| pubmed-article:17110436 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17110436 | lifeskim:mentions | umls-concept:C0034789 | lld:lifeskim |
| pubmed-article:17110436 | lifeskim:mentions | umls-concept:C0441889 | lld:lifeskim |
| pubmed-article:17110436 | lifeskim:mentions | umls-concept:C1135629 | lld:lifeskim |
| pubmed-article:17110436 | lifeskim:mentions | umls-concept:C1420083 | lld:lifeskim |
| pubmed-article:17110436 | lifeskim:mentions | umls-concept:C1424461 | lld:lifeskim |
| pubmed-article:17110436 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:17110436 | pubmed:issue | 48 | lld:pubmed |
| pubmed-article:17110436 | pubmed:dateCreated | 2006-11-29 | lld:pubmed |
| pubmed-article:17110436 | pubmed:abstractText | Src-like adaptor protein (SLAP) and c-Cbl recently have been shown to cooperate in regulating T cell receptor (TCR) levels in developing T cells. SLAP also is expressed in developing B cells, and its deficiency leads to alterations in B cell receptor (BCR) levels and B cell development. Hence, we hypothesized that SLAP and c-Cbl may cooperate during B cell development to regulate BCR levels. In mice deficient in both SLAP and c-Cbl, we found that B cell development is altered, suggesting that they function through intersecting pathways. To study the mechanism by which SLAP and c-Cbl alter BCR levels, we coexpressed them in a mature mouse B cell line (Bal-17). First we determined that SLAP associates with proximal components of the BCR complex after stimulation and internalization. Coexpression of SLAP and c-Cbl in Bal-17 led to decreased surface and total BCR levels. This decrease in BCR levels depended on intact Src homology 2 (SH2) and C-terminal domains of SLAP. In addition, a mutation in the SH2 domain of SLAP blocked its colocalization with c-Cbl and the BCR complex, whereas deletion of the C terminus did not affect its localization. Last, coexpression of SLAP and c-Cbl altered BCR complex recycling. This alteration in BCR complex recycling depended on enzymatically active c-Cbl and Src family kinases, as well as the intact SH2 and C-terminal domains of SLAP. These data suggest that SLAP has a conserved function in B and T cells by adapting c-Cbl to the antigen-receptor complex and targeting it for degradation. | lld:pubmed |
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| pubmed-article:17110436 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:17110436 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:17110436 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17110436 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:17110436 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:17110436 | pubmed:author | pubmed-author:WeissArthurA | lld:pubmed |
| pubmed-article:17110436 | pubmed:author | pubmed-author:GuHuaH | lld:pubmed |
| pubmed-article:17110436 | pubmed:author | pubmed-author:MyersMargaret... | lld:pubmed |
| pubmed-article:17110436 | pubmed:author | pubmed-author:DragoneLeonar... | lld:pubmed |
| pubmed-article:17110436 | pubmed:author | pubmed-author:SosinowskiTom... | lld:pubmed |
| pubmed-article:17110436 | pubmed:author | pubmed-author:WhiteCarmenC | lld:pubmed |
| pubmed-article:17110436 | pubmed:author | pubmed-author:GadwalShyamS | lld:pubmed |
| pubmed-article:17110436 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17110436 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:17110436 | pubmed:volume | 103 | lld:pubmed |
| pubmed-article:17110436 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17110436 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17110436 | pubmed:pagination | 18202-7 | lld:pubmed |
| pubmed-article:17110436 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:17110436 | pubmed:meshHeading | pubmed-meshheading:17110436... | lld:pubmed |
| pubmed-article:17110436 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:17110436 | pubmed:articleTitle | Src-like adaptor protein (SLAP) regulates B cell receptor levels in a c-Cbl-dependent manner. | lld:pubmed |
| pubmed-article:17110436 | pubmed:affiliation | Division of Pediatric Immunology/Rheumatology, Department of Pediatrics, University of California, San Francisco, CA 94143, USA. | lld:pubmed |
| pubmed-article:17110436 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17110436 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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