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Originally published online as doi:10.1189/jlb.0208084 on July 23, 2008

Published online before print July 23, 2008
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(Journal of Leukocyte Biology. 2008;84:1192-1201.)
© 2008 by Society for Leukocyte Biology

Critical role of Lck in L-selectin signaling induced by sulfatides engagement

Ting Xu, Liang Chen, Xin Shang, Lingling Cui, Jixian Luo, Cuixia Chen, Xueqing Ba and Xianlu Zeng1

Institute of Genetics and Cytology, Northeast Normal University, Changchun, P. R. China

1 Correspondence: Institute of Genetics and Cytology, Northeast Normal University, Renmin Street 5268, Changchun, P.R. China. E-mail: zengx779{at}nenu.edu.cn

Recruitment of leukocytes onto inflamed tissues is an important physiological event, in which L-selectin plays an essential role in initial leukocyte capture and at the same time, triggers cell signaling. Lck is a member of the Src family of protein tyrosine kinases and is critical for T cell activation triggered by receptor ligation. Here, we demonstrated that Lck was associated directly with and phosphorylated the L-selectin cytoplasmic tail upon L-selectin engagement with sulfatides. Through the direct interaction with ZAP-70 and c-Abl via its Src homology 2 (SH2) and SH3 domains, Lck organized a signaling complex at the cytoplasmic tail of L-selectin. In the cells with Lck knockdown by small interfering RNA treatment, L-selectin signaling was suppressed dramatically, as indicated by reduced phosphorylation of c-Abl and ZAP-70. Re-expression of wild-type or constitutively active but not kinase-dead murine Lck rescued the phosphorylation completely, but the SH2 domain mutant or the SH3/SH2 double mutant of murine Lck had no effect. These results suggest that Lck plays a critical role in L-selectin signaling upon sulfatides stimulation.

Key Words: c-Abl kinase • ZAP-70 kinase • siRNA




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