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Science 7 May 1993:
Vol. 260. no. 5109, pp. 822 - 825
DOI: 10.1126/science.8484124
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Articles

Science, Vol 260, Issue 5109, 822-825
Copyright © 1993 by American Association for the Advancement of Science

articles

Tyrosine kinase-stimulated guanine nucleotide exchange activity of Vav in T cell activation

E Gulbins, KM Coggeshall, G Baier, S Katzav, P Burn, and A Altman

Division of Cell Biology, La Jolla Institute for Allergy and Immunology, CA 92037.

The hematopoietically expressed product of the vav proto-oncogene, Vav, shared homology with guanine nucleotide releasing factors (GRFs) [also called guanosine diphosphate-dissociation stimulators (GDSs)] that activate Ras-related small guanosine triphosphate (GTP)-binding proteins. Human T cell lysates or Vav immunoprecipitates possessed GRF activity that increased after T cell antigen receptor (TCR)-CD3 triggering; an in vitro-translated Vav fragment that contained the putative GRF domain was also active. Vav-associated GRF stimulation after TCR-CD3 ligation paralleled its tyrosine phosphorylation; both were blocked by a protein tyrosine kinase (PTK) inhibitor. Vav also was a substrate for the p56lck PTK. Thus, Vav is a PTK-regulated GRF that may be important in TCR-CD3-initiated signal transduction through the activation of Ras.


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