메뉴 건너뛰기




Volumn 45, Issue 3, 2006, Pages 243-254

Dynamics of RhoA and ROKα translocation in single living cells

Author keywords

Activation; Green fluorescent protein; Rho kinase; Small G binding protein; Translocation

Indexed keywords

PROTEIN SERINE THREONINE KINASE; RHO KINASE; RHO-ASSOCIATED KINASE; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; SIGNAL PEPTIDE;

EID: 33746424429     PISSN: 10859195     EISSN: None     Source Type: Journal    
DOI: 10.1385/CBB:45:3:243     Document Type: Article
Times cited : (12)

References (30)
  • 1
    • 0029791373 scopus 로고    scopus 로고
    • The small GTPase Rho: Cellular functions and signal transduction
    • Narumiya, S. (1996) The small GTPase Rho: cellular functions and signal transduction. J. Biochem. (Tokyo) 120, 215-228.
    • (1996) J. Biochem. (Tokyo) , vol.120 , pp. 215-228
    • Narumiya, S.1
  • 2
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall, A. (1998) Rho GTPases and the actin cytoskeleton. Science 279, 509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 3
    • 0038024241 scopus 로고    scopus 로고
    • ROCKs: Multifunctional kinases in cell behaviour
    • Riento, K. and Ridley, A. J. (2003) ROCKs: multifunctional kinases in cell behaviour. Nat. Rev. Mol. Cell Biol. 4, 446-456.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 446-456
    • Riento, K.1    Ridley, A.J.2
  • 4
    • 0033601250 scopus 로고    scopus 로고
    • Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase
    • Feng, J., Ito, M., Ichikawa, K., et al. (1999) Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase. J. Biol. Chem. 274, 37,385-37,390.
    • (1999) J. Biol. Chem. , vol.274
    • Feng, J.1    Ito, M.2    Ichikawa, K.3
  • 5
    • 0033525125 scopus 로고    scopus 로고
    • Rho-associated kinase of chicken gizzard smooth muscle
    • Feng, J., Ito, M., Kureishi, Y., et al. (1999) Rho-associated kinase of chicken gizzard smooth muscle. J. Biol. Chem. 274, 3744-3752.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3744-3752
    • Feng, J.1    Ito, M.2    Kureishi, Y.3
  • 7
    • 0034805388 scopus 로고    scopus 로고
    • Regulation by GDI of RhoA/Rho-kinase-induced Ca2+ sensitization of smooth muscle myosin II
    • Gong, M. C., Gorenne, I., Read, P., et al. (2001) Regulation by GDI of RhoA/Rho-kinase-induced Ca2+ sensitization of smooth muscle myosin II. Am. J. Physiol. Cell Physiol. 281, C257-C269.
    • (2001) Am. J. Physiol. Cell Physiol. , vol.281
    • Gong, M.C.1    Gorenne, I.2    Read, P.3
  • 8
    • 0028863142 scopus 로고
    • A novel serine/threonine kinase binding the Ras-related RhoA GTPase, which translocates the kinase to peripheral membranes
    • Leung, T., Manser, E., Tan, L., and 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, 29,051-29,054.
    • (1995) J. Biol. Chem. , vol.270
    • Leung, T.1    Manser, E.2    Tan, L.3    Lim, L.4
  • 9
    • 0035079891 scopus 로고    scopus 로고
    • Intermolecular and intramolecular interactions regulate catalytic activity of myotonic dystrophy kinase-related Cdc42-binding kinase alpha
    • Tan, I., Seow, K. T., Lim, L., and Leung, T. (2001) Intermolecular and intramolecular interactions regulate catalytic activity of myotonic dystrophy kinase-related Cdc42-binding kinase alpha. Mol. Cell Biol. 21, 2767-2778.
    • (2001) Mol. Cell Biol. , vol.21 , pp. 2767-2778
    • Tan, I.1    Seow, K.T.2    Lim, L.3    Leung, T.4
  • 10
    • 0027938294 scopus 로고
    • Structural requirement of the regulatory light chain of smooth muscle myosin as a substrate for myosin light chain kinase
    • Ikebe, M., Reardon, S., Schwonek, J. P., Sanders, C. R., and Ikebe, R. (1994) Structural requirement of the regulatory light chain of smooth muscle myosin as a substrate for myosin light chain kinase. J. Biol. Chem. 269, 28,165-28,172.
    • (1994) J. Biol. Chem. , vol.269
    • Ikebe, M.1    Reardon, S.2    Schwonek, J.P.3    Sanders, C.R.4    Ikebe, R.5
  • 11
    • 0032504192 scopus 로고    scopus 로고
    • A hinge at the central helix of the regulatory light chain of myosin is critical for phosphorylation-dependent regulation of smooth muscle myosin motor activity
    • Ikebe, M., Kambara, T., Stafford, W. F., Sata, M., Katayama, E., and Ikebe, R. (1998) A hinge at the central helix of the regulatory light chain of myosin is critical for phosphorylation-dependent regulation of smooth muscle myosin motor activity. J. Biol. Chem. 273, 17,702-17,707.
    • (1998) J. Biol. Chem. , vol.273
    • Ikebe, M.1    Kambara, T.2    Stafford, W.F.3    Sata, M.4    Katayama, E.5    Ikebe, R.6
  • 12
    • 0037270157 scopus 로고    scopus 로고
    • Agonist-induced changes in the phosphorylation of the myosin-binding subunit of myosin light chain phosphatase and CPI17, two regulatory factors of myosin light chain phosphatase, in smooth muscle
    • Niiro, N., Koga, Y., and Ikebe, M. (2003) Agonist-induced changes in the phosphorylation of the myosin-binding subunit of myosin light chain phosphatase and CPI17, two regulatory factors of myosin light chain phosphatase, in smooth muscle. Biochem. J. 369, 117-128.
    • (2003) Biochem. J. , vol.369 , pp. 117-128
    • Niiro, N.1    Koga, Y.2    Ikebe, M.3
  • 13
    • 0027422816 scopus 로고
    • Boundary of the autoinhibitory region of smooth muscle myosin light chain kinase
    • Yano, K., Araki, Y., Hales, S. J., Tanaka, M., and Ikebe, M. (1993) Boundary of the autoinhibitory region of smooth muscle myosin light chain kinase. Biochemistry 32, 12,054-12,061.
    • (1993) Biochemistry , vol.32
    • Yano, K.1    Araki, Y.2    Hales, S.J.3    Tanaka, M.4    Ikebe, M.5
  • 14
    • 0026345394 scopus 로고
    • Protein kinase catalytic domain sequence database: Identification of conserved features of primary structure and classification of family members
    • Hanks, S. K. and Quinn, A. M. (1991) Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. Methods Enzymol. 200, 38-62.
    • (1991) Methods Enzymol. , vol.200 , pp. 38-62
    • Hanks, S.K.1    Quinn, A.M.2
  • 15
    • 0030615004 scopus 로고    scopus 로고
    • p160ROCK, a Rho-associated coiled-coil forming protein kinase, downstream of Rho and induces focal adhesions
    • Ishizaki, T., Naito, M., Fujisawa, K., et al. (1997) p160ROCK, a Rho-associated coiled-coil forming protein kinase, downstream of Rho and induces focal adhesions. FEBS Lett. 404, 118-124.
    • (1997) FEBS Lett. , vol.404 , pp. 118-124
    • Ishizaki, T.1    Naito, M.2    Fujisawa, K.3
  • 16
    • 0029789323 scopus 로고    scopus 로고
    • Identification of the Rho-binding domain of p160ROCK, a Rho-associated coiled-coil containing protein kinase
    • Fujisawa, K., Fujita, A., Ishizaki, T., Saito, Y., and Narumiya, S. (1996) Identification of the Rho-binding domain of p160ROCK, a Rho-associated coiled-coil containing protein kinase. J. Biol. Chem. 271, 23,022-23,028.
    • (1996) J. Biol. Chem. , vol.271
    • Fujisawa, K.1    Fujita, A.2    Ishizaki, T.3    Saito, Y.4    Narumiya, S.5
  • 17
    • 0000315614 scopus 로고    scopus 로고
    • Dissociation of LPA-induced cytoskeletal contraction from stress fiber formation by differential localization of RhoA
    • Kranenburg, O., Poland, M., Gebbink, M., Oomen, L., and Moolenaar, W. H. (1997) Dissociation of LPA-induced cytoskeletal contraction from stress fiber formation by differential localization of RhoA. J. Cell Sci. 110, 2417-2427.
    • (1997) J. Cell Sci. , vol.110 , pp. 2417-2427
    • Kranenburg, O.1    Poland, M.2    Gebbink, M.3    Oomen, L.4    Moolenaar, W.H.5
  • 18
    • 0022270772 scopus 로고
    • 2+ on the conformation and enzymatic activity of smooth muscle myosin
    • 2+ on the conformation and enzymatic activity of smooth muscle myosin. J. Biol. Chem. 260, 13,146-13,153.
    • (1985) J. Biol. Chem. , vol.260
    • Ikebe, M.1    Hartshorne, D.J.2
  • 19
    • 12644264656 scopus 로고    scopus 로고
    • Differential translocation of rho family GTPases by lysophosphatidic acid, endothelin-1, and platelet-derived growth factor
    • 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, 33,067-33,073.
    • (1996) J. Biol. Chem. , vol.271
    • Fleming, I.N.1    Elliott, C.M.2    Exton, J.H.3
  • 20
    • 0037181495 scopus 로고    scopus 로고
    • Dephosphorylation of the two regulatory components of myosin phosphatase, MBS and CPI17
    • Takizawa, N., Niiro, N., and Ikebe, M. (2002) Dephosphorylation of the two regulatory components of myosin phosphatase, MBS and CPI17. FEBS Lett. 515, 127-132.
    • (2002) FEBS Lett. , vol.515 , pp. 127-132
    • Takizawa, N.1    Niiro, N.2    Ikebe, M.3
  • 21
    • 0030656619 scopus 로고    scopus 로고
    • Calcium sensitization of smooth muscle mediated by a Rho-associated protein kinase in hypertension
    • Uehata, M., Ishizaki, T., Satoh, H., et al. (1997) Calcium sensitization of smooth muscle mediated by a Rho-associated protein kinase in hypertension. Nature 389, 990-994.
    • (1997) Nature , vol.389 , pp. 990-994
    • Uehata, M.1    Ishizaki, T.2    Satoh, H.3
  • 22
    • 0037016742 scopus 로고    scopus 로고
    • Rho-dependent agonist-induced spatio-temporal change in myosin phosphorylation in smooth muscle cells
    • Miyazaki, K., Yano, T., Schmidt, D. J., et al. (2002) Rho-dependent agonist-induced spatio-temporal change in myosin phosphorylation in smooth muscle cells. J. Biol. Chem. 277, 725-734.
    • (2002) J. Biol. Chem. , vol.277 , pp. 725-734
    • Miyazaki, K.1    Yano, T.2    Schmidt, D.J.3
  • 23
    • 0028043535 scopus 로고
    • Signal transduction and regulation in smooth muscle
    • Somlyo, A. P. and Somlyo, A. V. (1994) Signal transduction and regulation in smooth muscle. Nature 372, 231-236.
    • (1994) Nature , vol.372 , pp. 231-236
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 24
    • 0032502680 scopus 로고    scopus 로고
    • Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein beta subunits and the yeast response regulator protein Skn7
    • Alberts, A. S., Bouquin, N., Johnston, L. H., and Treisman, R. (1998) Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein beta subunits and the yeast response regulator protein Skn7. J. Biol. Chem. 273, 8616-8622.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8616-8622
    • Alberts, A.S.1    Bouquin, N.2    Johnston, L.H.3    Treisman, R.4
  • 25
    • 0034663568 scopus 로고    scopus 로고
    • Signal-dependent membrane targeting by pleckstrin homology (PH) domains
    • Lemmon, M. A. and Ferguson, K. M. (2000) Signal-dependent membrane targeting by pleckstrin homology (PH) domains. Biochem. J. 350, 1-18.
    • (2000) Biochem. J. , vol.350 , pp. 1-18
    • Lemmon, M.A.1    Ferguson, K.M.2
  • 26
    • 0037066777 scopus 로고    scopus 로고
    • Characterization of RhoA-binding kinase ROKalpha implication of the pleckstrin homology domain in ROKalpha function using region-specific antibodies
    • Chen, X. Q., Tan, I., Ng, C. H., Hall, C., Lim, L., and Leung, T. (2002) Characterization of RhoA-binding kinase ROKalpha implication of the pleckstrin homology domain in ROKalpha function using region-specific antibodies. J. Biol. Chem. 277, 12,680-12,688.
    • (2002) J. Biol. Chem. , vol.277
    • Chen, X.Q.1    Tan, I.2    Ng, C.H.3    Hall, C.4    Lim, L.5    Leung, T.6
  • 27
    • 9244220646 scopus 로고    scopus 로고
    • The small GTP-binding protein Rho binds to and activates a 160 kDa Ser/Thr protein kinase homologous to myotonic dystrophy kinase
    • Ishizaki, T., Maekawa, M., Fujisawa, K., 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.
    • (1996) EMBO J. , vol.15 , pp. 1885-1893
    • Ishizaki, T.1    Maekawa, M.2    Fujisawa, K.3
  • 28
    • 0141615707 scopus 로고    scopus 로고
    • GTPase regulation: Getting aRnd Rock and Rho inhibition
    • Chardin, P. (2003) GTPase regulation: getting aRnd Rock and Rho inhibition. Curr. Biol. 13, R702-R704.
    • (2003) Curr. Biol. , vol.13
    • Chardin, P.1
  • 29
    • 0037092045 scopus 로고    scopus 로고
    • The GTP binding proteins Gem and Rad are negative regulators of the Rho-Rho kinase pathway
    • Ward, Y., Yap, S. F., Ravichandran, V., et al. (2002) The GTP binding proteins Gem and Rad are negative regulators of the Rho-Rho kinase pathway. J. Cell Biol. 157, 291-302.
    • (2002) J. Cell Biol. , vol.157 , pp. 291-302
    • Ward, Y.1    Yap, S.F.2    Ravichandran, V.3
  • 30
    • 0038655599 scopus 로고    scopus 로고
    • RhoE binds to ROCK I and inhibits downstream signaling
    • Riento, K., Guasch, R. M., Garg, R., Jin, B., and Ridley A. J. (2003) RhoE binds to ROCK I and inhibits downstream signaling. Mol. Cell Biol. 23, 4219-4229.
    • (2003) Mol. Cell Biol. , vol.23 , pp. 4219-4229
    • Riento, K.1    Guasch, R.M.2    Garg, R.3    Jin, B.4    Ridley, A.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.