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* Division of Cell Biology, La Jolla Institute for Allergy and Immunology, San Diego, CA 92121;
Departments of Immunology and Cell Biology, The Scripps Research Institute, La Jolla, CA 92037;
Fundación Centro Nacional de Investigaciones Cardiovasculares Carlos III, Madrid, Spain; and
Institut de Génétique Moléculaire de Montpellier, Centre National de la Recherche Scientifique, Unité Mixte de Recherche 5535, Institut Fédératif de Recherche 24, Montpellier, France.
¶ Cardiovascular Research Center, University of Virginia, Charlottesville, VA 22908
Vav1 is a 95-kDa member of the Dbl family of guanine exchange
factors and a prominent hemopoietic cell-specific protein tyrosine
kinase substrate, the involvement of which in cytoskeletal
rearrangements has been linked to its ability to activate Rho family
small GTPases. 
1 integrin ligation by fibronectin
induced Vav1 phosphorylation in peripheral blood lymphocytes and in two
different T cell lines. Vav1 overexpression led to massive T cell
spreading on 1 integrin ligands, and, conversely, two
dominant negative mutants blocked integrin-induced spreading. Vav1 and
1 integrin ligation synergistically activated Pak, but
not Rac, Cdc42, or c-Jun N-terminal kinase. In addition, Vav1
cooperated with constitutively active V12Rac mutant, but not with
V12Cdc42, to induce T cell spreading after integrin occupancy. More
importantly, a Vav1 mutant that lacked guanine exchange factor activity
still cooperated with V12Rac. In contrast, a point mutation in the SH2
domain of Vav1 abolished this synergistic effect. Therefore, our
results suggest a new regulatory effect of Vav1 in T cell spreading,
which is independent of its guanine exchange factor
activity.
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