rdf:type |
|
lifeskim:mentions |
umls-concept:C0332307,
umls-concept:C0599697,
umls-concept:C0871261,
umls-concept:C1155003,
umls-concept:C1514873,
umls-concept:C1546857,
umls-concept:C1556066,
umls-concept:C1619636,
umls-concept:C1704632,
umls-concept:C1706817,
umls-concept:C2698651,
umls-concept:C2911692
|
pubmed:issue |
8
|
pubmed:dateCreated |
2007-3-30
|
pubmed:abstractText |
3BP2 is a pleckstrin homology domain- and Src homology 2 (SH2) domain-containing adapter protein that is mutated in the rare human bone disorder cherubism and which has also been implicated in immunoreceptor signaling. However, a function for this protein has yet to be established. Here we show that mice lacking 3BP2 exhibited a perturbation in the peritoneal B1 and splenic marginal-zone B-cell compartments and diminished thymus-independent type 2 antigen response. 3BP2(-/-) B cells demonstrated a proliferation defect in response to antigen receptor cross-linking and a heightened sensitivity to B-cell receptor-induced death via a caspase-3-dependent apoptotic pathway. We show that 3BP2 binds via its SH2 domain to the CD19 signaling complex and is required for optimum Syk phosphorylation and calcium flux.
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17283041-10049356,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/17283041-9846481
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Apr
|
pubmed:issn |
0270-7306
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
27
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
3109-22
|
pubmed:dateRevised |
2009-11-18
|
pubmed:meshHeading |
|