Vav, a GDP/GTP nucleotide exchange factor, interacts with GDIs, proteins that inhibit GDP/GTP dissociation.

Vav functions as a specific GDP/GTP nucleotide exchange factor which is regulated by tyrosine phosphorylation in the hematopoietic system. Loss of the amino-terminus sequences of Vav was sufficient to control its transforming potential and its function in T cells. We report here the identification of the hematopoietic GDP dissociation inhibitor ...
protein, Ly-GDI, as a protein that interacts with the amino-terminus of Vav. Further analysis confirmed that Vav and Ly-GDI interact both in in vitro and in in vivo assays. This association is maximal only when the amino region of Vav is intact and requires an intact carboxy-terminus of Ly-GDI. The interaction between Vav and Ly-GDI is not dependent on the tyrosine phosphorylation status of Vav. In addition, Rho-GDI, the highly homologous protein to Ly-GDI, associates with Vav as well. The contribution of the interaction between Vav and GDIs, proteins that are involved in the GDP/GTP exchange processes, to the biological function of Vav is further discussed.
Mesh Terms:
Animals, Cell Cycle Proteins, Cell Line, Guanine Nucleotide Dissociation Inhibitors, Guanosine Diphosphate, Guanosine Triphosphate, Humans, Mice, Molecular Weight, Muromonab-CD3, Phosphorylation, Phosphotyrosine, Precipitin Tests, Protein Binding, Proteins, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-vav, Receptors, Antigen, T-Cell, Recombinant Fusion Proteins, Sequence Deletion, T-Lymphocytes, Transfection, Tumor Suppressor Proteins, Two-Hybrid System Techniques
FEBS Lett.
Date: Feb. 04, 2000
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