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

Journal of leukocyte biology (2008-07-26)
Ting Xu, Liang Chen, Xin Shang, Lingling Cui, Jixian Luo, Cuixia Chen, Xueqing Ba, Xianlu Zeng
ABSTRACT

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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Anti-Glutathione-S-Transferase (GST) antibody produced in rabbit, IgG fraction of antiserum, buffered aqueous solution
Sigma-Aldrich
Phalloidin, Fluorescein Isothiocyanate Labeled, sequence Amanita phalloides(synthetic: peptide sequence)