Inhibition of RhoA translocation and calcium sensitization by in vivo ADP-ribosylation with the chimeric toxin DC3B

Molecular Biology of the Cell

Volumn 8, Issue 12, 1997, Pages 2437-2447

  Fujihara, Hideyoshi ^a   Walker, Lori A ^a   Gong, Ming Cui ^a   Lemichez, Emmanuel ^b   Boquet, Patrice ^b   Somlyo, Avril V ^a   Somlyo, Andrew P ^a  

^a UNIVERSITY OF VIRGINIA   (United States)

^b INSERM   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ENDOTHELIN; GUANOSINE TRIPHOSPHATE; MYOSIN LIGHT CHAIN; PHENYLEPHRINE; PROTEIN KINASE C;

ADENOSINE DIPHOSPHATE RIBOSYLATION; ANIMAL TISSUE; ARTICLE; CALCIUM TRANSPORT; CHIMERA; COMPLEX FORMATION; IMMUNOPRECIPITATION; IN VIVO STUDY; NONHUMAN; PORTAL VEIN; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; RABBIT; SMOOTH MUSCLE CONTRACTION; SMOOTH MUSCLE FIBER;

ANIMALIA; ORYCTOLAGUS CUNICULUS;

EID: 0030721443     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.8.12.2437     Document Type: Article

References (57)

1. Aktories, K., and Just, I. (1995). Monoglucosylation of low-molecular-mass GTP-binding Rho proteins by Clostridial cytotoxins. Trends Cell Biol. 5, 441-443.
2. Alessi, D., MacDougall, L.K., Sola, M.M., Ikebe, M., and Cohen, P. (1992). The control of protein phosphatase-1 by targetting subunits. The major myosin phosphatase in avian smooth muscle is a novel form of protein phosphatase-1. Eur. J. Biochem. 210, 1023-1035.
3. Amano, M., Mukai, H., Ono, Y., Chihara, K., Matsui, T., Hamajima, Y., Okawa, K., Iwamatsu, A., and Kaibuchi, K. (1996). Identification of a putative target for Rho as the serine-threonine kinase protein kinase N. Science 271, 648-650.
4. Aullo, P., Giry, M., Olsnes, S., Popoff, M.R., Kocks, C., and Boquet, P. (1993). A chimeric toxin to study the role of the 21 kDa GTP binding protein rho in the control of actin microfilament assembly. EMBO J. 12, 921-931.
5. Bokoch, G.M., Bohl, B.P., and Chuang, T.H. (1994). Guanine nucleotide exchange regulates membrane translocation of Rac/Rho GTP-binding proteins. J. Biol. Chem. 269, 31674-31679.
6. Boquet, P., Popoff, M.R., Giry, M., Lemichez, E., and Bergez-Aullo, P. (1995). Inhibition of p21 Rho in intact cells by C3 diphtheria toxin chimera proteins. Methods Enzymol. 256, 297-306.
7. Bourmeyster, N., Stasia, M.J., Garin, J., Gagnon, J., Boquet, P., and Vignais, P.V. (1992). Copurification of rho protein and the rho-GDP dissociation inhibitor from bovine neutrophil cytosol. Effect of phosphoinositides on rho ADP-ribosylation by the C3 exoenzyme of Clostridium botulinum. Biochemistry 31, 12863-12869.
8. Bradley, A.B., and Morgan, K.G. (1987). Alterations in cytoplasmic calcium sensitivity during porcine coronary artery contractions as detected by aequorin. J. Physiol. 385, 437-448.
9. Braun, U., Habermann, B., Just, I., Aktories, K., and Vandekerckhove, J. (1989). Purification of the 22 kDa protein substrate of botulinum ADP-ribosyltransferase C3 from porcine brain cytosol and its characterization as a GTP-binding protein highly homologous to the rho gene product. FEBS Lett. 243, 70-76.
10. Burridge, K., and Chrzanowska-Wodnicka, M. (1996). Focal adhesions, contractility, and signaling. Annu. Rev. Cell Dev. Biol. 12, 463-518.
11. Chardin, P., Boquet, P., Madaule, P., Popoff, M.R., Rubin, E.J., and Gill, D.M. (1989). The mammalian G protein rhoC is ADP-ribosy-lated by Clostridium botulinum exoenzyme C3 and affects actin microfilaments in Vero cells. EMBO J. 8, 1087-1092.
12. Fleming, I.N., Elliott, C.M., and Exton, J.H. (1996). Differential translocation of Rho family GTPases by lysophosphatidic acid, endothelin-1, and platelet-derived growth factor. J. Biol. Chem. 271, 33067-33073.
13. 2+ sensitization of rabbit smooth muscle. J. Physiol. 500, 95-109.
14. Gailly, P., Wu, X., Haystead, T.A., Somlyo, A.P., Cohen, P.T., Cohen, P., and Somlyo, A.V. (1996). Regions of the 110-kDa regulatory subunit M110 required for regulation of myosin-light-chain-phosphatase activity in smooth muscle. Eur. J. Biochem. 239, 326-332.
15. Goeckeler, Z.M., and Wysolmerski, R.B. (1995). Myosin light chain kinase-regulated endothelial cell contraction: the relationship between isometric tension, actin polymerization, and myosin phosphorylation. J. Cell Biol. 130, 613-627.
16. Gong, M.C., Fuglsang, A., Alessi, D., Kobayashi, S., Cohen, P., Somlyo, A.V., and Somlyo, A.P. (1992). Arachidonic acid inhibits myosin light chain phosphatase and sensitizes smooth muscle to calcium. J. Biol. Chem. 267, 21492-21598.
17. 2+ sensitization of smooth muscle. J. Biol. Chem. 272, 10704-10709.
18. 2+ sensitization in smooth muscle. Mol. Biol. Cell 8, 279-286.
19. 2+ sensitization of smooth muscle. Proc. Natl. Acad. Sci. USA 93, 1340-1345.
20. Gosser, Y.Q., Nomanbhoy, T.K., Aghazadeh, B., Manor, D., Combs, C., Cerione, R.A., and Rosen, M.K. (1997). C-terminal binding domain of Rho GDP-dissociation inhibitor directs N-terminal inhibitory peptide to GTPases. Nature 387, 814-819.
21. Hancock, J.F., and Hall, A. (1993). A novel role for rhoGDI as an inhibitor of GAP proteins. EMBO J. 12, 1915-1921.
22. Hartshorne, D.J. (1987). Biochemistry of the contractile process in smooth muscle. In Physiology of the Gastrointestinal Tract, ed. L.R. Johnson, New York: Raven Press, 423-482.
23. 2+ sensitivity in rabbit pulmonary artery smooth muscle. Pfluegers Arch. Eur. J. Physiol. 417, 21-28.
24. Ichikawa, K., Ito, M., and Hartshorne, D.J. (1996). Phosphorylation of the large subunit of myosin phosphatase and inhibition of phosphatase activity. J. Biol. Chem. 271, 4733-4740.
25. Ikebe, M., and Brozovich, F.V. (1996). Protein kinase C increases force and slows relaxation in smooth muscle: evidence for regulation of the myosin light chain phosphatase. Biochem. Biophys. Res. Commun. 225, 370-376.
26. 2+-sensitivity in rabbit arterial skinned muscle. Br. J. Pharmacol. 111, 311-317.
27. 2+ sensitization of myosin light chain phosphorylation in smooth muscle. Biochem. J. 318, 469-475.
28. Just, I., Mohr, C., Habermann, B., Koch, G., and Aktories, K. (1993). Enhancement of Clostridium botulinum C3-catalysed ADP-ribosylation of recombinant rhoA by sodium dodecyl sulfate. Biochem. Pharmacol. 45, 1409-1416.
29. Kamm, K.E., and Stull, J.T. (1989). Regulation of smooth muscle contractile elements by second messengers. Annu. Rev. Physiol. 51, 299-313.
30. Keep, N.H., Barnes, M., Barsukov, I., Badii, R., Lian, L.Y., Segal, A.W., Moody, P.C.E., and Roberts, G.C.K. (1997). A modulator of Rho family G proteins, rhoGDI, binds these G proteins via an immunoglobulin-like domain and a flexible N-terminal arm. Structure 5, 623-633.
31. Kimura, K., Ito, M., Amano, M., Chihara, K., Fukata, Y., Nakafuku, M., Yamamori, B., Feng, J., Nakano, T., Okawa, K., Iwamatsu, A., and Kaibuchi, K. (1996). Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase). Science 273, 245-248.
32. 2+. J. Biol. Chem. 264, 5339-5342.
33. Kitazawa, T., Masuo, M., and Somlyo, A.P. (1991).G protein-mediated inhibition of myosin light-chain phosphatase in vascular smooth muscle. Proc. Natl. Acad. Sci. USA 88, 9307-9310.
34. 2+ sensitization. Am. J. Physiol. 260, C364-C370.
35. 2+ release in smooth muscle. Physiological role of inositol 1,4,5-trisphosphate in pharmacomechanical coupling. J. Biol. Chem. 264, 17997-18004.
36. 2+-sensitization. Eur. J. Pharmacol. 290, 19-27.
37. Kureishi, Y., Kobayashi, S., Amano, M., Kimura, K., Kanaide, H., Nakano, T., Kaibuchi, K., and Ito, M. (1997). Rho-associated kinase directly induces smooth muscle contraction through myosin light chain phosphorylation. J. Biol. Chem. 272, 12257-12260.
38. Lee, M.W., and Severson, D.L. (1994). Signal transduction in vascular smooth muscle: diacylglycerol second messengers and PKC action. Am. J. Physiol. 267, C659-C678.
39. Lesh, R.E., Somlyo, A.P., Owens, G.K., and Somlyo, A.V. (1995). Reversible permeabilization: A novel technique for the intracellular introduction of antisense oligodeoxynucleotides into intact smooth muscle. Circ. Res. 77, 220-230.
40. Lim, L., Manser, E., Leung, T., and Hall, C. (1996). Regulation of phosphorylation pathways by p21 GTPases - The p21 Ras-related Rho subfamily and its role in phosphorylation signalling pathways. Eur. J. Biochem. 242, 171-185.
41. Malcolm, K.C., Elliott, C.M., and Exton, J.H. (1996). Evidence for Rho-mediated agonist stimulation of phospholipase D in rat1 fibroblasts. Effects of Clostridium botulinum C3 exoenzyme. J. Biol. Chem. 271, 13135-13139.
42. Mariot. P., O'Sullivan, A.J., Brown, A.M., and Tatham, P.E. (1996). Rho guanine nucleotide dissociation inhibitor protein (RhoGDI) inhibits exocytosis in mast cells. EMBO J. 15, 6476-6482.
43. 2+-sensitizing effect of protein kinase C on vascular smooth muscle: inhibition of myosin light chain phosphatase. J. Gen. Physiol. 104, 265-286.
44. Otto, B., Steusloff, A., Just, I., Aktories, K., and Pfitzer, G. (1996). Role of Rho proteins in carbachol-induced contractions in intact and permeabilized guinea-pig intestinal smooth muscle. J. Physiol. 496, 317-329.
45. Paterson, H.F., Self, A.J., Garrett, M.D., Just, I., Aktories, K., and Hall, A. (1990). Microinjection of recombinant p21rho induces rapid changes in cell morphology. J. Cell Biol. 111, 1001-1007.
46. Ridley, A.J., and Hall, A. (1992). The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70, 389-399.
47. Sandvig, K., and Olsnes, S. (1988). Diphtheria toxin-induced channels in Vero cells selective for monovalent cations. J. Biol. Chem. 263, 12352-12359.
48. Sekine, A., Fujiwara, M., and Narumiya, S. (1989). Asparagine residue in the rho gene product is the modification site for botulinum ADP-ribosyltransferase. J. Biol. Chem. 264, 8602-8605.
49. Shimizu, H., Ito, M., Miyahara, M., Ichikawa, K., Okubo, S., Konishi, T., Naka, M., Tanaka, T., Hirano, K., Hartshorne, D.J., and Nakano, T. (1994). Characterization of the myosin-binding subunit of smooth muscle myosin phosphatase. J. Biol. Chem. 269, 30407-30411.
50. Shirazi, A., Iizuka, K., Fadden, P., Mosse, C., Somlyo, A.P., Somlyo, A.V., and Haystead, T.A. (1994). Purification and characterization of the mammalian myosin light chain phosphatase holoenzyme. The differential effects of the holoenzyme and its subunits on smooth muscle. J. Biol. Chem. 269, 31598-31606.
51. 2+-sensitivity of the time course of contraction in smooth muscle: a major role of protein phosphatases? Adv. Protein Phosphatases 5, 181-195.
52. Somlyo, A.P., and Somlyo, A.V. (1994). Signal transduction and regulation in smooth muscle. Nature 372, 231-236.
53. Sugai, M., Hashimoto, K., Kikuchi, A., Inoue, S., Okumura, H., Matsumoto, K., Goto, Y., Ohgai, H., Moriishi, K., Syuto, B., Yoshikawa, K., Suginaka, H., and Takai, Y. (1992). Epidermal cell differentiation inhibitor ADP-ribosylates small GTP-binding proteins and induces hyperplasia of epidermis. J. Biol. Chem. 267, 2600-2604.
54. Tominaga, T., Sugie, K., Hirata, M., Morii, N., Fukata, J., Uchida, A., Imura, H., and Narumiya, S. (1993). Inhibition of PMA-induced, LFA-1-dependent lymphocyte aggregation by ADP ribosylation of the small molecular weight GTP binding protein, rho. J. Cell Biol. 220, 1529-1537.
55. Walsh, M.P., Andrea, J.E., Allen, B.G., Clement-Chomienne, O., Collins, E.M., and Morgan, K.G. (1994). Smooth muscle protein kinase C. Can. J. Physiol. Pharmacol. 72, 1392-1399.
56. Wei, Y., Zhang, Y., Derewenda, U., Liu, X., Minor, W., Nakamoto, R.K., Somlyo, A.V., Somlyo, A.P., and Derewenda, Z.S. (1997). Crystal structure of RhoA-GDP: implications for function of GEFs and Clostridium toxins. Nature Struct. Biol. 4, 699-703.
57. Williamson, K.C., Smith, L.A., Moss, J., and Vaughan, M. (1990). Guanine nucleotide-dependent ADP-ribosylation of soluble rho catalyzed by Clostridium botulinum C3 ADP-ribosyltransferase. Isolation and characterization of a newly recognized form of rhoA. J. Biol. Chem. 265, 20807-20812.