PubMed:10993915 JSONTXT

{"project":"PMID_GLOBAL","denotations":[{"id":"T1","span":{"begin":0,"end":88},"obj":"Sentence"},{"id":"T2","span":{"begin":89,"end":290},"obj":"Sentence"},{"id":"T3","span":{"begin":291,"end":392},"obj":"Sentence"},{"id":"T4","span":{"begin":393,"end":541},"obj":"Sentence"},{"id":"T5","span":{"begin":542,"end":898},"obj":"Sentence"},{"id":"T6","span":{"begin":899,"end":967},"obj":"Sentence"},{"id":"T7","span":{"begin":968,"end":1235},"obj":"Sentence"}],"text":"Involvement of LAT, Gads, and Grb2 in compartmentation of SLP-76 to the plasma membrane.\nB cell linker protein (BLNK) and Src homology 2 domain-containing leukocyte protein of 76 kD (SLP-76) are adaptor proteins required for B cell receptor (BCR) and T cell receptor function, respectively. Here, we show that expression of SLP-76 cannot reconstitute BCR function in Zap-70(+)BLNK(-) B cells. This could be attributable to inability of SLP-76 to be recruited into glycolipid-enriched microdomains (GEMs) after antigen receptor cross-linking. Supporting this idea, the BCR function was restored when a membrane-associated SLP-76 chimera was enforcedly localized to GEMs. Moreover, we demonstrate that addition of both linker for activation of T cells (LAT) and Grb2-related adaptor downstream of Shc (Gads) to SLP-76 allow SLP-76 to be recruited into GEMs, whereby the BCR function is reconstituted. The Gads function was able to be replaced by overexpression of Grb2. In contrast to SLP-76, BLNK did not require Grb2 families for its recruitment to GEMs. Hence, these data suggest a functional overlap between BLNK and SLP-76, while emphasizing the difference in requirement for additional adaptor molecules in their targeting to GEMs."}