GTPase-activating proteins and their complexes

Current Opinion in Structural Biology

Volumn 8, Issue 2, 1998, Pages 195-201

  Gamblin, Steven J ^a   Smerdon, Stephen J ^a  

^a NATIONAL INSTITUTE FOR MEDICAL RESEARCH   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; RAS PROTEIN; RHO FACTOR;

COMPLEX FORMATION; CRYSTALLOGRAPHY; HYDROLYSIS; PRIORITY JOURNAL; PROTEIN STABILITY; REVIEW; STRUCTURE ACTIVITY RELATION;

EID: 0032054663     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(98)80038-9     Document Type: Article

References (48)

1. Bourne HR, Sanders DA, McCormick F. The GTPase superfamily: a conserved switch for diverse cell functions. Nature. 348:1990;125-132.
2. Bourne HR, Sanders DA, McCormick F. The GTPase superfamily: conserved structure and molecular mechanism. Nature. 349:1991;117-127.
3. Boguski MS, McCormick F. Proteins regulating Ras and its relatives. Nature. 366:1993;643-654.
4. Gideon P, John J, Frech M, Lautwein A, Clark R, Scheffler JE, Wittinghofer A. Mutational and kinetic analysis of the GTPase-activating protein (GAP)-p21 interaction: the C-terminal domain of GAP is not sufficient for full activity. Mol Cell Biol. 12:1992;2050-2056.
5. Lamarche N, Hall A. GAPs for rho-related GTPases. Trends Genet. 10:1994;436-440.
6. Pai EF, Krenge U, Petsko GA, Goody RS, Kabsch W, Wittingnofer A. Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 Å resolution: implications for the mechanism of GTP hydrolysis. EMBO J. 9:1990;2351-2359.
7. Milburn MV, Tong L, deVos AM, Bruenger A, Yamaizumi Z, Nishimura S, Kim S-H. Molecular switch for signal transduction: structural differences between active and inactive forms of photooncogenic ras proteins. Science. 247:1990;939-945.
8. Schlichting I, Almo SC, Rapp G, Wilson K, Petratos, Lentfer A, Wittinghofer, Kabsch W, Pai EF, Petsko GA, Goody RS. Time-resolved X-ray crystallographic study of the conformational change in Ha-Ras p21 protein on GTP hydrolysis. Nature. 345:1990;309-315.
9. Cherfils J, Menetrey J, Le Bras G, Le Bras G, Janoueix-Lerosey I, de Grunzburg J, Garel J-R, Auzat I. Crystal structures of the small G protein Rap2A in complex with its substrate GTP, with GDP and with GTPγS. EMBO J. 16:1997;5582-5591.
10. Kjeldgaard M, Nissen P, Thirup S, Nyborg J. The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation. Structure. 1:1993;35-50.
11. Bechtold H, Reshetnikova L, Reiser COA, Schirmer NK, Sprinzl M, Hilgenfeld R. Crystal structure of active elongation factor Tu reveals major domain rearrangements. Nature. 365:1993;126-132.
12. Lambright DG, Noel JP, Hamm HE, Sigler PB. Structural determinants for activation of the α subunit of a heterotrimeric G protein. Nature. 369:1994;621-628.
13. iα1 and the mechanism of GTP hydrolysis. Science. 265:1994;1405-1412.
14. -. Nature. 372:1994;276-279.
15. iα1. Biochemistry. 36:1997;15660-15669.
16. Hirshberg M, Stockley RW, Dodson G, Webb MR. The crystal structure of human rac1, a member of the rho-family complexed with a GTP analogue. of special interest Nat Struct Biol. 4:1997;147-152 This paper reports the the first structure determination of a Rho subfamily small G protein, rac1A.
17. Feltham JL, Doetsch V, Raza S, Manor D, Cerione RA, Sutcliffe MJ, Wagner G, Oswald RE. Definition of the switch surface in the solution structure of Cdc42Hs. Biochemistry. 36:1997;8755-8766.
18. Wei Y, Zhang Y, Derewenda U, Liu X, Minor W, Nakamoto RK, Somlyo AV, Somlyo AP, Derewenda ZS. Crystal structure of RhoAGDP: implications for function of GEFs and Clostridium toxins. Nat Struct Biol. 4:1997;699-703.
19. Kjeldgaard M, Nyborg J, Clark BFC. The GTP binding motif: variations on a theme. of special interest FASEB J. 10:1996;1347-1368 An excellent review describing the widespread occurrence of the GTP-binding motif.
20. Barbacid M. Ras genes. Annu Rev Biochem. 56:1987;779-828.
21. Musacchio A, Cantley LC, Harrison SC. Crystal structure of the breakpoint cluster region-homology domain from phosphoinositide 3-kinase p85α subunit. Proc Natl Acad Sci USA. 93:1996;14373-14378.
22. Scheffzek K, Lautwein A, Kabsch W, Ahmadian MR, Wittinghofer A. Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras. Nature. 384:1996;591-596.
23. Barrett T, Xiao B, Dodson EJ, Dodson G, Ludbrook SB, Nurmahomed K, Gamblin SJ, Musacchio A, Smerdon SJ, Eccleston JF. The structure of the GTPase-activating domain from p50rhoGAP. Nature. 385:1997;458-461.
24. α - GAP complex indicates that activation occurs through the stabilisation of the switch regions of the G protein.
25. Scheffzek K, Ahmadian MR, Kabsch W, Wiesmuller L, Lautwein A, Schmitz F, Wittinghofer A. The ras - rasGAP complex: structural basis for GTPase activation and its loss in oncogenic ras mutants. of outstanding interest Science. 277:1997;333-338 The complex described in this paper provides the first structural description of RasGAP-mediated GTPase activation of Ras.
26. Rittinger K, Walker PA, Eccleston JF, Nurmahomed K, Owen D, Laue E, Gamblin SJ, Smerdon SJ. Crystal structure of the complex between Cdc42Hs·GMPPNP and p50rhoGAP. of outstanding interest Nature. 388:1997;693-697 The first structural analysis of a Rho family G protein in complex with RhoGAP. This complex represents the ground state of GAP-assisted GTPase reactions.
27. Rittinger K, Walker AP, Eccleston JF, Smerdon SK, Gamblin SJ. Structure at 1.65 Å of RhoA and its GTPase-activating protein in complex with a transition-state analogue. of outstanding interest Nature. 389:1997;758-762 This structure of Rho - RhoGAP in a transition-state complex provides the first structural description of the substantial conformational change during the catalytic cycle.
28. Zheng Y, Bagrodia S, Cerione RA. Activation of phosphoinositide 3-kinase activity by cdc42Hs binding to p85. J Biol Chem. 269:1994;18727-18730.
29. Tolias KF, Cantley LC, Carpenter CL. Rho family GTPases bind to phosphoinositide kinases. J Biol Chem. 270:1995;17656-17659.
30. Rittinger K, Taylor WR, Smerdon S, Gamblin SJ. RhoGaP and rasGAP share a common fold. of special interest Nature. 1998; A comparison of the core structures of RhoGAP and RasGAP reveals a common fold in the absence of any sequence homology.
31. Rall TW, Sutherland EW. Formation of a cyclic adenine ribonucleotide by tissue particles. J Biol Chem. 232:1958;1065-1067.
32. Steinweis PC, Gilman AG. Aluminium: a requirement for activation of the regulatory component of adenylate cyclase by fluoride. Proc Natl Acad Sci USA. 79:1982;4888-4891.
33. Chabre M. Aluminofluoride and beryllfluoride complexes: new phosphate analogs in enxymology. Trends Biochem Sci. 15:1990;6-10.
34. Wittinghofer A, Pai E, Goody RS. Structural and kinetic aspects of the GTPase reaction of H-ras p21. Handbook Exp Pharmacol. 108:1993;195-212.
35. x transition-state analogue.
36. Noel JP. Turning off the Ras switch with the flick of a finger. Nat Struct Biol. 4:1997;677-680.
37. Bournè HR. The arginine finger strikes again. Nature. 389:1997;673-674.
38. Gilman AG. G proteins: transducers of receptor-generated signals. Annu Rev Biochem. 56:1987;615-649.
39. Hamm HE, Gilchrist A. Heterotrimeric G proteins. Curr Opin Cell Biol. 8:1996;189-196.
40. Sprang SR. G-protein mechanisms: insights from structural analysis. Annu Rev Biochem. 66:1997;639-678.
41. Dohlman HG, Thorners J. RGS proteins and signaling by heterotrimeric G-proteins. J Biol Chem. 272:1997;3871-3874.
42. Koelle MR. A new family of G-protein regulators - the RGS proteins. Curr Opin Cell Biol. 9:1997;143-147.
43. Markby DW, Onrust R, Bourne HR. Separate GTP binding and GTPase activating domains of Gα subunit. Science. 262:1993;1895-1901.
44. Nassar N, Horn G, Herrmann C, Scherer A, McCormick F, Wittinghofer A. The 2.2 Å crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue. Nature. 375:1995;554-560.
45. iα in complex with its downstream effector adenylyl cyclase. The effector binds mainly through interactions with switch II.
46. α. Proc Natl Acad Sci USA, 94:428-432.
47. Carson M. RIBBONS 2.0. J Appl Crystallogr. 24:1991;958-961.
48. Kraulis PJ. MOLSCRIPT - a program to produce both detailed and schematic plots of protein structures. J Appl Crystallogr. 24:1991;946-950.