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MBC in Press, published online ahead of print November 18, 2002
Mol. Biol. Cell 10.1091/mbc.E02-07-0382

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Submitted on July 5, 2002
Revised on October 1, 2002
Accepted on October 10, 2002

Integrin-mediated Tyrosine Phosphorylation of Shc in T Cells is Regulated by PKC-dependent Phosphorylations of Lck

Shi Niu1, Haichun Xie1, and Eugene E. Marcantonio1*

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

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

Integrin receptor signals are co-stimulatory for mitogenesis with the T cell receptor (TCR) 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 here that integrin signaling to Shc in T cells requires the receptor tyrosine phosphatase CD45, the Src family kinase member Lck, and Protein Kinase C (PKC). 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 co-stimulation with the TCR during lymphocyte activation.




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