| Literature DB >> 27896837 |
C D Hem1, M Ekornhol1, S Granum1, V Sundvold-Gjerstad1, A Spurkland1.
Abstract
The T cell-specific adaptor protein (TSAd) contains several protein interaction domains, and is merging as a modulator of T cell activation. Several interaction partners for the TSAd proline-rich region and phosphotyrosines have been identified, including the Src and Tec family kinases lymphocyte-specific protein tyrosine kinase and interleukin 2-inducible T cell kinase. Via its Src homology 2 (SH2) domain, TSAd may thus function as a link between these enzymes and other signalling molecules. However, few binding partners to the TSAd SH2 domain in T cells are hitherto known. Through the use of in silico ligand prediction, peptide spot arrays, pull-down and immunoprecipitation experiments, we here report novel interactions between the TSAd SH2 domain and CD6 phosphotyrosine (pTyr)629 and linker of activated T cells (LAT) pTyr171 , pTyr191 and pTyr226 .Entities:
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Year: 2017 PMID: 27896837 DOI: 10.1111/sji.12513
Source DB: PubMed Journal: Scand J Immunol ISSN: 0300-9475 Impact factor: 3.487