Hem C D, Ekornhol M, Granum S, Sundvold-Gjerstad V, Spurkland A
Department of Molecular Medicine, Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway.
Scand J Immunol. 2017 Feb;85(2):104-112. doi: 10.1111/sji.12513.
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) and linker of activated T cells (LAT) pTyr , pTyr and pTyr .
T细胞特异性衔接蛋白（TSAd）含有多个蛋白质相互作用结构域，正逐渐成为T细胞活化的调节因子。TSAd富含脯氨酸区域和磷酸酪氨酸的几个相互作用伙伴已被确定，包括Src和Tec家族激酶淋巴细胞特异性蛋白酪氨酸激酶和白细胞介素2诱导型T细胞激酶。因此，TSAd可能通过其Src同源2（SH2）结构域，作为这些酶与其他信号分子之间的连接物发挥作用。然而，目前已知的T细胞中与TSAd SH2结构域结合的伙伴很少。通过计算机配体预测、肽点阵列、下拉和免疫沉淀实验，我们在此报告TSAd SH2结构域与CD6磷酸酪氨酸（pTyr）以及活化T细胞连接蛋白（LAT）的pTyr、pTyr和pTyr之间的新相互作用。
