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Volumn 14, Issue 3, 2006, Pages 589-600

Molecular mechanism for the regulation of rho-kinase by dimerization and its inhibition by fasudil

Author keywords

[No Author keywords available]

Indexed keywords

FASUDIL; PHOSPHATE; RHO KINASE;

EID: 33644837834     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2005.11.024     Document Type: Article
Times cited : (138)

References (42)
  • 4
    • 0344234281 scopus 로고    scopus 로고
    • Protein kinase a in complex with Rho-kinase inhibitors Y-27632, Fasudil, and H-1152P: Structural basis of selectivity
    • C. Breitenlechner, M. Gassel, H. Hidaka, V. Kinzel, R. Huber, R.A. Engh, and D. Bossemeyer Protein kinase A in complex with Rho-kinase inhibitors Y-27632, Fasudil, and H-1152P: structural basis of selectivity Structure 11 2003 1595 1607
    • (2003) Structure , vol.11 , pp. 1595-1607
    • Breitenlechner, C.1    Gassel, M.2    Hidaka, H.3    Kinzel, V.4    Huber, R.5    Engh, R.A.6    Bossemeyer, D.7
  • 6
    • 0034713879 scopus 로고    scopus 로고
    • Myotonic dystrophy protein kinase domains mediate localization, oligomerization, novel catalytic activity, and autoinhibition
    • E.W. Bush, S.M. Helmke, R.A. Birnbaum, and M.B. Perryman Myotonic dystrophy protein kinase domains mediate localization, oligomerization, novel catalytic activity, and autoinhibition Biochemistry 39 2000 8480 8490
    • (2000) Biochemistry , vol.39 , pp. 8480-8490
    • Bush, E.W.1    Helmke, S.M.2    Birnbaum, R.A.3    Perryman, M.B.4
  • 7
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4 (Collaborative Computational Project, Number 4)
    • CCP4 (Collaborative Computational Project, Number 4) The CCP4 suite: programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 8
    • 0037066777 scopus 로고    scopus 로고
    • Characterization of RhoA-binding kinase ROKα implication of the pleckstrin homology domain in ROKα function using region-specific antibodies
    • X.Q. Chen, I. Tan, C.H. Ng, C. Hall, L. Lim, and T. Leung Characterization of RhoA-binding kinase ROKα implication of the pleckstrin homology domain in ROKα function using region-specific antibodies J. Biol. Chem. 277 2002 12680 12688
    • (2002) J. Biol. Chem. , vol.277 , pp. 12680-12688
    • Chen, X.Q.1    Tan, I.2    Ng, C.H.3    Hall, C.4    Lim, L.5    Leung, T.6
  • 9
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • S.P. Davies, H. Reddy, M. Caivano, and P. Cohen Specificity and mechanism of action of some commonly used protein kinase inhibitors Biochem. J. 351 2000 95 105
    • (2000) Biochem. J. , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 10
    • 10644234702 scopus 로고    scopus 로고
    • New insights into the structure-function relationships of Rho-associated kinase: A thermodynamic and hydrodynamic study of the dimer-to-monomer transition and its kinetic implications
    • J.D. Doran, X. Liu, P. Taslimi, A. Saadat, and T. Fox New insights into the structure-function relationships of Rho-associated kinase: a thermodynamic and hydrodynamic study of the dimer-to-monomer transition and its kinetic implications Biochem. J. 384 2004 255 262
    • (2004) Biochem. J. , vol.384 , pp. 255-262
    • Doran, J.D.1    Liu, X.2    Taslimi, P.3    Saadat, A.4    Fox, T.5
  • 11
    • 1342304087 scopus 로고    scopus 로고
    • Structural insights into the interaction of ROCKI with the switch regions of RhoA
    • R. Dvorsky, L. Blumenstein, I.R. Vetter, and M.R. Ahmadian Structural insights into the interaction of ROCKI with the switch regions of RhoA J. Biol. Chem. 279 2004 7098 7104
    • (2004) J. Biol. Chem. , vol.279 , pp. 7098-7104
    • Dvorsky, R.1    Blumenstein, L.2    Vetter, I.R.3    Ahmadian, M.R.4
  • 12
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology
    • S. Etienne-Manneville, and A. Hall Rho GTPases in cell biology Nature 420 2002 629 635
    • (2002) Nature , vol.420 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, A.2
  • 13
    • 0035150402 scopus 로고    scopus 로고
    • Rho-Rho-kinase pathway in smooth muscle contraction and cytoskeletal reorganization of non-muscle cells
    • Y. Fukata, M. Amano, and K. Kaibuchi Rho-Rho-kinase pathway in smooth muscle contraction and cytoskeletal reorganization of non-muscle cells Trends Pharmacol. Sci. 22 2001 32 39
    • (2001) Trends Pharmacol. Sci. , vol.22 , pp. 32-39
    • Fukata, Y.1    Amano, M.2    Kaibuchi, K.3
  • 14
    • 2542500761 scopus 로고    scopus 로고
    • The protein kinase C inhibitor bisindolyl maleimide 2 binds with reversed orientations to different conformations of protein kinase a
    • M. Gassel, C.B. Breitenlechner, N. König, R. Huber, R.A. Engh, and D. Bossemeyer The protein kinase C inhibitor bisindolyl maleimide 2 binds with reversed orientations to different conformations of protein kinase A J. Biol. Chem. 279 2004 23679 23690
    • (2004) J. Biol. Chem. , vol.279 , pp. 23679-23690
    • Gassel, M.1    Breitenlechner, C.B.2    König, N.3    Huber, R.4    Engh, R.A.5    Bossemeyer, D.6
  • 15
    • 23644453653 scopus 로고    scopus 로고
    • Rho kinase as potential therapeutic target for cardiovascular diseases: Opportunities and challenges
    • E. Hu, and D. Lee Rho kinase as potential therapeutic target for cardiovascular diseases: opportunities and challenges Expert Opin. Ther. Targets 9 2005 715 736
    • (2005) Expert Opin. Ther. Targets , vol.9 , pp. 715-736
    • Hu, E.1    Lee, D.2
  • 16
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • M. Huse, and J. Kuriyan The conformational plasticity of protein kinases Cell 109 2002 275 282
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 19
    • 0032860424 scopus 로고    scopus 로고
    • Regulation of the cytoskeleton and cell adhesion by the Rho family GTPases in mammalian cells
    • K. Kaibuchi, S. Kuroda, and M. Amano Regulation of the cytoskeleton and cell adhesion by the Rho family GTPases in mammalian cells Annu. Rev. Biochem. 68 1999 459 486
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 459-486
    • Kaibuchi, K.1    Kuroda, S.2    Amano, M.3
  • 21
    • 0030845843 scopus 로고    scopus 로고
    • Model building and refinement practice
    • G.J. Kleywegt, and T. Jones Model building and refinement practice Methods Enzymol. 277 1997 208 230
    • (1997) Methods Enzymol. , vol.277 , pp. 208-230
    • Kleywegt, G.J.1    Jones, T.2
  • 23
    • 0028863142 scopus 로고
    • A novel serine/threonine kinase binding the Ras-related RhoA GTPase which translocates the kinase to peripheral membranes
    • T. Leung, E. Manser, L. Tan, and L. Lim A novel serine/threonine kinase binding the Ras-related RhoA GTPase which translocates the kinase to peripheral membranes J. Biol. Chem. 270 1995 29051 29054
    • (1995) J. Biol. Chem. , vol.270 , pp. 29051-29054
    • Leung, T.1    Manser, E.2    Tan, L.3    Lim, L.4
  • 24
    • 0029789678 scopus 로고    scopus 로고
    • The p160 RhoA-binding kinase ROKα is a member of a kinase family and is involved in the reorganization of the cytoskeleton
    • T. Leung, X.Q. Chen, E. Manser, and L. Lim The p160 RhoA-binding kinase ROKα is a member of a kinase family and is involved in the reorganization of the cytoskeleton Mol. Cell. Biol. 16 1996 5313 5327
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5313-5327
    • Leung, T.1    Chen, X.Q.2    Manser, E.3    Lim, L.4
  • 27
    • 0030945871 scopus 로고    scopus 로고
    • Structures of the tyrosine kinase domain of fibroblast growth factor receptor in complex with inhibitors
    • M. Mohammadi, G. McMahon, L. Sun, C. Tang, P. Hirth, B.K. Yeh, S.R. Hubbard, and J. Schlessinger Structures of the tyrosine kinase domain of fibroblast growth factor receptor in complex with inhibitors Science 276 1997 955 960
    • (1997) Science , vol.276 , pp. 955-960
    • Mohammadi, M.1    McMahon, G.2    Sun, L.3    Tang, C.4    Hirth, P.5    Yeh, B.K.6    Hubbard, S.R.7    Schlessinger, J.8
  • 28
    • 18944372230 scopus 로고    scopus 로고
    • Rho kinase, a promising drug target for neurological disorders
    • B.K. Mueller, H. Mack, and N. Teusch Rho kinase, a promising drug target for neurological disorders Nat. Rev. Drug Discov. 4 2005 387 398
    • (2005) Nat. Rev. Drug Discov. , vol.4 , pp. 387-398
    • Mueller, B.K.1    MacK, H.2    Teusch, N.3
  • 31
    • 0037337159 scopus 로고    scopus 로고
    • Regulation of the ABC kinases by phosphorylation: Protein kinase C as a paradigm
    • A.C. Newton Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigm Biochem. J. 370 2003 361 371
    • (2003) Biochem. J. , vol.370 , pp. 361-371
    • Newton, A.C.1
  • 32
    • 4444353636 scopus 로고    scopus 로고
    • Regulation of protein kinases: Controlling activity through activation segment conformation
    • B. Nolen, S. Taylor, and G. Ghosh Regulation of protein kinases: controlling activity through activation segment conformation Mol. Cell 15 2004 661 675
    • (2004) Mol. Cell , vol.15 , pp. 661-675
    • Nolen, B.1    Taylor, S.2    Ghosh, G.3
  • 33
    • 0032988987 scopus 로고    scopus 로고
    • H-series protein kinase inhibitors and potential clinical applications
    • N. Ono-Saito, I. Niki, and H. Hidaka H-series protein kinase inhibitors and potential clinical applications Pharmacol. Ther. 82 1999 123 131
    • (1999) Pharmacol. Ther. , vol.82 , pp. 123-131
    • Ono-Saito, N.1    Niki, I.2    Hidaka, H.3
  • 34
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 35
    • 0028329918 scopus 로고
    • Release of proteins and peptides from fusion proteins using a recombinant plant virus proteinase
    • T.D. Parks, K.K. Leuther, E.D. Howard, S.A. Johnston, and W.G. Dougherty Release of proteins and peptides from fusion proteins using a recombinant plant virus proteinase Anal. Biochem. 216 1994 413 417
    • (1994) Anal. Biochem. , vol.216 , pp. 413-417
    • Parks, T.D.1    Leuther, K.K.2    Howard, E.D.3    Johnston, S.A.4    Dougherty, W.G.5
  • 36
    • 0036909402 scopus 로고    scopus 로고
    • Regulation of protein kinases in insulin, growth factor and Wnt signalling
    • L.H. Pearl, and D. Barford Regulation of protein kinases in insulin, growth factor and Wnt signalling Curr. Opin. Struct. Biol. 12 2002 761 767
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 761-767
    • Pearl, L.H.1    Barford, D.2
  • 37
    • 0033565773 scopus 로고    scopus 로고
    • Kinase phosphorylation: Keeping it all in the family
    • R.T. Peterson, and S.L. Schreiber Kinase phosphorylation: keeping it all in the family Curr. Biol. 9 1999 R521 R524
    • (1999) Curr. Biol. , vol.9
    • Peterson, R.T.1    Schreiber, S.L.2
  • 38
    • 0031574365 scopus 로고    scopus 로고
    • Staurosporine-induced conformational changes of cAMP-dependent protein kinase catalytic subunit explain inhibitory potential
    • L. Prade, R.A. Engh, A. Girod, V. Kinzel, R. Huber, and D. Bossemeyer Staurosporine-induced conformational changes of cAMP-dependent protein kinase catalytic subunit explain inhibitory potential Structure 5 1997 1627 1637
    • (1997) Structure , vol.5 , pp. 1627-1637
    • Prade, L.1    Engh, R.A.2    Girod, A.3    Kinzel, V.4    Huber, R.5    Bossemeyer, D.6
  • 39
    • 0038024241 scopus 로고    scopus 로고
    • Rocks: Multifunctional kinases in cell behaviour
    • K. Riento, and A.J. Ridley Rocks: multifunctional kinases in cell behaviour Nat. Rev. Mol. Cell Biol. 4 2003 446 456
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 446-456
    • Riento, K.1    Ridley, A.J.2
  • 41
    • 0035079891 scopus 로고    scopus 로고
    • Intermolecular and intramolecular interactions regulate catalytic activity of myotonic dystrophy kinase-related Cdc42-binding kinase α
    • I. Tan, K.T. Seow, L. Lim, and T. Leung Intermolecular and intramolecular interactions regulate catalytic activity of myotonic dystrophy kinase-related Cdc42-binding kinase α Mol. Cell. Biol. 21 2001 2767 2778
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2767-2778
    • Tan, I.1    Seow, K.T.2    Lim, L.3    Leung, T.4


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