메뉴 건너뛰기




Volumn 582, Issue 12, 2008, Pages 1637-1642

ROCK and PRK-2 mediate the inhibitory effect of Y-27632 on polyglutamine aggregation

Author keywords

Androgen receptor; Huntingtin; Neurodegeneration; Polyglutamine; PRK 2; ROCK

Indexed keywords

4 (1 AMINOETHYL) N (4 PYRIDYL)CYCLOHEXANECARBOXAMIDE; ANDROGEN RECEPTOR; FASUDIL; HUNTINGTIN; POLYGLUTAMINE; PROTEIN KINASE B BETA; RHO KINASE; RNA;

EID: 43549084329     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.04.009     Document Type: Article
Times cited : (26)

References (31)
  • 1
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • The Huntington's Disease Collaborative Research Group
    • The Huntington's Disease Collaborative Research Group. A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 72 (1993) 971-983
    • (1993) Cell , vol.72 , pp. 971-983
  • 2
    • 0025800526 scopus 로고
    • Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy
    • La Spada A.R., Wilson E.M., Lubahn D.B., Harding A.E., and Fischbeck K.H. Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophy. Nature 352 (1991) 77-79
    • (1991) Nature , vol.352 , pp. 77-79
    • La Spada, A.R.1    Wilson, E.M.2    Lubahn, D.B.3    Harding, A.E.4    Fischbeck, K.H.5
  • 4
    • 0038024241 scopus 로고    scopus 로고
    • Rocks: multifunctional kinases in cell behaviour
    • Riento K., and Ridley A.J. 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
  • 5
    • 0034715885 scopus 로고    scopus 로고
    • Regulation and functions of Rho-associated kinase
    • Amano M., Fukata Y., and Kaibuchi K. Regulation and functions of Rho-associated kinase. Exp. Cell Res. 261 (2000) 44-51
    • (2000) Exp. Cell Res. , vol.261 , pp. 44-51
    • Amano, M.1    Fukata, Y.2    Kaibuchi, K.3
  • 6
    • 18944372230 scopus 로고    scopus 로고
    • Rho kinase, a promising drug target for neurological disorders
    • Mueller B.K., Mack H., and Teusch N. 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
  • 7
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies S.P., Reddy H., Caivano M., and Cohen P. 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
  • 8
    • 0030894714 scopus 로고    scopus 로고
    • The PRK2 kinase is a potential effector target of both Rho and Rac GTPases and regulates actin cytoskeletal organization
    • Vincent S., and Settleman J. The PRK2 kinase is a potential effector target of both Rho and Rac GTPases and regulates actin cytoskeletal organization. Mol. Cell Biol. 17 (1997) 2247-2256
    • (1997) Mol. Cell Biol. , vol.17 , pp. 2247-2256
    • Vincent, S.1    Settleman, J.2
  • 9
    • 0037283966 scopus 로고    scopus 로고
    • The structure and function of PKN, a protein kinase having a catalytic domain homologous to that of PKC
    • Mukai H. The structure and function of PKN, a protein kinase having a catalytic domain homologous to that of PKC. J. Biochem. 133 (2003) 17-27
    • (2003) J. Biochem. , vol.133 , pp. 17-27
    • Mukai, H.1
  • 10
    • 0030615004 scopus 로고    scopus 로고
    • p160ROCK, a Rho-associated coiled-coil forming protein kinase, works downstream of Rho and induces focal adhesions
    • Ishizaki T., Naito M., Fujisawa K., Maekawa M., Watanabe N., Saito Y., and Narumiya S. p160ROCK, a Rho-associated coiled-coil forming protein kinase, works downstream of Rho and induces focal adhesions. FEBS Lett. 404 (1997) 118-124
    • (1997) FEBS Lett. , vol.404 , pp. 118-124
    • Ishizaki, T.1    Naito, M.2    Fujisawa, K.3    Maekawa, M.4    Watanabe, N.5    Saito, Y.6    Narumiya, S.7
  • 11
    • 0029789678 scopus 로고    scopus 로고
    • The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton
    • Leung T., Chen X.Q., Manser E., and Lim L. 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 (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
  • 13
    • 0035990918 scopus 로고    scopus 로고
    • The novel and specific Rho-kinase inhibitor (S)-(+)-2-methyl-1-[(4-methyl-5-isoquinoline)sulfonyl]-homopiperazine as a probing molecule for Rho-kinase-involved pathway
    • Sasaki Y., Suzuki M., and Hidaka H. The novel and specific Rho-kinase inhibitor (S)-(+)-2-methyl-1-[(4-methyl-5-isoquinoline)sulfonyl]-homopiperazine as a probing molecule for Rho-kinase-involved pathway. Pharmacol. Ther. 93 (2002) 225-232
    • (2002) Pharmacol. Ther. , vol.93 , pp. 225-232
    • Sasaki, Y.1    Suzuki, M.2    Hidaka, H.3
  • 14
    • 0036077667 scopus 로고    scopus 로고
    • Inhibition of rho-kinase-induced myristoylated alanine-rich C kinase substrate (MARCKS) phosphorylation in human neuronal cells by H-1152, a novel and specific Rho-kinase inhibitor
    • Ikenoya M., Hidaka H., Hosoya T., Suzuki M., Yamamoto N., and Sasaki Y. Inhibition of rho-kinase-induced myristoylated alanine-rich C kinase substrate (MARCKS) phosphorylation in human neuronal cells by H-1152, a novel and specific Rho-kinase inhibitor. J. Neurochem. 81 (2002) 9-16
    • (2002) J. Neurochem. , vol.81 , pp. 9-16
    • Ikenoya, M.1    Hidaka, H.2    Hosoya, T.3    Suzuki, M.4    Yamamoto, N.5    Sasaki, Y.6
  • 16
    • 0030603119 scopus 로고    scopus 로고
    • ROCK-I and ROCK-II, two isoforms of Rho-associated coiled-coil forming protein serine/threonine kinase in mice
    • Nakagawa O., Fujisawa K., Ishizaki T., Saito Y., Nakao K., and Narumiya S. ROCK-I and ROCK-II, two isoforms of Rho-associated coiled-coil forming protein serine/threonine kinase in mice. FEBS Lett. 392 (1996) 189-193
    • (1996) FEBS Lett. , vol.392 , pp. 189-193
    • Nakagawa, O.1    Fujisawa, K.2    Ishizaki, T.3    Saito, Y.4    Nakao, K.5    Narumiya, S.6
  • 17
    • 36249031068 scopus 로고    scopus 로고
    • Recognizing and exploiting differences between RNAi and small-molecule inhibitors
    • Weiss W.A., Taylor S.S., and Shokat K.M. Recognizing and exploiting differences between RNAi and small-molecule inhibitors. Nat. Chem. Biol. 3 (2007) 739-744
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 739-744
    • Weiss, W.A.1    Taylor, S.S.2    Shokat, K.M.3
  • 18
    • 0036460051 scopus 로고    scopus 로고
    • Rho/Rho-kinase mediated signaling in physiology and pathophysiology
    • Wettschureck N., and Offermanns S. Rho/Rho-kinase mediated signaling in physiology and pathophysiology. J. Mol. Med. 80 (2002) 629-638
    • (2002) J. Mol. Med. , vol.80 , pp. 629-638
    • Wettschureck, N.1    Offermanns, S.2
  • 19
    • 0033711895 scopus 로고    scopus 로고
    • A critical role for a Rho-associated kinase, p160ROCK, in determining axon outgrowth in mammalian CNS neurons
    • Bito H., et al. A critical role for a Rho-associated kinase, p160ROCK, in determining axon outgrowth in mammalian CNS neurons. Neuron 26 (2000) 431-441
    • (2000) Neuron , vol.26 , pp. 431-441
    • Bito, H.1
  • 20
    • 0032579378 scopus 로고    scopus 로고
    • p160 RhoA-binding kinase ROKalpha induces neurite retraction
    • Katoh H., Aoki J., Ichikawa A., and Negishi M. p160 RhoA-binding kinase ROKalpha induces neurite retraction. J. Biol. Chem. 273 (1998) 2489-2492
    • (1998) J. Biol. Chem. , vol.273 , pp. 2489-2492
    • Katoh, H.1    Aoki, J.2    Ichikawa, A.3    Negishi, M.4
  • 21
    • 14444288533 scopus 로고    scopus 로고
    • Molecular dissection of the Rho-associated protein kinase (p160ROCK)-regulated neurite remodeling in neuroblastoma N1E-115 cells
    • Hirose M., et al. Molecular dissection of the Rho-associated protein kinase (p160ROCK)-regulated neurite remodeling in neuroblastoma N1E-115 cells. J. Cell Biol. 141 (1998) 1625-1636
    • (1998) J. Cell Biol. , vol.141 , pp. 1625-1636
    • Hirose, M.1
  • 22
    • 0034604710 scopus 로고    scopus 로고
    • Phosphorylation of collapsin response mediator protein-2 by Rho-kinase. Evidence for two separate signaling pathways for growth cone collapse
    • Arimura N., et al. Phosphorylation of collapsin response mediator protein-2 by Rho-kinase. Evidence for two separate signaling pathways for growth cone collapse. J. Biol. Chem. 275 (2000) 23973-23980
    • (2000) J. Biol. Chem. , vol.275 , pp. 23973-23980
    • Arimura, N.1
  • 23
    • 0033946174 scopus 로고    scopus 로고
    • Protein kinase inhibition by fasudil hydrochloride promotes neurological recovery after spinal cord injury in rats
    • Hara M., Takayasu M., Watanabe K., Noda A., Takagi T., Suzuki Y., and Yoshida J. Protein kinase inhibition by fasudil hydrochloride promotes neurological recovery after spinal cord injury in rats. J. Neurosurg. 93 (2000) 94-101
    • (2000) J. Neurosurg. , vol.93 , pp. 94-101
    • Hara, M.1    Takayasu, M.2    Watanabe, K.3    Noda, A.4    Takagi, T.5    Suzuki, Y.6    Yoshida, J.7
  • 25
    • 0037443069 scopus 로고    scopus 로고
    • Rho kinase inhibition enhances axonal regeneration in the injured CNS
    • Fournier A.E., Takizawa B.T., and Strittmatter S.M. Rho kinase inhibition enhances axonal regeneration in the injured CNS. J. Neurosci. 23 (2003) 1416-1423
    • (2003) J. Neurosci. , vol.23 , pp. 1416-1423
    • Fournier, A.E.1    Takizawa, B.T.2    Strittmatter, S.M.3
  • 26
    • 3042552705 scopus 로고    scopus 로고
    • Cytoplasmic p21(Cip1/WAF1) enhances axonal regeneration and functional recovery after spinal cord injury in rats
    • Tanaka H., Yamashita T., Yachi K., Fujiwara T., Yoshikawa H., and Tohyama M. Cytoplasmic p21(Cip1/WAF1) enhances axonal regeneration and functional recovery after spinal cord injury in rats. Neuroscience 127 (2004) 155-164
    • (2004) Neuroscience , vol.127 , pp. 155-164
    • Tanaka, H.1    Yamashita, T.2    Yachi, K.3    Fujiwara, T.4    Yoshikawa, H.5    Tohyama, M.6
  • 27
    • 0242414463 scopus 로고    scopus 로고
    • Nonsteroidal anti-inflammatory drugs can lower amyloidogenic Abeta42 by inhibiting Rho
    • Zhou Y., et al. Nonsteroidal anti-inflammatory drugs can lower amyloidogenic Abeta42 by inhibiting Rho. Science 302 (2003) 1215-1217
    • (2003) Science , vol.302 , pp. 1215-1217
    • Zhou, Y.1
  • 28
    • 0035057192 scopus 로고    scopus 로고
    • Takanashi, Y., Ishida, T., Meguro, T., Kiwada, H., Zhang, J.H. and Yamamoto, I. (2001) Efficacy of intrathecal liposomal fasudil for experimental cerebral vasospasm after subarachnoid hemorrhage. Neurosurgery 48, 894-900 (discussion 900-1).
    • Takanashi, Y., Ishida, T., Meguro, T., Kiwada, H., Zhang, J.H. and Yamamoto, I. (2001) Efficacy of intrathecal liposomal fasudil for experimental cerebral vasospasm after subarachnoid hemorrhage. Neurosurgery 48, 894-900 (discussion 900-1).
  • 30
    • 0035150402 scopus 로고    scopus 로고
    • Rho-Rho-kinase pathway in smooth muscle contraction and cytoskeletal reorganization of non-muscle cells
    • Fukata Y., Amano M., and Kaibuchi K. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.