Crystal structure of a coiled-coil domain from human ROCK I

PLoS ONE

Volumn 6, Issue 3, 2011, Pages

  Tu, Daqi ^a,b   Li, Yiqun ^b   Song, Hyun Kyu ^c   Toms, Angela V ^a,b   Gould, Christopher J ^d   Ficarro, Scott B ^a,b   Marto, Jarrod A ^a,b   Goode, Bruce L ^d   Eck, Michael J ^a,b  

^a HARVARD MEDICAL SCHOOL   (United States)

^b DANA FARBER CANCER INSTITUTE   (United States)

^c Korea University   (South Korea)

^d BRANDEIS UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN P160; RHO KINASE; RHO KINASE 1; TROPOMYOSIN; UNCLASSIFIED DRUG;

ACTIN FILAMENT; ALPHA HELIX; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; HUMAN; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN INTERACTION; RESIDUE ANALYSIS; SEQUENCE ALIGNMENT; STRUCTURE ANALYSIS; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; DIMERIZATION; MOLECULAR GENETICS; SEQUENCE HOMOLOGY; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; RHO-ASSOCIATED KINASES; SEQUENCE HOMOLOGY, AMINO ACID; TROPOMYOSIN;

EID: 79952836685     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0018080     Document Type: Article

References (49)

1. Nakagawa O, Fujisawa K, Ishizaki T, Saito Y, Nakao K, et al. (1996) ROCK-I and ROCK-II, two isoforms of Rho-associated coiled-coil forming protein serine/threonine kinase in mice. FEBS Lett 392: 189-193.
2. Leung T, Chen XQ, Manser E, Lim L, (1996) The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton. Mol Cell Biol 16: 5313-5327.
3. Ishizaki T, Maekawa M, Fujisawa K, Okawa K, Iwamatsu A, et al. (1996) The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase. EMBO J 15: 1885-1893.
4. Leung T, Manser E, Tan L, Lim L, (1995) A novel serine/threonine kinase binding the Ras-related RhoA GTPase which translocates the kinase to peripheral membranes. J Biol Chem 270: 29051-29054.
5. Matsui T, Amano M, Yamamoto T, Chihara K, Nakafuku M, et al. (1996) Rho-associated kinase, a novel serine/threonine kinase, as a putative target for small GTP binding protein Rho. EMBO J 15: 2208-2216.
6. Riento K, Ridley AJ, (2003) Rocks: multifunctional kinases in cell behaviour. Nat Rev Mol Cell Biol 4: 446-456.
7. Amano M, Ito M, Kimura K, Fukata Y, Chihara K, et al. (1996) Phosphorylation and activation of myosin by Rho-associated kinase (Rho-kinase). J Biol Chem 271: 20246-20249.
8. Kawano Y, Fukata Y, Oshiro N, Amano M, Nakamura T, et al. (1999) Phosphorylation of myosin-binding subunit (MBS) of myosin phosphatase by Rho-kinase in vivo. J Cell Biol 147: 1023-1038.
9. Kureishi Y, Kobayashi S, Amano M, Kimura K, Kanaide H, et al. (1997) Rho-associated kinase directly induces smooth muscle contraction through myosin light chain phosphorylation. J Biol Chem 272: 12257-12260.
10. Amano M, Chihara K, Kimura K, Fukata Y, Nakamura N, et al. (1997) Formation of actin stress fibers and focal adhesions enhanced by Rho-kinase. Science 275: 1308-1311.
11. Ishizaki T, Naito M, Fujisawa K, Maekawa M, Watanabe N, et al. (1997) p160ROCK, a Rho-associated coiled-coil forming protein kinase, works downstream of Rho and induces focal adhesions. FEBS Lett 404: 118-124.
12. Amano M, Chihara K, Nakamura N, Fukata Y, Yano T, et al. (1998) Myosin II activation promotes neurite retraction during the action of Rho and Rho-kinase. Genes Cells 3: 177-188.
13. Fukata Y, Oshiro N, Kinoshita N, Kawano Y, Matsuoka Y, et al. (1999) Phosphorylation of adducin by Rho-kinase plays a crucial role in cell motility. J Cell Biol 145: 347-361.
14. Chrzanowska-Wodnicka M, Burridge K, (1996) Rho-stimulated contractility drives the formation of stress fibers and focal adhesions. J Cell Biol 133: 1403-1415.
15. Maekawa M, Ishizaki T, Boku S, Watanabe N, Fujita A, et al. (1999) Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase. Science 285: 895-898.
16. Li F, Higgs HN, (2003) The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition. Curr Biol 13: 1335-1340.
17. Watanabe N, Kato T, Fujita A, Ishizaki T, Narumiya S, (1999) Cooperation between mDia1 and ROCK in Rho-induced actin reorganization. Nature Cell Biology 1: 136-143.
18. Watanabe S, Ando Y, Yasuda S, Hosoya H, Watanabe N, et al. (2008) mDia2 induces the actin scaffold for the contractile ring and stabilizes its position during cytokinesis in NIH 3T3 cells. Mol Biol Cell 19: 2328-2338.
19. Kosako H, Yoshida T, Matsumura F, Ishizaki T, Narumiya S, et al. (2000) Rho-kinase/ROCK is involved in cytokinesis through the phosphorylation of myosin light chain and not ezrin/radixin/moesin proteins at the cleavage furrow. Oncogene 19: 6059-6064.
20. Mukai Y, Shimokawa H, Matoba T, Kandabashi T, Satoh S, et al. (2001) Involvement of Rho-kinase in hypertensive vascular disease: a novel therapeutic target in hypertension. FASEB J 15: 1062-1064.
21. Sato M, Tani E, Fujikawa H, Kaibuchi K, (2000) Involvement of Rho-kinase-mediated phosphorylation of myosin light chain in enhancement of cerebral vasospasm. Circ Res 87: 195-200.
22. Chiba Y, Takada Y, Miyamoto S, MitsuiSaito M, Karaki H, et al. (1999) Augmented acetylcholine-induced, Rho-mediated Ca2+ sensitization of bronchial smooth muscle contraction in antigen-induced airway hyperresponsive rats. Br J Pharmacol 127: 597-600.
23. Itoh K, Yoshioka K, Akedo H, Uehata M, Ishizaki T, et al. (1999) An essential part for Rho-associated kinase in the transcellular invasion of tumor cells. Nat Med 5: 221-225.
24. Nakajima M, Hayashi K, Katayama K, Amano Y, Egi Y, et al. (2003) Wf-536 prevents tumor metastasis by inhibiting both tumor motility and angiogenic actions. Eur J Pharmacol 459: 113-120.
25. Dvorsky R, Blumenstein L, Vetter IR, Ahmadian MR, (2004) Structural insights into the interaction of ROCKI with the switch regions of RhoA. J Biol Chem 279: 7098-7104.
26. Amano M, Chihara K, Nakamura N, Kaneko T, Matsuura Y, et al. (1999) The COOH terminus of Rho-kinase negatively regulates rho-kinase activity. J Biol Chem 274: 32418-32424.
27. Sebbagh M, Renvoize C, Hamelin J, Riche N, Bertoglio J, et al. (2001) Caspase-3-mediated cleavage of ROCK I induces MLC phosphorylation and apoptotic membrane blebbing. Nat Cell Biol 3: 346-352.
28. Coleman ML, Sahai EA, Yeo M, Bosch M, Dewar A, et al. (2001) Membrane blebbing during apoptosis results from caspase-mediated activation of ROCK I. Nat Cell Biol 3: 339-345.
29. Jacobs M, Hayakawa K, Swenson L, Bellon S, Fleming M, et al. (2006) The structure of dimeric ROCK I reveals the mechanism for ligand selectivity. Journal of Biological Chemistry 281: 260-268.
30. Lupas A, Van Dyke M, Stock J, (1991) Predicting coiled coils from protein sequences. Science 252: 1162-1164.
31. Burkhard P, Stetefeld J, Strelkov SV, (2001) Coiled coils: a highly versatile protein folding motif. Trends Cell Biol 11: 82-88.
32. Walshaw J, Woolfson DN, (2001) Socket: a program for identifying and analysing coiled-coil motifs within protein structures. J Mol Biol 307: 1427-1450.
33. Grum VL, Li D, MacDonald RI, Mondragon A, (1999) Structures of two repeats of spectrin suggest models of flexibility. Cell 98: 523-535.
34. Glover JN, Harrison SC, (1995) Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA. Nature 373: 257-261.
35. Freedman SJ, Song HK, Xu Y, Sun ZY, Eck MJ, (2003) Homotetrameric structure of the SNAP-23 N-terminal coiled-coil domain. J Biol Chem 278: 13462-13467.
36. Strelkov SV, Burkhard P, (2002) Analysis of alpha-helical coiled coils with the program TWISTER reveals a structural mechanism for stutter compensation. J Struct Biol 137: 54-64.
37. O'Shea EK, Klemm JD, Kim PS, Alber T, (1991) X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil. Science 254: 539-544.
38. Holm L, Sander C, (1993) Protein structure comparison by alignment of distance matrices. J Mol Biol 233: 123-138.
39. Nitanai Y, Minakata S, Maeda K, Oda N, Maeda Y, (2007) Crystal structures of tropomyosin: flexible coiled-coil. Adv Exp Med Biol 592: 137-151.
40. Derewenda U, Tarricone C, Choi WC, Cooper DR, Lukasik S, et al. (2007) The structure of the coiled-coil domain of Ndel1 and the basis of its interaction with Lis1, the causal protein of Miller-Dieker lissencephaly. Structure 15: 1467-1481.
41. Whitby FG, Phillips GN Jr, (2000) Crystal structure of tropomyosin at 7 Angstroms resolution. Proteins 38: 49-59.
42. Van Duyne GD, Standaert RF, Karplus PA, Schreiber SL, Clardy J, (1993) Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. Journal of molecular biology 229: 105-124.
43. Otwinowski Z, Minor W, (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods in enzymology 276: 307-326.
44. Adams PD, Afonine PV, Bunkoczi G, Chen VB, Davis IW, et al. (2010) PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66: 213-221.
45. McCoy AJ, Grosse-Kunstleve RW, Adams PD, Winn MD, Storoni LC, et al. (2007) Phaser crystallographic software. J Appl Crystallogr 40: 658-674.
46. Terwilliger TC, (2003) Automated main-chain model building by template matching and iterative fragment extension. Acta Crystallogr D Biol Crystallogr 59: 38-44.
47. Terwilliger TC, (2000) Maximum-likelihood density modification. Acta Crystallogr D Biol Crystallogr 56: 965-972.
48. Emsley P, Cowtan K, (2004) Coot: model-building tools for molecular graphics. Acta Crystallographica Section D: Biological Crystallography 60: 2126-2132.
49. Brunger AT, (2007) Version 1.2 of the Crystallography and NMR system. Nature Protocols 2: 2728-2733.