| pubmed-article:17339324 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17339324 | lifeskim:mentions | umls-concept:C0913092 | lld:lifeskim |
| pubmed-article:17339324 | lifeskim:mentions | umls-concept:C1539102 | lld:lifeskim |
| pubmed-article:17339324 | lifeskim:mentions | umls-concept:C0916194 | lld:lifeskim |
| pubmed-article:17339324 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:17339324 | lifeskim:mentions | umls-concept:C2611812 | lld:lifeskim |
| pubmed-article:17339324 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:17339324 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:17339324 | lifeskim:mentions | umls-concept:C1136376 | lld:lifeskim |
| pubmed-article:17339324 | pubmed:issue | 17 | lld:pubmed |
| pubmed-article:17339324 | pubmed:dateCreated | 2007-4-23 | lld:pubmed |
| pubmed-article:17339324 | pubmed:abstractText | The two lectin receptors, CLEC-2 and Dectin-1, have been shown to signal through a Syk-dependent pathway, despite the presence of only a single YXXL in their cytosolic tails. In this study, we show that stimulation of CLEC-2 in platelets and in two mutant cell lines is dependent on the YXXL motif and on proteins that participate in signaling by immunoreceptor tyrosine-based activation motif receptors, including Src, Syk, and Tec family kinases, and on phospholipase Cgamma. Strikingly, mutation of either Src homology (SH) 2 domain of Syk blocks signaling by CLEC-2 despite the fact that it has only a single YXXL motif. Furthermore, signaling by CLEC-2 is only partially dependent on the BLNK/SLP-76 family of adapter proteins in contrast to that of immunoreceptor tyrosine-based activation motif receptors. The C-type lectin receptor, Dectin-1, which contains a YXXL motif preceded by the same four amino acids as for CLEC-2 (DEDG), signals like CLEC-2 and also requires the two SH2 domains of Syk and is only partially dependent on the BLNK/SLP-76 family of adapters. In marked contrast, the C-type lectin receptor, DC-SIGN, which has a distinct series of amino acids preceding a single YXXL, signals independent of this motif. A mutational analysis of the DEDG sequence of CLEC-2 revealed that the glycine residue directly upstream of the YXXL tyrosine is important for CLEC-2 signaling. These results demonstrate that CLEC-2 and Dectin-1 signal through a single YXXL motif that requires the tandem SH2 domains of Syk but is only partially dependent on the SLP-76/BLNK family of adapters. | lld:pubmed |
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| pubmed-article:17339324 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17339324 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17339324 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17339324 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:17339324 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17339324 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:17339324 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:17339324 | pubmed:author | pubmed-author:WatsonSteve... | lld:pubmed |
