim |
| pubmed-article:12771181 | lifeskim:mentions | umls-concept:C1514762 | lld:lifeskim |
| pubmed-article:12771181 | lifeskim:mentions | umls-concept:C1519751 | lld:lifeskim |
| pubmed-article:12771181 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:12771181 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:12771181 | pubmed:dateCreated | 2003-6-3 | lld:pubmed |
| pubmed-article:12771181 | pubmed:abstractText | Members of the Cbl family of molecular adaptors play key roles in regulating tyrosine kinase-dependent signaling in a variety of cellular systems. Here we provide evidence that in B cells Cbl-b functions as a negative regulator of B cell antigen receptor (BCR) signaling during the normal course of a response. In B cells from Cbl-b-deficient mice cross-linking the BCRs resulted in sustained phosphorylation of Igalpha, Syk, and phospholipase C (PLC)-gamma2, leading to prolonged Ca2+ mobilization, and increases in extracellular signal-regulated kinase (ERK) and c-Jun NH2-terminal protein kinase (JNK) phosphorylation and surface expression of the activation marker, CD69. Image analysis following BCR cross-linking showed sustained polarization of the BCRs into large signaling-active caps associated with phosphorylated Syk in Cbl-b-deficient B cells in contrast to the BCRs in Cbl-b-expressing B cells that rapidly proceeded to form small, condensed, signaling inactive caps. Significantly, prolonged phosphorylation of Syk correlated with reduced ubiquitination of Syk indicating that Cbl-b negatively regulates BCR signaling by targeting Syk for ubiquitination. | lld:pubmed |
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| pubmed-article:12771181 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:12771181 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12771181 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12771181 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:12771181 | pubmed:issn | 0022-1007 | lld:pubmed |
| pubmed-article:12771181 | pubmed:author | pubmed-author:GuHuaH | lld:pubmed |
| pubmed-article:12771181 | pubmed:author | pubmed-author:PierceSusan... | lld:pubmed |
| pubmed-article:12771181 | pubmed:author | pubmed-author:SohnHae WonHW | lld:pubmed |
| pubmed-article:12771181 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12771181 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:12771181 | pubmed:volume | 197 | lld:pubmed |
| pubmed-article:12771181 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12771181 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12771181 | pubmed:pagination | 1511-24 | lld:pubmed |
| pubmed-article:12771181 | pubmed:dateRevised | 2011-11-2 | lld:pubmed |
| pubmed-article:12771181 | pubmed:meshHeading | pubmed-meshheading:12771181... | lld:pubmed |
| pubmed-article:12771181 | pubmed:meshHeading | pubmed-meshheading:12771181... | lld:pubmed |
| pubmed-article:12771181 | pubmed:meshHeading | pubmed-meshheading:12771181... | lld:pubmed |
