The inhibitory G protein Gi identified as pertussis toxin-catalyzed ADP-ribosylation

Biological and Pharmaceutical Bulletin

Volumn 35, Issue 12, 2012, Pages 2103-2111

  Katada, Toshiaki ^a  

^a UNIVERSITY OF TOKYO   (Japan)

Author keywords

ADP ribosylation; G protein; Guanosine 5 triphosphate; Pertussis toxin; Receptor; Signal transduction

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALPHA ADRENERGIC RECEPTOR; INHIBITORY GUANINE NUCLEOTIDE BINDING PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; PERTUSSIS TOXIN; PERTUSSIS VACCINE;

ADENOSINE DIPHOSPHATE RIBOSYLATION; CATALYSIS; CELL CULTURE; CELL FREE SYSTEM; DRUG EFFICACY; DRUG MECHANISM; HYPERGLYCEMIA; INSULIN RELEASE; INTRACELLULAR SIGNALING; NONHUMAN; PANCREAS ISLET; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN MODIFICATION; PROTEIN PURIFICATION; PROTEIN TARGETING; REVIEW;

ADENOSINE DIPHOSPHATE RIBOSE; ADENYLATE CYCLASE; ADRENERGIC ALPHA-2 RECEPTOR ANTAGONISTS; ANIMALS; CELL MEMBRANE; CYCLIC AMP; GTP-BINDING PROTEIN ALPHA SUBUNITS, GI-GO; GTP-BINDING PROTEINS; HUMANS; INSULIN; ISLETS OF LANGERHANS; NAD; PERTUSSIS TOXIN; SIGNAL TRANSDUCTION;

EID: 84871574702     PISSN: 09186158     EISSN: 13475215     Source Type: Journal    
DOI: 10.1248/bpb.b212024     Document Type: Review

References (53)

1. Katada T, Ui M. Accelerated turnover of blood glucose in pertussis-sensitized rats due to combined actions of endogenous insulin and adrenergic β-stimulation. Biochim. Biophys. Acta, 421, 57-69 (1976).
2. Yajima M, Hosoda K, Kanbayashi Y, Nakamura T, Nogimori K, Mizushima Y, Nakase Y, Ui M. Islets-activating protein (IAP) in Bordetella pertussis that potentiates insulin secretory responses of rats. Purification and characterization. J. Biochem., 83, 295-303 (1978).
3. Yajima M, Hosoda K, Kanba yashi Y, Nakamura T, Takahashi I, Ui M. Biological properties of islets-activating protein (IAP) purified from the culture medium of Bordetella pertussis. J. Biochem., 83, 305-312 (1978).
4. Katada T, Ui M. Effect of in vivo pretreatment of rats with a new protein purified from Bordetella pertussis on in vitro secretion of insulin: role of calcium. Endocrinology, 104, 1822-1827 (1979).
5. Katada T, Ui M. Islet-activating protein. Enhanced insulin secretion and cyclic AMP accumulation in pancreatic islets due to activation of native calcium ionophores. J. Biol. Chem., 254, 469-479 (1979).
6. 45Ca flux. J. Biochem., 89, 979-990 (1981).
7. Katada T, Ui M. Islet-activating protein. A modifier of receptor-mediated regulation of rat islet adenylate cyclase. J. Biol. Chem., 256, 8310-8317 (1981).
8. 2-adrenergic inhibition of insulin secretion via interference with cyclic AMP generation in rat pancreatic islets. Mol. Pharmacol., 21, 648-653 (1982).
9. Hazeki O, Ui M. Modification by islet-activating protein of receptor-mediated regulation of cyclic AMP accumulation in isolated rat heart cells. J. Biol. Chem., 256, 2856-2862 (1981).
10. Kurose H, Katada T, Amano T, Ui M. Specific uncoupling by islet-activating protein, pertussis toxin, of negative signal transduction via α-adrenergic, cholinergic, and opiate receptors in neuroblastomaxglioma hybrid cells. J. Biol. Chem., 258, 4870-4875 (1983).
11. Katada T, Ui M. Slow interaction of islet-activating protein with pancreatic islets during primary culture to cause reversal of α-adrenergic inhibition of insulin secretion. J. Biol. Chem., 255, 9580-9588 (1980).
12. Katada T, Amano T, Ui M. Modulation by islet-activating protein of adenylate cyclase activity in C6 glioma cells. J. Biol. Chem., 257, 3739-3746 (1982).
13. Katada T, Ui M. Direct modification of the membrane adenylate cyclase system by islet-activating protein due to ADP-ribosylation of a membrane protein. Proc. Natl. Acad. Sci. U.S.A., 79, 3129-3133 (1982).
14. Katada T, Ui M. ADP-ribosylation of the specific membrane protein of C6 cells by islet-activating protein associated with modification of adenylate cyclase activity. J. Biol. Chem., 257, 7210-7216 (1982).
15. Tamura M, Nogimori K, Murai S, Yajima M, Ito K, Katada T, Ui M, Ishii S. Subunit structure of islet-activating protein, pertussis toxin, in conformity with the A-B model. Biochemistry, 21, 5516-5522 (1982).
16. Locht C, Keith JM. Pertussis toxin gene: nucleotide sequence and genetic organization. Science, 232, 1258-1264 (1986).
17. Nicosia A, Perugini M, Franzini C, Casagli MC, Borri MG, Antoni G, Almoni M, Neri P, Ratti G, Rappuoli R. Cloning and sequencing of the pertussis toxin genes: operon structure and gene duplication. Proc. Natl. Acad. Sci. U.S.A., 83, 4631-4635 (1986).
18. Katada T, Tamura M, Ui M. The A protomer of islet-activating protein, pertussis toxin, as an active peptide catalyzing ADP-ribosylation of a membrane protein. Arch. Biochem. Biophys., 224, 290-298 (1983).
19. Burns DL, Manclark CR. Adenine nucleotides promote dissociation of pertussis toxin subunits. J. Biol. Chem., 261, 4324-4327 (1986).
20. Hausman SZ, Manclark CR, Burns DL. Binding of ATP by pertussis toxin and isolated toxin subunits. Biochemistry, 29, 6128-6131 (1990).
21. Brennan MJ, David JL, Kenimer JG, Manclark CR. Lectin-like binding of pertussis toxin to a 165-kilodalton Chinese hamster ovary cell glycoprotein. J. Biol. Chem., 263, 4895-4899 (1988).
22. Clark CG, Armstrong GD. Lymphocyte receptors for pertussis toxin. Infect. Immun., 58, 3840-3846 (1990).
23. Heerze LD, Chong PC, Armstrong GD. Investigation of the lectin-like binding domains in pertussis toxin using synthetic peptide sequences. Identification of a sialic acid binding site in the S2 subunit of the toxin. J. Biol. Chem., 267, 25810-25815 (1992).
24. Kaslow HR, Burns DL. Pertussis toxin and target eukaryotic cells: binding, entry, and activation. FASEB J., 6, 2684-2690 (1992).
25. Saukkonen K, Burnette WN, Mar VL, Masure HR, Tuomanen EI. Pertussis toxin has eukaryotic-like carbohydrate recognition domains. Proc. Natl. Acad. Sci. U.S.A., 89, 118-122 (1992).
26. Hausman SZ, Burns DL. Interaction of pertussis toxin with cells and model membranes. J. Biol. Chem., 267, 13735-13739 (1992).
27. Cortina G, Barbieri JT. Localization of a region of the S1 subunit of pertussis toxin required for efficient ADP-ribosyltransferase activity. J. Biol. Chem., 266, 3022-3030 (1991).
28. Bokoch GM, Katada T, Northup JK, Hewlett EL, Gilman AG. Identification of the predominant substrate for ADP-ribosylation by islet activating protein. J. Biol. Chem., 258, 2072-2075 (1983).
29. Bokoch GM, Katada T, Northup JK, Ui M, Gilman AG. Purification and properties of the inhibitory guanine nucleotide-binding regulatory component of adenylate cyclase. J. Biol. Chem., 259, 3560-3567 (1984).
30. Katada T, Bokoch GM, Northup JK, Ui M, Gilman AG. The inhibitory guanine nucleotide-binding regulatory component of adenylate cyclase. Properties and function of the purified protein. J. Biol. Chem., 259, 3568-3577 (1984).
31. Katada T, Northup JK, Bokoch GM, Ui M, Gilman AG. The inhibitory guanine nucleotide-binding regulatory component of adenylate cyclase. Subunit dissociation and guanine nucleotide-dependent hormonal inhibition. J. Biol. Chem., 259, 3578-3585 (1984).
32. - and wild type membranes. J. Biol. Chem., 259, 3586-3595 (1984).
33. Sternweis PC, Robishaw JD. Isolation of two proteins with high affinity for guanine nucleotides from membranes of bovine brain. J. Biol. Chem., 259, 13806-13813 (1984).
34. i) purified from bovine brain is a high affinity GTPase. J. Biol. Chem., 260, 2057-2063 (1985).
35. Katada T, Oinuma M, Ui M. Two guanine nucleotide-binding proteins in rat brain serving as the specific substrate of islet-activating protein, pertussis toxin. Interaction of the α-subunits with βγ-subunits in development of their biological activities. J. Biol. Chem., 261, 8182-8191 (1986).
36. Stryer L, Bourne HR. G proteins: a family of signal transducers. Annu. Rev. Cell Biol., 2, 391-419 (1986).
37. Kurose H, Katada T, Haga T, Haga K, Ichiyama A, Ui M. Functional interaction of purified muscarinic receptors with purified inhibitory guanine nucleotide regulatory proteins reconstituted in phospholipid vesicles. J. Biol. Chem., 261, 6423-6428 (1986).
38. Haga K, Haga T, Ichiyama A, Katada T, Kurose H, Ui M. Functional reconstitution of purified muscarinic receptors and inhibitory guanine nucleotide regulatory protein. Nature, 316, 731-733 (1985).
39. West REJ Jr, Moss J, Vaughan M, Liu T, Liu TY. Pertussis toxin-catalyzed ADP-ribosylation of transducin. Cysteine 347 is the ADP-ribose acceptor site. J. Biol. Chem., 260, 14428-14430 (1985).
40. Hoshino S, Kikkawa S, Takahashi K, Itoh H, Kaziro Y, Kawasaki H, Suzuki K, Katada T, Ui M. Identification of sites for alkylation by N-ethylmaleimide and pertussis toxin-catalyzed ADP-ribosylation on GTP-binding proteins. FEBS Lett., 276, 227-231 (1990).
41. Katada T, Oinuma M, Ui M. Mechanisms for inhibition of the catalytic activity of adenylate cyclase by the guanine nucleotide-binding proteins serving as the substrate of islet-activating protein, pertussis toxin. J. Biol. Chem., 261, 5215-5221 (1986).
42. Van Dop C, Tsubokawa M, Bourne HR, Ramachandran J. Amino acid sequence of retinal transducin at the site ADP-ribosylated by cholera toxin. J. Biol. Chem., 259, 696-698 (1984).
43. Iiri T, Ohoka Y, Ui M, Katada T. Functional modification by cholera-toxin-catalyzed ADP-ribosylation of a guanine-nucleotide-binding regulatory protein serving as the substrate of pertussis toxin. Eur. J. Biochem., 202, 635-641 (1991).
44. Iiri T, Ohoka Y, Ui M, Katada T. Modification of the function of pertussis toxin substrate GTP-binding protein by cholera toxin-catalyzed ADP-ribosylation. J. Biol. Chem., 267, 1020-1026 (1992).
45. Bornancin F, Franco M, Bigay J, Chabre M. Functional modifications of transducin induced by cholera or pertussis-toxin-catalyzed ADP-ribosylation. Eur. J. Biochem., 210, 33-44 (1992).
46. Landis CA, Masters SB, Spada A, Pace AM, Bourne HR, Vallar L. GTPase inhibiting mutations activate the α chain of Gs and stimulate adenylyl cyclase in human pituitary tumours. Nature, 340, 692-696 (1989).
47. Lyons J, Landis CA, Harsh G, Vallar L, Grünewald K, Feichtinger H, Duh QY, Clark OH, Kawasaki E, Bourne HR, McCormick F. Two G protein oncogenes in human endocrine tumors. Science, 249, 655-659 (1990).
48. i2 induces neoplastic transformation of Rat-1 cells. Proc. Natl. Acad. Sci. U.S.A., 88, 7031-7035 (1991).
49. i2 inhibit cyclic AMP accumulation. Nature, 351, 63-65 (1991).
50. Schleifer LS, Kahn RA, Hanski E, Northup JK, Sternweis PC, Gilman AG. Requirements for cholera toxin-dependent ADP-ribosylation of the purified regulatory component of adenylate cyclase. J. Biol. Chem., 257, 20-23 (1982).
51. Kahn RA, Gilman AG. Purification of a protein cofactor required for ADP-ribosylation of the stimulatory regulatory component of adenylate cyclase by cholera toxin. J. Biol. Chem., 259, 6228-6234 (1984).
52. s by cholera toxin is itself a GTP binding protein. J. Biol. Chem., 261, 7906-7911 (1986).
53. Rasmussen SGF, DeVree BT, Zou Y, Kruse AC, Chung KY, Kobilka TS, Thian FS, Chae PS, Pardon E, Calinski D, Mathiesen JM, Shah STA, Lyons JA, Caffrey M, Gellman SH, Steyaert J, Skiniotis G, Weis WI, Sunahara RK, Kobilka BK. Crystal structure of the β2 adrenergic receptor-Gs protein complex. Nature, 477, 549-555 (2011).