메뉴 건너뛰기




Volumn 306, Issue 2, 2003, Pages 382-387

Phosphorylation of protein phosphatase type-1 inhibitory proteins by integrin-linked kinase and cyclic nucleotide-dependent protein kinases

Author keywords

C kinase enhanced (potentiated) phosphatase inhibitors (CPI 17 and KEPI); Myosin phosphatase; Protein kinase A; Protein kinase G

Indexed keywords

C KINASE PROTEIN PHOSPHATASE 1 INHIBITOR; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIC GMP DEPENDENT PROTEIN KINASE; CYCLIC NUCLEOTIDE; HOLOENZYME; INTEGRIN; KINASE ENHANCED PROTEIN PHOSPHATASE 1 INHIBITOR; PHOSPHATASE; PHOSPHATASE HOLOENZYME INHIBITOR 1; PHOSPHOPROTEIN PHOSPHATASE INHIBITOR; PHOSPHOTRANSFERASE; PROTEIN KINASE; UNCLASSIFIED DRUG;

EID: 0037532608     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)00976-8     Document Type: Article
Times cited : (37)

References (30)
  • 1
    • 0024397415 scopus 로고
    • The structure and regulation of protein phosphatases
    • Cohen P. The structure and regulation of protein phosphatases. Annu. Rev. Biochem. 58:1989;453-508.
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 453-508
    • Cohen, P.1
  • 2
    • 0026695872 scopus 로고
    • The structure, role and regulation of type 1 protein phosphatases
    • Bollen M., Stalmans W. The structure, role and regulation of type 1 protein phosphatases. Crit. Rev. Biochem. Mol. Biol. 27:1992;227-281.
    • (1992) Crit. Rev. Biochem. Mol. Biol. , vol.27 , pp. 227-281
    • Bollen, M.1    Stalmans, W.2
  • 3
    • 0027143725 scopus 로고
    • Protein serine/threonine phosphatases: Structure, regulation, and function in cell growth
    • Mumby M.C., Walter G. Protein serine/threonine phosphatases: structure, regulation, and function in cell growth. Physiol. Rev. 73:1993;673-699.
    • (1993) Physiol. Rev. , vol.73 , pp. 673-699
    • Mumby, M.C.1    Walter, G.2
  • 4
    • 0001919787 scopus 로고    scopus 로고
    • Comparative analysis of Ser/Thr protein phosphatases
    • Dombrádi V. Comparative analysis of Ser/Thr protein phosphatases. Trends Comp. Biochem. Physiol. 3:1997;23-48.
    • (1997) Trends Comp. Biochem. Physiol. , vol.3 , pp. 23-48
    • Dombrádi, V.1
  • 5
    • 0029583638 scopus 로고
    • A novel protein phosphatase-1 inhibitory protein potentiated by protein kinase C. Isolation from porcine aorta media and characterization
    • Eto M., Ohmori T., Suzuki M., Furuya K., Morita F. A novel protein phosphatase-1 inhibitory protein potentiated by protein kinase C. Isolation from porcine aorta media and characterization. J. Biochem. (Tokyo). 118:1995;1104-1107.
    • (1995) J. Biochem. (Tokyo) , vol.118 , pp. 1104-1107
    • Eto, M.1    Ohmori, T.2    Suzuki, M.3    Furuya, K.4    Morita, F.5
  • 6
    • 0030795828 scopus 로고    scopus 로고
    • Molecular cloning of a novel phosphorylation-dependent inhibitory protein of protein phosphatase-1 (CPI17) in smooth muscle: Its specific localization in smooth muscle
    • Eto M., Senba S., Morita F., Yazawa M. Molecular cloning of a novel phosphorylation-dependent inhibitory protein of protein phosphatase-1 (CPI17) in smooth muscle: its specific localization in smooth muscle. FEBS Lett. 410:1997;356-360.
    • (1997) FEBS Lett. , vol.410 , pp. 356-360
    • Eto, M.1    Senba, S.2    Morita, F.3    Yazawa, M.4
  • 8
    • 0037137711 scopus 로고    scopus 로고
    • Cerebellar long-term synaptic depression requires PKC-mediated activation of CPI-17, a myosin/moesin phosphatase inhibitor
    • Eto M., Bock R., Brautigan D.L., Linden D.J. Cerebellar long-term synaptic depression requires PKC-mediated activation of CPI-17, a myosin/moesin phosphatase inhibitor. Neuron. 36:2002;1145-1158.
    • (2002) Neuron , vol.36 , pp. 1145-1158
    • Eto, M.1    Bock, R.2    Brautigan, D.L.3    Linden, D.J.4
  • 9
    • 0033593066 scopus 로고    scopus 로고
    • A novel phosphoprotein inhibitor of protein type-1 phosphatase holoenzymes
    • Eto M., Karginov A., Brautigan D.L. A novel phosphoprotein inhibitor of protein type-1 phosphatase holoenzymes. Biochemistry. 38:1999;16952-16957.
    • (1999) Biochemistry , vol.38 , pp. 16952-16957
    • Eto, M.1    Karginov, A.2    Brautigan, D.L.3
  • 10
    • 0037066747 scopus 로고    scopus 로고
    • KEPI, a PKC-dependent protein phosphatase 1 inhibitor regulated by morphine
    • Liu Q.R., Zhang P.W., Zhen Q., Walther D., Wang X.B., Uhl G.R. KEPI, a PKC-dependent protein phosphatase 1 inhibitor regulated by morphine. J. Biol. Chem. 277:2002;13312-13320.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13312-13320
    • Liu, Q.R.1    Zhang, P.W.2    Zhen, Q.3    Walther, D.4    Wang, X.B.5    Uhl, G.R.6
  • 11
    • 0035860716 scopus 로고    scopus 로고
    • Activation of myosin light chain phosphatase in intact arterial smooth muscle during nitric oxide-induced relaxation
    • Etter E.F., Eto M., Wardle R.L., Brautigan D.L., Murphy R.A. Activation of myosin light chain phosphatase in intact arterial smooth muscle during nitric oxide-induced relaxation. J. Biol. Chem. 276:2001;34681-34685.
    • (2001) J. Biol. Chem. , vol.276 , pp. 34681-34685
    • Etter, E.F.1    Eto, M.2    Wardle, R.L.3    Brautigan, D.L.4    Murphy, R.A.5
  • 12
    • 0034650714 scopus 로고    scopus 로고
    • Signal transduction by G-proteins, rho-kinase and protein phosphatase to smooth muscle and non-muscle myosin II
    • Somlyo A.P., Somlyo A.V. Signal transduction by G-proteins, rho-kinase and protein phosphatase to smooth muscle and non-muscle myosin II. J. Physiol. 522:2000;177-185.
    • (2000) J. Physiol. , vol.522 , pp. 177-185
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 13
    • 0031798554 scopus 로고    scopus 로고
    • Myosin light chain phosphatase: Subunit composition, interactions and regulation
    • Hartshorne D.J., Ito M., Erdodi F. Myosin light chain phosphatase: subunit composition, interactions and regulation. J. Muscle Res. Cell Motil. 19:1998;325-341.
    • (1998) J. Muscle Res. Cell Motil. , vol.19 , pp. 325-341
    • Hartshorne, D.J.1    Ito, M.2    Erdodi, F.3
  • 14
    • 0033601250 scopus 로고    scopus 로고
    • Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase
    • Feng J., Ito M., Ichikawa K., Isaka N., Nishikawa M., Hartshorne D.J., Nakano T. Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase. J. Biol. Chem. 274:1999;37385-37390.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37385-37390
    • Feng, J.1    Ito, M.2    Ichikawa, K.3    Isaka, N.4    Nishikawa, M.5    Hartshorne, D.J.6    Nakano, T.7
  • 16
    • 0027049145 scopus 로고
    • The control of protein phosphatase-1 by targetting subunits. The major myosin phosphatase in avian smooth muscle is a novel form of protein phosphatase-1
    • Alessi D., MacDougall L.K., Sola M.M., Ikebe M., Cohen P. The control of protein phosphatase-1 by targetting subunits. The major myosin phosphatase in avian smooth muscle is a novel form of protein phosphatase-1. Eur. J. Biochem. 210:1992;1023-1035.
    • (1992) Eur. J. Biochem. , vol.210 , pp. 1023-1035
    • Alessi, D.1    MacDougall, L.K.2    Sola, M.M.3    Ikebe, M.4    Cohen, P.5
  • 17
    • 0032993518 scopus 로고    scopus 로고
    • Identification of trimeric myosin phosphatase (PP1M) as a target for a novel PKC-potentiated protein phosphatase-1 inhibitory protein (CPI17) in porcine aorta smooth muscle
    • Senba S., Eto M., Yazawa M. Identification of trimeric myosin phosphatase (PP1M) as a target for a novel PKC-potentiated protein phosphatase-1 inhibitory protein (CPI17) in porcine aorta smooth muscle. J. Biochem. (Tokyo). 125:1999;354-362.
    • (1999) J. Biochem. (Tokyo) , vol.125 , pp. 354-362
    • Senba, S.1    Eto, M.2    Yazawa, M.3
  • 18
    • 0034705765 scopus 로고    scopus 로고
    • Phosphorylation of CPI-17, an inhibitory phosphoprotein of smooth muscle myosin phosphatase, by Rho-kinase
    • Koyama M., Ito M., Feng J., Seko T., Shiraki K., Takase K., Hartshorne D.J., Nakano T. Phosphorylation of CPI-17, an inhibitory phosphoprotein of smooth muscle myosin phosphatase, by Rho-kinase. FEBS Lett. 475:2000;197-200.
    • (2000) FEBS Lett. , vol.475 , pp. 197-200
    • Koyama, M.1    Ito, M.2    Feng, J.3    Seko, T.4    Shiraki, K.5    Takase, K.6    Hartshorne, D.J.7    Nakano, T.8
  • 20
    • 0035970713 scopus 로고    scopus 로고
    • Dual Ser and Thr phosphorylation of CPI-17, an inhibitor of myosin phosphatase, by MYPT-associated kinase
    • MacDonald J.A., Eto M., Borman M.A., Brautigan D.L., Haystead T.A.J. Dual Ser and Thr phosphorylation of CPI-17, an inhibitor of myosin phosphatase, by MYPT-associated kinase. FEBS Lett. 493:2001;91-94.
    • (2001) FEBS Lett. , vol.493 , pp. 91-94
    • MacDonald, J.A.1    Eto, M.2    Borman, M.A.3    Brautigan, D.L.4    Haystead, T.A.J.5
  • 21
    • 0037109063 scopus 로고    scopus 로고
    • Phosphorylation of the myosin phosphatase inhibitors, CPI-17 and PHI-1, by integrin-linked kinase
    • Deng J.T., Sutherland C., Brautigan D.L., Eto M., Walsh M.P. Phosphorylation of the myosin phosphatase inhibitors, CPI-17 and PHI-1, by integrin-linked kinase. Biochem. J. 367:2002;517-524.
    • (2002) Biochem. J. , vol.367 , pp. 517-524
    • Deng, J.T.1    Sutherland, C.2    Brautigan, D.L.3    Eto, M.4    Walsh, M.P.5
  • 22
  • 24
  • 25
    • 0035955681 scopus 로고    scopus 로고
    • Defining the structural determinants and a potential mechanism for inhibition of myosin phosphatase by the protein kinase C-potentiated inhibitor protein of 17 kDa
    • Hayashi Y., Senba S., Yazawa M., Brautigan D.L., Eto M. Defining the structural determinants and a potential mechanism for inhibition of myosin phosphatase by the protein kinase C-potentiated inhibitor protein of 17. kDa J. Biol. Chem. 276:2001;39858-39863.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39858-39863
    • Hayashi, Y.1    Senba, S.2    Yazawa, M.3    Brautigan, D.L.4    Eto, M.5
  • 26
    • 0034616292 scopus 로고    scopus 로고
    • Agonists trigger G protein-mediated activation of the CPI-17 inhibitor phosphoprotein of myosin light chain phosphatase to enhance vascular smooth muscle contractility
    • Kitazawa T., Eto M., Woodsome T.P., Brautigan D.L. Agonists trigger G protein-mediated activation of the CPI-17 inhibitor phosphoprotein of myosin light chain phosphatase to enhance vascular smooth muscle contractility. J. Biol. Chem. 275:2000;9897-9900.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9897-9900
    • Kitazawa, T.1    Eto, M.2    Woodsome, T.P.3    Brautigan, D.L.4
  • 27
    • 0034602531 scopus 로고    scopus 로고
    • Phosphorylation of MYPT1 by protein kinase C attenuates interaction with PP1 catalytic subunit and the 20 kDa light chain of myosin
    • Tóth A., Kiss E., Gergely P., Walsh M.P., Hartshorne D.J., Erdodi F. Phosphorylation of MYPT1 by protein kinase C attenuates interaction with PP1 catalytic subunit and the 20. kDa light chain of myosin FEBS Lett. 484:2000;113-117.
    • (2000) FEBS Lett. , vol.484 , pp. 113-117
    • Tóth, A.1    Kiss, E.2    Gergely, P.3    Walsh, M.P.4    Hartshorne, D.J.5    Erdodi, F.6
  • 29
    • 0036646489 scopus 로고    scopus 로고
    • Integrin-linked kinase phosphorylates the myosin phosphatase target subunit at the inhibitory site in platelet cytoskeleton
    • Kiss E., Murányi A., Csortos C., Gergely P., Ito M., Hartshorne D.J., Erdodi F. Integrin-linked kinase phosphorylates the myosin phosphatase target subunit at the inhibitory site in platelet cytoskeleton. Biochem. J. 365:2002;79-87.
    • (2002) Biochem. J. , vol.365 , pp. 79-87
    • Kiss, E.1    Murányi, A.2    Csortos, C.3    Gergely, P.4    Ito, M.5    Hartshorne, D.J.6    Erdodi, F.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.