GAIP and RGS4 are GTPase-activating proteins for the G(i) subfamily of G protein α subunits

Cell

Volumn 86, Issue 3, 1996, Pages 445-452

  Berman, David M ^a   Wilkie, Thomas M ^a   Gilman, Alfred G ^a  

^a UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; GUANOSINE TRIPHOSPHATE;

ARTICLE; BINDING SITE; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME SPECIFICITY; HYDROLYSIS; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN PROTEIN INTERACTION; REGULATORY MECHANISM; SIGNAL TRANSDUCTION;

EID: 0030576518     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80117-8     Document Type: Article

References (49)

1. Adari, H., Lowy, D.R., Willumsen, B.M., Der, C.J., and McCormick, F. (1988). Guanosine triphosphatase activating protein (GAP) interacts with the p21 ras effector binding domain. Science 240, 518-521.
2. Angleson, J.K., and Wensel, T.G. (1993). A GTPase-accelerating factor for transducin, distinct from its effector cGMP phosphodiesterase, in rod outer segment membranes. Neuron 11, 939-949.
3. Arshavsky, V.Y., and Bownds, M.D. (1992). Regulation of deactivation of photoreceptor G protein by its target enzyme and cGMP. Nature 357, 416-417.
4. Arshavsky, V.Y., Dumke, C.L., Zhu, Y., Artemyev, N.O., Skiba, N.P., Hamm, H.E., and Bownds, M.D. (1994). Regulation of transducin GTPase activity in bovine rod outer segments. J. Biol. Chem. 269, 19882-19887.
5. Berstein, G., Blank, J.L., Jhon, D.Y., Exton, J.H., Rhee, S.G., and Ross, E.M. (1992). Phospholipase C-β1 is a GTPase-activating protein for Gq/11, its physiologic regulator. Cell 70, 411-418.
6. q and m1 muscarinic cholinergic receptor. J. Biol. Chem. 271, 7999-8007.
7. Cassel, D., and Selinger, Z. (1977). Mechanism of adenylate cyclase activation by cholera toxin: an inhibition of GTP hydrolysis at the regulatory site. Proc. Natl. Acad. Sci. USA 74, 3307-3311.
8. Chan, R.K., and Otte, C.A. (1982a). Isolation and genetic analysis of Saccharomyces cerevisiae mutants supersensitive to G1 arrest by a factor and α factor pheromones. Mol. Cell. Biol. 2, 11-20.
9. Chan, R.K., and Otte, C.A. (1982b). Physiological characterization of Saccharomyces cerevisiae mutants supersensitive to G1 arrest by a factor and α factor pheromones. Mol. Cell. Biol. 2, 21-29.
10. iα1 and the mechanism of GTP hydrolysis. Science 265, 1405-1412.
11. αi3, is a member of a protein family with a highly conserved core domain. Proc. Natl. Acad. Sci. USA 92, 11916-11920.
12. H genes mutated at codon 61. Cell 44, 167-176.
13. Dietzel, C., and Kurjan, J. (1987). Pheromonal regulation and sequence of the Saccharomyces cerevisiae SST2 gene: a model for desensitization to pheromone. Mol. Cell. Biol. 7, 4169-4177.
14. Dohlman, H.G., Apaniesk, D., Chen, Y., Song, J.P., and Nusskern, D. (1995). Inhibition of G protein signaling by dominant gain-of-function mutations in SST2P, a pheromone desensitization factor in Saccharomyces cerevisiae. Mol. Cell. Biol. 15, 3635-3643.
15. Druey, K.M., Blumer, K.J., Kang, V.H., and Kehri, J.H. (1996). Inhibition of a G protein-mediated MAP kinase activation by a new mammalian gene family. Nature 379, 742-746.
16. Feig, L.A., and Cooper, G.M. (1988). Inhibition of NIH 3T3 cell proliferation by a mutant ras protein with preferential affinity for GDP. Mol. Cell. Biol. 8, 3235-3243.
17. rho GTPase-activating protein, rho GAP. Biochem. J. 276, 833-836.
18. Gideon, P., John, J., Frech, M., Lautwein, A., Clark, R., Scheffler, J.E., and Wittinghofer, A. (1992). Mutational and kinetic analyses of the GTPase-activating protein (GAP)-p21 interaction: the C-terminal domain of GAP is not sufficient for full activity. Mol. Cell. Biol. 12, 2050-2056.
19. Gilman, A.G. (1987). G proteins: transducers of receptor-generated signals. Annu. Rev. Biochem. 56, 615-649.
20. sα. J. Biol. Chem. 264, 15475-15482.
21. Hamm, H.E., and Gilchrist, A. (1996). Heterotrimeric G proteins. Curr. Opin. Cell Biol. 8, 189-196.
22. o. J. Biol. Chem. 262, 757-761.
23. Hong, J.X., Wilson, G.L., Fox, C.H., and Kehrl, J.H. (1993). Isolation and characterization of a novel B cell activation gene. J. Immunol. 150, 3895-3904.
24. Kaziro, Y. (1978). The role of guanosine 5′-triphosphate in polypeptide chain elongation. Biochim. Biophys. Acta 505, 95-127.
25. Kaziro, Y., Itoh, H., Kozasa, T., Nakafuku, M., and Satoh, T. (1991). Structure and function of signal-transducing GTP-binding proteins. Annu. Rev. Biochem. 60, 349-400.
26. Kleuss, C., Raw, A.S., Lee, E., Sprang, S.R., and Gilman, A.G. (1994). Mechanism of GTP hydrolysis by G protein α subunits. Proc. Natl. Acad. Sci. USA 91, 9828-9831.
27. Koelle, M.R., and Horvitz, H.R. (1996). EGL-10 regulates G protein signaling in the C. elegans nervous system and shares a conserved domain with many mammalian proteins. Cell 84, 115-125.
28. Lancaster, C.A., Taylor-Harris, P.M., Self, A.J., Brill, S., van Erp, H.E., and Hall, A. (1994). Characterization of rhoGAP: a GTPase-activating protein for rho-related small GTPases. J. Biol. Chem. 269, 1137-1142.
29. s and stimulate adenylyl cyclase in human pituitary tumors. Nature 340, 692-696.
30. Sα highlights the requirement for dissociation of G protein subunits. J. Biol. Chem. 267, 1212-1218.
31. Lee, E., Linder, M.E., and Gilman, A.G. (1994). Expression of G protein α subunits in Escherichia coli. Meth. Enzymol. 237, 146-164.
32. iα after expression in Escherichia coli. J. Biol. Chem. 264, 8243-8251.
33. McCormick, F. (1989). ras GTPase-activating protein: signal transmitter and signal terminator. Cell 56, 5-8.
34. Neer, E.J., and Smith,T.F. (1996). G protein heterodimers: new structures propel new questions. Cell 84, 175-178.
35. Newton, J.S., Deed, R.W., Mitchell, E.L.D., Murphy, J.J., and Norton, J.D. (1993). A B cell-specific immediate early human gene is located on chromosome band 1q31 and encodes an α helical basic phosphoprotein. Biochim. Biophys. Acta 1216, 314-316.
36. Noel, J.P., Hamm, H.E., and Sigler, P.B. (1993). The 2.2 Å crystal structure of transducin α complexed with GTP-γS. Nature 366, 654-663.
37. Pages, F., Deterre, P., and Pfister, C. (1993). Enhancement by phosphodiesterase subunits of the rate of GTP hydrolysis by transducin in bovine retinal rods: essential role of the phosphodiesterase catalytic core. J. Biol. Chem. 268, 26358-26364.
38. Ridley, A.J., Self, A.J., Kasmi, F., Paterson, H.F., Hall, A., Marshall, C.J., and Ellis, C. (1993). rho family GTPase-activating proteins p190, bcr, and rhoGAP show distinct specificities in vitro and in vivo. EMBO J. 12, 5151-5160.
39. Ross, E.M. (1995). G protein GTPase-activating proteins: regulation of speed, amplitude, and signaling selectivity. Rec. Prog. Hormone Res. 50, 207-219.
40. Roush, W. (1996). Regulating G protein signaling. Science 271, 1056-1058.
41. Siderovski, D.P., Heximer, S.P., and Forsdyke, D.R. (1994). A human gene encoding a putative basic helix-loop-helix phosphoprotein whose mRNA increases rapidly in cycloheximide-treated blood mononuclear cells. Mol. Cell. Biol. 13, 125-147.
42. Simon, M.I., Strathmann, M.P., and Gautam, N. (1991). Diversity of G proteins in signal transduction. Science 252, 802-808.
43. oα expressed in Escherichia coli. J. Biol. Chem. 268, 1414-1423.
44. 4-. Nature 372, 276-279.
45. Sternweis, P.C., and Robishaw, J.D. (1984). Isolation of two proteins with high affinity for guanine nucleotides from membranes of bovine brain. J. Biol. Chem. 259, 13806-13813.
46. Trahey, M., and McCormick, F. (1987). Acytoplasmic protein stimulates normal N-ras p21 GTPase but does not affect oncogenic mutants. Science 238, 542-545.
47. Van Dop, C., Tsubokawa, M., Bourne, H.R., and Ramachandran, J. (1984). Amino acid sequence of retinal transducin at the site ADP-ribosylated by cholera toxin. J. Biol. Chem. 259, 696-698.
48. Weiner, J.L., Guttierez-Steil, C., and Blumer, K.J. (1993). Disruption of receptor-G protein coupling in yeast promotes the function of an SST2-dependent adaption pathway. J. Biol. Chem. 268, 8070-8077.
49. Wilkie, T.M., and Simon, M.I. (1991). Cloning multigene families with degenerate PCR primers. METHODS: Companion Meth. Enzymol. 2, 32-41.