Structural aspects of heterotrimeric G-protein signaling

Current Opinion in Biotechnology

Volumn 8, Issue 4, 1997, Pages 480-487

  Bohm, Andrew ^a   Gaudet, Rachelle ^a   Sigler, Paul B ^a  

^a YALE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; MEMBRANE PROTEIN; MEMBRANE RECEPTOR; PHOSDUCIN; PROTEIN SUBUNIT;

ANIMAL CELL; CONTROLLED STUDY; CRYSTAL STRUCTURE; NONHUMAN; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; PROTEIN STRUCTURE; REVIEW; SIGNAL TRANSDUCTION;

ANIMALIA;

EID: 0030835649     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(97)80072-9     Document Type: Article

References (52)

1. Gautam N, Strathmann MP, Simon MI: Diversity of G-Proteins in signal transduction. Science 1991, 252:802-808.
2. -, the transition-state analog. See also references [3,38]. Describes the GTPase activating activity of RGS proteins, and the mechanism of their action.
3. Watson N, Linder ME, Druey KM, Kehrl JH, Blumer KJ: RGS family members: GTPase-activating proteins for heterotrimeric G-protein α-subunits. Nature 1996, 383:172-175.
4. 2+/calmodulin-dependent adenylyl cyclase. Proc Natl Acad Sci USA 1996, 93:1475-1479. This paper proposes a light-dependent mechanism for phosducin's regulation by PKA and phosphatase. In doing so, they explain how phosducin regulates the light sensitivity of rod cells.
5. Noel JP, Hamm HE, Sigler PB: The 2.2 Ȧ crystal structure of transducin-αcomplexed with GTPγS. Nature 1993, 356:654-663.
6. Lambright DG, Noel JP, Hamm HE, Sigler PB: Structural determinants for the activation of the α-subunit of a heterotrimeric G-protein. Nature 1994, 369:621-628.
7. 4. Nature 1994, 372:276-279.
8. 1 and the mechanism of GTP hydrolysis. Science 1994, 265:1405-1412.
9. 1 induced by GTP hydrolysis. Science 1995, 270:954-960.
10. --bound states of Gtα and Giα) this structure clarifies the GTP hydrolysis mechanism.
11. Kjeldgaard M, Nyborg J, Clark BFC: The GTP binding motif: variations on a theme. FASEB J 1996, 10:1347-1368. An extensive review of nucleotide binding by G proteins, incorporating work on heterotrimeric G proteins as well as small G proteins like Ras and EF-Tu.
12. Hilgenfeld R: How do the GTPases really work? Struct Biol 1995, 2:3-6.
13. Berlot CH, Bourne HR: Identification of effector-activating residues of Gsα. Cell 1992, 68:911-922.
14. Skiba NP, Bae H, Hamm HE: Mapping of effector binding sites of transducin alpha-subunit using G-alpha t/G alpha i1 chimeras. J Biol Chem 1996, 271:413-424.
15. 1 in the absence of Gα. This paper contains a detailed map of contacts between Gβ and Gγ, and details of the structure formed by the WD-40 sequence motif.
16. 1 chimera. This paper details the interactions between Gα and Gβ. It also presents the model for Gαβγ's interaction with the membrane.
17. Gaudet R, Bohm A, Sigler PB: Crystal structure at 2.4 Ȧ resolution of the complex of transducin βγ and its regulator, Phosducin. Cell 1996, 87:577-588. This structure explains how phosducin competes with Gα for Gβγ. Electrostatic calculations predict how Gβγ binds the membrane in the absence of Gα, and how phosducin disrupts this interaction.
18. 2. Cell 1995, 83:1047-1058.
19. Kleuss C, Scherubl H, Hescheler J, Schultz G, Wittig B: Selectivity of signal transducion determined by ysubunits of heterotrimeric G proteins. Science 1993, 259:832-834.
20. Muller S, Hekman M, Lohse MJ: Specific enhancement of β-adrenergic receptor kinase activity by defined G-protein β and γ subunits. Proc Natl Acad Sci USA 1993, 90:10439-10443.
21. Murzin AG: Structural principles for the propeller assembly of β-sheets: the preference for seven-fold fymmetry. Proteins 1992, 14:191-201.
22. Neer EJ, Schmidt CJ, Nambudripad R, Smith TF: The ancient regulatory-protein family of WD-repeat proteins. Nature 1994, 371:297-300.
23. Wedegaertner PB, Wilson PT, H Bourne HR: Lipid modifications of trimeric G-proteins. J Biol Chem 1995, 270:503-506.
24. Kisselev OG, Ermolaeva MV, Gautam N: A farnesylated domain in the G protein γ subunit is a specific determinant of receptor coupling. J Biol Chem 1994, 269:21399-21402.
25. Hargrave PA, Hamm HE, Hofmann KP: Interaction of rhodopsin with the G-protein, transducin. Bioessays 1993, 15:43-50.
26. Lichtarge O, Bourne HR, Cohen FE: Evolutionary conserved Gαβγ binding surfaces support a model of the G protein-receptor complex. Proc Natl Acad Sci USA 1996, 93:7507-7511.
27. Onrust R, Herzmark P, Chi P, Garcia PD, Lichtarge O, Kingsley C, Bourne HR: Receptor and βγ binding sites in the alpha subunit of the retinal G-protein transducin. Science 1997, 275:381-384. This paper describes a variety of site-directed mutants of Gα that disrupt interactions with Gβγ and with 7TM receptors. On the basis of these mutations, the authors present a model for receptor catalyzed nucleotide exchange.
28. Taylor JM, Jocob-Mosier GG, Lawton RG, VanDort M, Neubig RR: Receptor and membrane interaction sites on Gβ. J Biol Chem 1996, 271:3336-3339. The authors show crosslinking between a peptide derived from the β-adrenergic receptor and the sixth or seventh WD-40 repeats of Gβ.
29. Hamm HE, Deretic D, Arendt A, Margrave PA, Koenig B, Hofmann KP: Site of G protein binding to rhodopsin mapped with synthetic peptides from the α subunit. Science 1988, 241:832-835.
30. Gierschik P, Scheer A: S-prenylated cystein analogues inhibit receptor-mediated G protein activation in native human granulocyte and reconstituted retinal rod outer segment membranes. Biochemistry 1995, 34:4952-4961.
31. Fung BK-K: Characterization of transducin from bovine retinal rod outer segments. J Biol Chem 1983, 258:10495-10502.
32. Yoshida T, Willardson BM, Wilkins JF, Jensen GJ, Thornton BD, Bitensky MW: The Phosphorylation state of phosducin determines its ability to block transducin subunit interaction and inhibit transducin binding to activated rhodopsin. J Biol Chem 1994, 269:24050-24057.
33. Danner S, Lohse MJ: Phosducin is a ubiquitious regulator of Gβγ subunits. Proc Natl Acad Sci USA 1996, 93:10145-10150.
34. Muller S, Straub A, Schoder S, Bauer PH, Lohse MJ: Interactions of phosducin with defined G-protein βγ-subunits. J Biol Chem 1996, 271:11781-11786.
35. Lee RH, Brown BM, Lolley RN: Protein kinase A phosphorylates retinal phosducin on serine 73 in situ. J Biol Chem 1990, 265:15860-15866.
36. Tanaka H, Kuo C-H, Matsuda T, Fukada Y, Hayashi F, Ding Y, Irie Y, Miki N: MEKA/Phosducin attenuates hydrophobicity of transducin bg subunits without binding to farnesyl moiety. Biochem Biophys Res Comm 1996, 223:587-591.
37. 1: stabilization of the transition state for GTP hydrolysis. Cell 1997, 89:251-261. Although only the RGS domain of RGS4 is seen, the structure explains how RGS proteins bind and accelerate GTPase activity of Gα subunits.
38. Chen C-K, Wieland T, Simon MI: RGS-r, a retinal specific RGS protein, binds an intermediate conformation of transducin and enhances recycling. Proc Natl Acad Sci USA 1996, 93:12885-12889.
39. Zhang G, Lui Y, Ruoho AE, Hurley JH: Structure of the adenylyl cyclase catalytic core. Nature 1997, 386:247-253. The two cytoplasmic domains of adenylyl cyclase are homologous to each other. This structure of a catalytically inactive homodimer of one of the two cytoplasmic domains (IIC2) presents a picture of the overall fold, but not the catalytic machinery of the ATP→cAMP reaction.
40. Yan S-Z, Huang Z-H, Hurley JH, Tang W-J: Gsα binding site and activation of mammalian adenylyl cyclase. J Biol Chem 1997, in press.
41. Clapham D, Neer EJ: New roles for G-protein βγ-dimers in transmembrane signalling. Nature 1993, 365:403-406.
42. Inglese J, Koch W, Touhara K, Lefkowitz RJ: Gβγ interactions with PH domains and Ras-MAPK signalling pathways. Trends Biochem Sci 1995, 20:151-156.
43. Van Dop C, Yamanaka G, Steinberg F, Sekura RD, Manclark CR, Stryer L, Bourne HR: ADP-ribosylation of transducin by pertussis toxin blocks the light-stimulated hydrolysis of GTP and cGMP in retinal photoreceptors. J Biol Chem 1984, 259:23-26.
44. Taroh I, Herzmark P, Nakomoto JM, Van Dop C, Bourne HR: Rapid GDP release from Gsa in patients with gain and loss of endocrine function. Nature 1994, 371:164-168.
45. 2+ binding site.
46. Wang Y, Jiang Y, Meyering-Vos M, Sprinzl M, Sigler PB: Crystal structure of the EF-Tu-EF-Ts complex from Thermus thermophilus. Nat Struct Biol 1997, in press.
47. Birnbaumer L: G Proteins in signal transduction. Annu Rev Pharmacol Toxicol 1990, 30:675-705.
48. Schertler GFX, Hargrave PA: Projection structure of frog rhodopsin in two crystal forms. Proc Natl Acad Sci USA 1995, 92:11578-11582.
49. Reeves PJ, Thurmond RL, Khorana HG: Structure and function in rhodopsin: high level expression of a synthetic bovine opsin gene and its mutants in stable mammalian cell lines. Proc Natl Acad Sci USA 1996, 93:11487-11492.
50. Kiefer H, Krieger J, Olszewski JD, Von Heijne G, Prestwich GD, Breer H: Expression of an olfactory receptor in Escherichia coli: purification, reconstitution, and ligand binding. Biochemistry 1996, 35:16077-16084.
51. Dorset DL: Electron crystallography. Acta Cryst B 1996, 52:753-769.
52. Landau EM, Rosenbusch JP: Lipidic cubic phases: a novel concept for the crystallization of membrane proteins. Proc Natl Acad Sci USA 1996, 93:14532-14535.