The Journal of Experimental Medicine
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Published online 30 January 2006 doi:10.1084/jem.20051637
Rockefeller University Press, 0022-1007 $8.00
JEM, Volume 203, Number 2, 281-287
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BRIEF DEFINITIVE REPORT

 Essential role of the T cell–specific adapter protein in the activation of LCK in peripheral T cells

Francesc Marti1, Gonzalo G. Garcia2, Philip E. Lapinski1, Jennifer N. MacGregor1, and Philip D. King1

1 Department of Microbiology and Immunology and 2 Department of Pathology, University of Michigan Medical School, Ann Arbor, MI 48109

CORRESPONDENCE Philip D. King: kingp{at}umich.edu

T cell–specific adapter protein (TSAd) is a SRC-homology-2 (SH2) domain–containing intracellular signaling molecule that is required for T cell antigen receptor (TCR)–induced cytokine synthesis in T cells. How TSAd functions in TCR signal transduction is not clear. Previous work has suggested a nuclear role for this adapter. However, other evidence suggests that TSAd also functions in the cytoplasm. Using T cells from TSAd-deficient mice, we now show that the major role of TSAd in the cytoplasm is in activation of the LCK protein tyrosine kinase at the outset of TCR signal transduction. Consequently, TSAd regulates several downstream signaling events, including intracellular calcium mobilization and activation of the Ras–extracellular signal–regulated kinase signaling pathway. TSAd regulates LCK activity directly through physical interaction with LCK SH3 and SH2 domains. These studies reveal TSAd as a positive regulator of proximal TCR signal transduction and provide important new information on the mechanism of TCR-induced LCK activation.


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