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Science 28 March 1997:
Vol. 275. no. 5308, pp. 1927 - 1930
DOI: 10.1126/science.275.5308.1927
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Reports

Signaling by Phosphoinositide-3,4,5-Trisphosphate Through Proteins Containing Pleckstrin and Sec7 Homology Domains

Jes K. Klarlund, Adilson Guilherme, John J. Holik, Joseph V. Virbasius, Anil Chawla, Michael P. Czech *

Signal transmission by many cell surface receptors results in the activation of phosphoinositide (PI) 3-kinases that phosphorylate the 3' position of polyphosphoinositides. From a screen for mouse proteins that bind phosphoinositides, the protein GRP1 was identified. GRP1 binds phosphatidylinositol-3,4,5-trisphosphate [PtdIns(3,4,5)P3] through a pleckstrin homology (PH) domain and displays a region of high sequence similarity to the yeast Sec7 protein. The PH domain of the closely related protein cytohesin-1, which, through its Sec7 homology domain, regulates integrin beta 2 and catalyzes guanine nucleotide exchange of the small guanine nucleotide-binding protein ARF1, was also found to specifically bind PtdIns(3,4,5)P3. GRP1 and cytohesin-1 appear to connect receptor-activated PI 3-kinase signaling pathways with proteins that mediate biological responses such as cell adhesion and membrane trafficking.

Program in Molecular Medicine and Department of Biochemistry and Molecular Biology, University of Massachusetts Medical Center, 373 Plantation Street, Worcester, MA 01605, USA.
*   To whom correspondence should be addressed.

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J. Virol. 72, 8806-8812
   Abstract »    Full Text »    PDF »
Remodeling of the Actin Cytoskeleton Is Coordinately Regulated by Protein Kinase C and the ADP-Ribosylation Factor Nucleotide Exchange Factor ARNO.
S. R. Frank, J. C. Hatfield, and J. E. Casanova (1998)
Mol. Biol. Cell 9, 3133-3146
   Abstract »    Full Text »
Guanine Nucleotide Exchange on ADP-ribosylation Factors Catalyzed by Cytohesin-1 and Its Sec7 Domain.
G. Pacheco-Rodriguez, E. Meacci, N. Vitale, J. Moss, and M. Vaughan (1998)
J. Biol. Chem. 273, 26543-26548
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Reconstitution of Insulin Signaling Pathways in Rat 3Y1 Cells Lacking Insulin Receptor and Insulin Receptor Substrate-1. EVIDENCE THAT ACTIVATION OF Akt IS INSUFFICIENT FOR INSULIN-STIMULATED GLYCOGEN SYNTHESIS OR GLUCOSE UPTAKE IN RAT 3Y1 CELLS.
T. Imanaka, H. Hayashi, K. Kishi, L. Wang, K. Ishii, O. Hazeki, T. Katada, and Y. Ebina (1998)
J. Biol. Chem. 273, 25347-25355
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Chimeric Receptors Composed of Phosphoinositide 3-Kinase Domains and Fcgamma Receptor Ligand-binding Domains Mediate Phagocytosis in COS Fibroblasts.
M. B. Lowry, A.-M. Duchemin, K. M. Coggeshall, J. M. Robinson, and C. L. Anderson (1998)
J. Biol. Chem. 273, 24513-24520
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Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase.
M. Delcommenne, C. Tan, V. Gray, L. Rue, J. Woodgett, and S. Dedhar (1998)
PNAS 95, 11211-11216
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Phosphoinositide 3-Kinase Regulates P