The multidomain protein Trio binds the LAR transmembrane tyrosine phosphatase, contains a protein kinase domain, and has separate rac-specific and rho-specific guanine nucleotide exchange factor domains.

Abstract

rho-like GTP binding proteins play an essential role in regulating cell growth and actin polymerization. These molecular switches are positively regulated by guanine nucleotide exchange factors (GEFs) that promote the exchange of GDP for GTP. Using the interaction-trap assay to identify candidate proteins that bind the cytoplasmic region of the LAR… (More)

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@article{Debant1996TheMP, title={The multidomain protein Trio binds the LAR transmembrane tyrosine phosphatase, contains a protein kinase domain, and has separate rac-specific and rho-specific guanine nucleotide exchange factor domains.}, author={Anne Debant and Carles Serra-Pag{\`e}s and Katka Seipel and S. O'Brien and M. Tang and S. H. Park and Michel Streuli}, journal={Proceedings of the National Academy of Sciences of the United States of America}, year={1996}, volume={93 11}, pages={5466-71} }