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Vol. 14, Issue 2, 349-360, February 2003

Integrin-mediated Tyrosine Phosphorylation of Shc in T Cells Is Regulated by Protein Kinase C-dependent Phosphorylations of Lck

Shi Niu,^* Haichun Xie,^* and Eugene E. Marcantonio

Departments of Pathology and Anatomy and Cell Biology, College of Physicians and Surgeons, Columbia University, New York, New York 10032

Integrin receptor signals are costimulatory for mitogenesis with the T-cell receptor during T-cell activation. A subset of integrin receptors can link to the adapter protein Shc and provide a mitogenic stimulus. Using a combination of genetic and pharmacological approaches, we show herein that integrin signaling to Shc in T cells requires the receptor tyrosine phosphatase CD45, the Src family kinase member Lck, and protein kinase C. Our results suggest a model in which integrin-dependent serine phosphorylation of Lck is the critical step that determines the efficiency of Shc tyrosine phosphorylation in T cells. Serine phosphorylation of Lck is dependent on PKC and is also linked to CD45 dephosphorylation. Mutants of Lck that cannot be phosphorylated on the critical serine residues do not signal efficiently to Shc and have greatly reduced kinase activity. This signaling from integrins to Lck may be an important step in the costimulation with the T-cell receptor during lymphocyte activation.

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^* These authors contributed equally to this work.

Corresponding author. E-mail address: eem2{at}columbia.edu.

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Molecular Biology of the Cell
Vol. 14, 349-360, February 2003
Copyright © 2003 by The American Society for Cell Biology

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