Regulation of GRP1-catalyzed ADP ribosylation factor guanine nucleotide exchange by phosphatidylinositol 3,4,5-trisphosphate.

Abstract

Cellular levels of phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) are rapidly elevated in response to activation of growth factor receptor tyrosine kinases. This polyphosphoinositide binds the pleckstrin homology (PH) domain of GRP1, a protein that also contains 200 residues with high sequence similarity to a segment of the yeast Sec7 protein… (More)

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@article{Klarlund1998RegulationOG, title={Regulation of GRP1-catalyzed ADP ribosylation factor guanine nucleotide exchange by phosphatidylinositol 3,4,5-trisphosphate.}, author={Jes K. Klarlund and Lucia E. Rameh and Lewis C. Cantley and Jane Buxton and John Holik and C Sakelis and Vrishali Patki and Silvia Corvera and M. P. Czech}, journal={The Journal of biological chemistry}, year={1998}, volume={273 4}, pages={1859-62} }