Trends in Cardiovascular Medicine
Volume 16, Issue 6 , Pages 199-204 , August 2006

Regulation of Rho Proteins by Phosphorylation in the Cardiovascular System

  • Gervaise Loirand
  • ,
  • Christophe Guilluy
  • ,
  • Pierre Pacaud

      Affiliations

    • Corresponding Author InformationAddress correspondence to: Pierre Pacaud, Inserm U-533 Institut du Thorax, Faculté des Sciences, 2 rue de la Houssinière, BP 92208, 44322 Nantes cedex 3, France. Tel.: (+33) 2-51-12-56-14; fax: (+33) 2-51-12-56-14.

References 

  1. Andresen BT, Shome K, Jackson EK, et al. AT2 receptors cross talk with AT1 receptors through a nitric oxide- and RhoA-dependent mechanism resulting in decreased phospholipase D activity. Am J Physiol. 2005;288:F763–F770
  2. Begum N, Sandu OA, Ito M, et al. Active Rho kinase (ROK-alpha) associates with insulin receptor substrate-1 and inhibits insulin signaling in vascular smooth muscle cells. J Biol Chem. 2002;277:6214–6222
  3. Brophy CM, Woodrum DA, Pollock J, et al. cGMP-dependent protein kinase expression restores contractile function in cultured vascular smooth muscle cells. J Vasc Res. 2002;39:95–103
  4. Budzyn K, Marley PD, Sobey CG. Targeting Rho and Rho-kinase in the treatment of cardiovascular disease. Trends Pharmacol Sci. 2005;27:97–104
  5. Burridge K, Wennerberg K. Rho and Rac take center stage. Cell. 2004;116:167–179
  6. Cario-Toumaniantz C, Reillaudoux G, Sauzeau V, et al. Modulation of RhoA–Rho kinase-mediated Ca2+ sensitization of rabbit myometrium during pregnancy-role of Rnd3. J Physiol. 2003;552:403–413
  7. Chitaley K, Webb RC. Nitric oxide induces dilation of rat aorta via inhibition of rho-kinase signaling. Hypertension. 2002;39:438–442
  8. Ellerbroek SM, Wennerberg K, Burridge K. Serine phosphorylation negatively regulates RhoA in vivo. J Biol Chem. 2003;278:19023–19031
  9. Etienne-Manneville S, Hall A. Rho GTPases in cell biology. Nature. 2002;420:629–635
  10. Forget MA, Desrosiers RR, Gingras D, et al. Phosphorylation states of Cdc42 and RhoA regulate their interactions with Rho GDP dissociation inhibitor and their extraction from biological membranes. Biochem J. 2002;361:243–254
  11. Fu HW, Casey PJ. Enzymology and biology of CaaX protein prenylation. Recent Prog Horm Res. 1999;54:315–342[disussion 342–313]
  12. Gudi T, Chen JC, Casteel DE, et al. cGMP-dependent protein kinase inhibits serum-response element-dependent transcription by inhibiting rho activation and functions. J Biol Chem. 2002;277:37382–37393
  13. Hoffman GR, Nassar N, Cerione RA. Structure of the Rho family GTP-binding protein Cdc42 in complex with the multifunctional regulator RhoGDI. Cell. 2000;100:345–356
  14. Kjoller L, Hall A. Signaling to Rho GTPases. Exp Cell Res. 1999;253:166–179
  15. Kwon T, Kwon DY, Chun J, et al. Akt protein kinase inhibits Rac1–GTP binding through phosphorylation at serine 71 of Rac1. J Biol Chem. 2000;275:423–428
  16. Lang P, Gesbert F, Delespine-Carmagnat M, et al. Protein kinase A phosphorylation of RhoA mediates the morphological and functional effects of cyclic AMP in cytotoxic lymphocytes. Embo J. 1996;15:510–519
  17. Laufs U, Liao JK. Post-transcriptional regulation of endothelial nitric oxide synthase mRNA stability by Rho GTPase. J Biol Chem. 1998;273:24266–24271
  18. Liao JK, Laufs U. Pleiotropic effects of statins. Annu Rev Pharmacol Toxicol. 2004;45:89–118
  19. Loirand G, Cario-Toumaniantz C, Chardin P, et al. The Rho-related protein Rnd1 inhibits Ca2+ sensitization of rat smooth muscle. J Physiol. 1999;516(Pt 3):825–834
  20. Ming XF, Viswambharan H, Barandier C, et al. Rho GTPase/Rho kinase negatively regulates endothelial nitric oxide synthase phosphorylation through the inhibition of protein kinase B/Akt in human endothelial cells. Mol Cell Biol. 2002;22:8467–8477
  21. Moon SY, Zheng Y. Rho GTPase-activating proteins in cell regulation. Trends Cell Biol. 2003;13:13–22
  22. Moriki N, Ito M, Seko T, et al. RhoA activation in vascular smooth muscle cells from stroke-prone spontaneously hypertensive rats. Hypertens Res. 2004;27:263–270
  23. Nobes CD, Hall A. Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell. 1995;81:53–62
  24. Nusser N, Gosmanova E, Makarova N, et al. Serine phosphorylation differentially affects RhoA binding to effectors: implications to NGF-induced neurite outgrowth. Cell Signal. 2006;18:704–714
  25. Pacaud P, Sauzeau V, Loirand G. Rho proteins and vascular diseases. Arch Mal Coeur Vaiss. 2005;98:249–254
  26. Riento K, Guasch RM, Garg R, et al. RhoE binds to ROCK I and inhibits downstream signaling. Mol Cell Biol. 2003;23:4219–4229
  27. Riento K, Totty N, Villalonga P, et al. RhoE function is regulated by ROCK I-mediated phosphorylation. Embo J. 2005;24:1170–1180
  28. Rolli-Derkinderen M, Sauzeau V, Boyer L, et al. Phosphorylation of serine 188 protects RhoA from ubiquitin/proteasome-mediated degradation in vascular smooth muscle cells. Circ Res. 2005;96:1152–1160
  29. Sauzeau V, Le Jeune H, Cario-Toumaniantz C, et al. Cyclic GMP-dependent protein kinase signaling pathway inhibits RhoA-induced Ca2+ sensitization of contraction in vascular smooth muscle. J Biol Chem. 2000;275:21722–21729
  30. Sauzeau V, Rolli-Derkinderen M, Lehoux S, et al. Sildenafil prevents change in RhoA expression induced by chronic hypoxia in rat pulmonary artery. Circ Res. 2003;93:630–637
  31. Sauzeau V, Rolli-Derkinderen M, Marionneau C, et al. RhoA expression is controlled by nitric oxide through cGMP-dependent protein kinase activation. J Biol Chem. 2003;278:9472–9480
  32. Savoia C, Tabet F, Yao G, et al. Negative regulation of RhoA/Rho kinase by angiotensin II type 2 receptor in vascular smooth muscle cells: role in angiotensin II-induced vasodilation in stroke-prone spontaneously hypertensive rats. J Hypertens. 2005;23:1037–1045
  33. Sawada N, Itoh H, Tsujimoto H, et al. Phosphorylation and inhibition of vascular smooth muscle RhoA by cGMP-dependent protein kinase modulates vascular remodeling in vivo. Circulation. 2005;112(Supp II):II-251
  34. Sawada N, Itoh H, Yamashita J, et al. cGMP-dependent protein kinase phosphorylates and inactivates RhoA. Biochem Biophys Res Commun. 2001;280:798–805
  35. Schmidt A, Hall A. Guanine nucleotide exchange factors for Rho GTPases: turning on the switch. Genes Dev. 2002;16:1587–1609
  36. Seabra MC. Membrane association and targeting of prenylated Ras-like GTPases. Cell Signal. 1998;10:167–172
  37. Seasholtz TM, Majumdar M, Brown JH. Rho as a mediator of G protein-coupled receptor signaling. Mol Pharmacol. 1999;55:949–956
  38. Tu S, Wu WJ, Wang J, et al. Epidermal growth factor-dependent regulation of Cdc42 is mediated by the Src tyrosine kinase. J Biol Chem. 2003;278:49293–49300
  39. Van Nieuw Amerongen GP, Van Hinsbergh VW. Cytoskeletal effects of rho-like small guanine nucleotide-binding proteins in the vascular system. Arterioscler Thromb Vasc Biol. 2001;21:300–311

PII: S1050-1738(06)00053-3

doi: 10.1016/j.tcm.2006.03.010

Trends in Cardiovascular Medicine
Volume 16, Issue 6 , Pages 199-204 , August 2006