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Volumn 288, Issue 11, 2013, Pages 7596-7605

Signaling through myosin light chain kinase in smooth muscles

Author keywords

[No Author keywords available]

Indexed keywords

CONTRACTILE DYSFUNCTION; DIFFERENTIAL CONTRIBUTION; INHIBITOR PROTEINS; MUSCARINIC AGONISTS; MYOSIN LIGHT CHAIN KINASE; MYOSIN LIGHT CHAIN PHOSPHATASE; REGULATORY LIGHT CHAINS; REGULATORY SUBUNITS;

EID: 84875155465     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.427112     Document Type: Article
Times cited : (61)

References (61)
  • 1
    • 39449101285 scopus 로고    scopus 로고
    • Nonmuscle myosin II moves in new directions
    • Conti, M. A., and Adelstein, R. S. (2008) Nonmuscle myosin II moves in new directions. J. Cell Sci. 121, 11-18
    • (2008) J.Cell Sci. , vol.121 , pp. 11-18
    • Conti, M.A.1    Adelstein, R.S.2
  • 2
    • 77952787533 scopus 로고    scopus 로고
    • Common structural motifs for the regulation of divergent class II myosins
    • Lowey, S., and Trybus, K. M. (2010) Common Structural Motifs for the Regulation of Divergent Class II Myosins. J. Biol. Chem. 285, 16403-16407
    • (2010) J. Biol. Chem. , vol.285 , pp. 16403-16407
    • Lowey, S.1    Trybus, K.M.2
  • 3
    • 0035895901 scopus 로고    scopus 로고
    • Dedicated myosin light chain kinases with diverse cellular functions
    • Kamm, K. E., and Stull, J. T. (2001) Dedicated myosin light chain kinases with diverse cellular functions. J. Biol. Chem. 276, 4527-4530
    • (2001) J. Biol. Chem. , vol.276 , pp. 4527-4530
    • Kamm, K.E.1    Stull, J.T.2
  • 6
    • 0021894617 scopus 로고
    • The function of myosin and myosin light chain kinase phosphorylation in smooth muscle
    • Kamm, K. E., and Stull, J. T. (1985) The function of myosin and myosin light chain kinase phosphorylation in smooth muscle. Annu. Rev. Pharmacol. Toxicol. 25, 593-620
    • (1985) Annu. Rev. Pharmacol. Toxicol. , vol.25 , pp. 593-620
    • Kamm, K.E.1    Stull, J.T.2
  • 7
    • 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., and Somlyo, A. V. (2000) Signal transduction by G-proteins, rho-kinase and protein phosphatase to smooth muscle and non-muscle myosin II. J. Physiol. 522, 177-185
    • (2000) J. Physiol. , vol.522 , pp. 177-185
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 8
    • 40849097955 scopus 로고    scopus 로고
    • Myosin phosphatase target subunit: Many roles in cell function
    • Matsumura, F., and Hartshorne, D. J. (2008) Myosin phosphatase target subunit: Many roles in cell function. Biochem. Biophys. Res. Commun. 369, 149-156
    • (2008) Biochem. Biophys. Res. Commun. , vol.369 , pp. 149-156
    • Matsumura, F.1    Hartshorne, D.J.2
  • 9
    • 4444303564 scopus 로고    scopus 로고
    • Role of protein phosphatase Type 1 in contractile functions: Myosin phosphatase
    • Hartshorne, D. J., Ito, M., and Erdödi, F. (2004) Role of protein phosphatase Type 1 in contractile functions: Myosin phosphatase. J. Biol. Chem. 279, 37211-37214
    • (2004) J. Biol. Chem. , vol.279 , pp. 37211-37214
    • Hartshorne, D.J.1    Ito, M.2    Erdödi, F.3
  • 10
    • 0141751697 scopus 로고    scopus 로고
    • 2+-sensitivity of smooth and non-muscle myosin II: Modulation by G Proteins, kinases and myosin phosphatase
    • 2+-sensitivity of smooth and non-muscle myosin II: modulation by G Proteins, kinases and myosin phosphatase. Physiol. Rev. 83, 1325-1358
    • (2003) Physiol. Rev. , vol.83 , pp. 1325-1358
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 12
    • 77957663118 scopus 로고    scopus 로고
    • 2+-sensitization of CPI-17 phosphorylation in arterial smooth muscle
    • 2+-sensitization of CPI-17 phosphorylation in arterial smooth muscle. Biochem. Biophys. Res. Comm. 401, 75-78
    • (2010) Biochem. Biophys. Res. Comm. , vol.401 , pp. 75-78
    • Kitazawa, T.1
  • 13
    • 79958753913 scopus 로고    scopus 로고
    • The myosin phosphatase targeting protein (MYPT) family: A regulated mechanism for achieving substrate specificity of the catalytic subunit of protein phosphatase type 1δ
    • Grassie, M. E., Moffat, L. D., Walsh, M. P., and MacDonald, J. A. (2011) The myosin phosphatase targeting protein (MYPT) family: a regulated mechanism for achieving substrate specificity of the catalytic subunit of protein phosphatase type 1δ. Arch. Biochem. Biophys. 510, 147-159
    • (2011) Arch. Biochem. Biophys. , vol.510 , pp. 147-159
    • Grassie, M.E.1    Moffat, L.D.2    Walsh, M.P.3    Macdonald, J.A.4
  • 14
    • 33645957353 scopus 로고    scopus 로고
    • Signaling for contraction and relaxation in smooth muscle of the gut
    • Murthy, K. S. (2006) Signaling for contraction and relaxation in smooth muscle of the gut. Ann. Rev. Physiol. 68, 345-374
    • (2006) Ann. Rev. Physiol. , vol.68 , pp. 345-374
    • Murthy, K.S.1
  • 15
    • 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., and Brautigan, D. L. (2000) 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, 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
  • 16
    • 0038303504 scopus 로고    scopus 로고
    • Protein kinase network in the regulation of phosphorylation and dephosphorylation of smooth muscle myosin light chain
    • Hirano, K., Derkach, D. N., Hirano, M., Nishimura, J., and Kanaide, H. (2003) Protein kinase network in the regulation of phosphorylation and dephosphorylation of smooth muscle myosin light chain. Mol. Cell Biochem. 248, 105-114
    • (2003) Mol. Cell Biochem. , vol.248 , pp. 105-114
    • Hirano, K.1    Derkach, D.N.2    Hirano, M.3    Nishimura, J.4    Kanaide, H.5
  • 19
    • 0026692912 scopus 로고
    • Myosin light chain phosphatase activities and the effects of phosphatase inhibitors in tonic and phasic smooth muscle
    • Gong, M. C., Cohen, P., Kitazawa, T., Ikebe, M., Masuo, M., Somlyo, A. P., and Somlyo, A. V. (1992) Myosin light chain phosphatase activities and the effects of phosphatase inhibitors in tonic and phasic smooth muscle. J. Biol. Chem. 267, 14662-14668
    • (1992) J. Biol. Chem. , vol.267 , pp. 14662-14668
    • Gong, M.C.1    Cohen, P.2    Kitazawa, T.3    Ikebe, M.4    Masuo, M.5    Somlyo, A.P.6    Somlyo, A.V.7
  • 22
    • 0028786311 scopus 로고
    • Kinetics of prephosphorylation reactions and myosin light chain phosphorylation in smooth muscle. Flash photolysis studies with caged calcium and caged ATP
    • Zimmermann, B., Somlyo, A. V., Ellis-Davies, G. C., Kaplan, J. H., and Somlyo, A. P. (1995) Kinetics of prephosphorylation reactions and myosin light chain phosphorylation in smooth muscle. Flash photolysis studies with caged calcium and caged ATP. J. Biol. Chem. 270, 23966-23974
    • (1995) J. Biol. Chem. , vol.270 , pp. 23966-23974
    • Zimmermann, B.1    Somlyo, A.V.2    Ellis-Davies, G.C.3    Kaplan, J.H.4    Somlyo, A.P.5
  • 25
    • 0041589199 scopus 로고    scopus 로고
    • Intracellular coupling via limiting calmodulin
    • Tran, Q. K., Black, D. J., and Persechini, A. (2003) Intracellular coupling via limiting calmodulin. J. Biol. Chem. 278, 24247-24250
    • (2003) J. Biol. Chem. , vol.278 , pp. 24247-24250
    • Tran, Q.K.1    Black, D.J.2    Persechini, A.3
  • 26
    • 84867479200 scopus 로고    scopus 로고
    • Signaling to contractile proteins by muscarinic and purinergic pathways in neurally stimulated bladder smooth muscle
    • Tsai, M. H., Kamm, K. E., and Stull, J. T. (2012) Signaling to contractile proteins by muscarinic and purinergic pathways in neurally stimulated bladder smooth muscle. J. Physiol. 590, 5107-5121
    • (2012) J. Physiol. , vol.590 , pp. 5107-5121
    • Tsai, M.H.1    Kamm, K.E.2    Stull, J.T.3
  • 30
    • 0034119477 scopus 로고    scopus 로고
    • Maturational differences between vascular and bladder smooth muscle during ovine development
    • Arens, Y. H., Rosenfeld, C. R., and Kamm, K. E. (2000) Maturational differences between vascular and bladder smooth muscle during ovine development. Am. J. Physiol. Regul. Integr. Comp. Physiol. 278, R1305-1313
    • (2000) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.278
    • Arens, Y.H.1    Rosenfeld, C.R.2    Kamm, K.E.3
  • 31
    • 0037144531 scopus 로고    scopus 로고
    • Properties of long myosin light chain kinase binding to F-actin in vitro and in vivo
    • Smith, L., Parizi-Robinson, M., Zhu, M. S., Zhi, G., Fukui, R., Kamm, K. E., and Stull, J. T. (2002) Properties of long myosin light chain kinase binding to F-actin in vitro and in vivo. J. Biol. Chem. 277, 35597-35604
    • (2002) J. Biol. Chem. , vol.277 , pp. 35597-35604
    • Smith, L.1    Parizi-Robinson, M.2    Zhu, M.S.3    Zhi, G.4    Fukui, R.5    Kamm, K.E.6    Stull, J.T.7
  • 32
    • 0024791474 scopus 로고
    • Phosphorylation of smooth muscle myosin heavy and light chains. Effects of phorbol dibutyrate and agonists
    • Kamm, K. E., Hsu, L. C., Kubota, Y., and Stull, J. T. (1989) Phosphorylation of smooth muscle myosin heavy and light chains. Effects of phorbol dibutyrate and agonists. J. Biol. Chem. 264, 21223-21229
    • (1989) J. Biol. Chem. , vol.264 , pp. 21223-21229
    • Kamm, K.E.1    Hsu, L.C.2    Kubota, Y.3    Stull, J.T.4
  • 33
    • 0028114606 scopus 로고
    • Molecular cloning of cDNA encoding the 110 kDa and 21 kDa regulatory subunits of smooth muscle protein phosphatase 1M
    • Chen, Y. H., Chen, M. X., Alessi, D. R., Campbell, D. G., Shanahan, C., Cohen, P., and Cohen, P. T. (1994) Molecular cloning of cDNA encoding the 110 kDa and 21 kDa regulatory subunits of smooth muscle protein phosphatase 1M. FEBS Lett. 356, 51-55
    • (1994) FEBS Lett. , vol.356 , pp. 51-55
    • Chen, Y.H.1    Chen, M.X.2    Alessi, D.R.3    Campbell, D.G.4    Shanahan, C.5    Cohen, P.6    Cohen, P.T.7
  • 36
    • 80054705200 scopus 로고    scopus 로고
    • Chemical genetics of zipper-interacting protein kinase reveal myosin light chain as a bona fide substrate in permeabilized arterial smooth muscle
    • Moffat, L. D., Brown, S. B., Grassie, M. E., Ulke-Lemée, A., Williamson, L. M., Walsh, M. P., and MacDonald, J. A. (2011) Chemical genetics of zipper-interacting protein kinase reveal myosin light chain as a bona fide substrate in permeabilized arterial smooth muscle. J. Biol. Chem. 286, 36978-36991
    • (2011) J. Biol. Chem. , vol.286 , pp. 36978-36991
    • Moffat, L.D.1    Brown, S.B.2    Grassie, M.E.3    Ulke-Lemée, A.4    Williamson, L.M.5    Walsh, M.P.6    Macdonald, J.A.7
  • 37
    • 55349124996 scopus 로고    scopus 로고
    • Smooth muscle cell calcium activation mechanisms
    • Berridge, M. J. (2008) Smooth muscle cell calcium activation mechanisms. J. Physiol. 586, 5047-5061
    • (2008) J. Physiol. , vol.586 , pp. 5047-5061
    • Berridge, M.J.1
  • 39
    • 17644378712 scopus 로고    scopus 로고
    • Signal transduction through the RhoA/Rho-kinase pathway in smooth muscle
    • Somlyo, A. P., and Somlyo, A. V. (2004) Signal transduction through the RhoA/Rho-kinase pathway in smooth muscle. J. Muscle Res. Cell Motil. 25, 613-615
    • (2004) J. Muscle Res. Cell Motil. , vol.25 , pp. 613-615
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 40
    • 79958704519 scopus 로고    scopus 로고
    • Role of myosin light chain kinase and myosin light chain phosphatase in the resistance arterial myogenic response to intravascular pressure
    • Cole, W. C., and Welsh, D. G. (2011) Role of myosin light chain kinase and myosin light chain phosphatase in the resistance arterial myogenic response to intravascular pressure. Arch. Biochem. Biophys. 510, 160-173
    • (2011) Arch. Biochem. Biophys. , vol.510 , pp. 160-173
    • Cole, W.C.1    Welsh, D.G.2
  • 41
    • 66549106916 scopus 로고    scopus 로고
    • 2+/ calmodulin of an exogenous myosin light chain kinase (MLCK) in mouse arteries
    • 2+/ calmodulin of an exogenous myosin light chain kinase (MLCK) in mouse arteries. J. Physiol. 587, 2599-2612
    • (2009) J. Physiol. , vol.587 , pp. 2599-2612
    • Raina, H.1    Zacharia, J.2    Li, M.3    Wier, W.G.4
  • 42
    • 34250792930 scopus 로고    scopus 로고
    • The regulation of smooth muscle contractility by zipper-interacting protein kinase
    • Ihara, E., and MacDonald, J. A. (2007) The regulation of smooth muscle contractility by zipper-interacting protein kinase. Can. J. Physiol. Pharmacol. 85, 79-87
    • (2007) Can. J. Physiol. Pharmacol. , vol.85 , pp. 79-87
    • Ihara, E.1    Macdonald, J.A.2
  • 43
    • 0022410257 scopus 로고
    • Phosphorylation of smooth muscle myosin at two distinct sites by myosin light chain kinase
    • Ikebe, M., and Hartshorne, D. J. (1985) Phosphorylation of smooth muscle myosin at two distinct sites by myosin light chain kinase. J. Biol. Chem. 260, 10027-10031
    • (1985) J. Biol. Chem. , vol.260 , pp. 10027-10031
    • Ikebe, M.1    Hartshorne, D.J.2
  • 45
    • 84055199978 scopus 로고    scopus 로고
    • Vascular smooth muscle myosin light chain diphosphorylation: Mechanism, function, and pathological implications
    • Walsh, M. P. (2011) Vascular smooth muscle myosin light chain diphosphorylation: mechanism, function, and pathological implications. IUBMB life 63, 987-1000
    • (2011) IUBMB Life , vol.63 , pp. 987-1000
    • Walsh, M.P.1
  • 48
    • 80051919561 scopus 로고    scopus 로고
    • LPA(1) -induced migration requires nonmuscle myosin II light chain phosphorylation in breast cancer cells
    • Kim, J. H., and Adelstein, R. S. (2011) LPA(1) -induced migration requires nonmuscle myosin II light chain phosphorylation in breast cancer cells. J. Cell Physiol. 226, 2881-2893
    • (2011) J. Cell Physiol. , vol.226 , pp. 2881-2893
    • Kim, J.H.1    Adelstein, R.S.2
  • 49
    • 66749172932 scopus 로고    scopus 로고
    • Protein kinase C activation disrupts epithelial apical junctions via ROCK-II dependent stimulation of actomyosin contractility
    • Ivanov, A. I., Samarin, S. N., Bachar, M., Parkos, C. A., and Nusrat, A. (2009) Protein kinase C activation disrupts epithelial apical junctions via ROCK-II dependent stimulation of actomyosin contractility. BMC Cell Biol. 10:36
    • (2009) BMC Cell Biol. , vol.10 , pp. 36
    • Ivanov, A.I.1    Samarin, S.N.2    Bachar, M.3    Parkos, C.A.4    Nusrat, A.5
  • 51
    • 79958748938 scopus 로고    scopus 로고
    • Myosin light chain kinase and the role of myosin light chain phosphorylation in skeletal muscle
    • Stull, J. T., Kamm, K. E., and Vandenboom, R. (2011) Myosin light chain kinase and the role of myosin light chain phosphorylation in skeletal muscle. Arch. Biochem. Biophys. 510, 120-128
    • (2011) Arch. Biochem. Biophys. , vol.510 , pp. 120-128
    • Stull, J.T.1    Kamm, K.E.2    Vandenboom, R.3
  • 52
    • 79953183003 scopus 로고    scopus 로고
    • Signaling to myosin regulatory light chain in sarcomeres
    • Kamm, K. E., and Stull, J. T. (2011) Signaling to myosin regulatory light chain in sarcomeres. J. Biol. Chem. 286, 9941-9947
    • (2011) J. Biol. Chem. , vol.286 , pp. 9941-9947
    • Kamm, K.E.1    Stull, J.T.2
  • 54
    • 67650138614 scopus 로고    scopus 로고
    • Signaling processes for initiating smooth muscle contraction upon neural stimulation
    • Ding, H. L., Ryder, J. W., Stull, J. T., and Kamm, K. E. (2009) Signaling processes for initiating smooth muscle contraction upon neural stimulation. J. Biol. Chem. 284, 15541-15548
    • (2009) J. Biol. Chem. , vol.284 , pp. 15541-15548
    • Ding, H.L.1    Ryder, J.W.2    Stull, J.T.3    Kamm, K.E.4
  • 56
    • 0034256090 scopus 로고    scopus 로고
    • Calmodulin: A prototypical calcium sensor
    • Chin, D., and Means, A. R. (2000) Calmodulin: a prototypical calcium sensor. Trends Cell Biol. 10, 322-328
    • (2000) Trends Cell Biol. , vol.10 , pp. 322-328
    • Chin, D.1    Means, A.R.2
  • 57
    • 84868104219 scopus 로고    scopus 로고
    • 2+ sensitization in rat arterial smooth muscle
    • 2+ sensitization in rat arterial smooth muscle. J. Physiol. 590, 5401-5423
    • (2012) J. Physiol. , vol.590 , pp. 5401-5423
    • Kitazawa, T.1    Kitazawa, K.2
  • 58
    • 0030924806 scopus 로고    scopus 로고
    • Differential inhibition and posttranslational modification of protein phosphatase 1 and 2A in MCF7 cells treated with calyculin-A, okadaic acid, and tautomycin
    • Favre, B., Turowski, P., and Hemmings, B. A. (1997) Differential inhibition and posttranslational modification of protein phosphatase 1 and 2A in MCF7 cells treated with calyculin-A, okadaic acid, and tautomycin. J. Biol. Chem. 272, 13856-13863
    • (1997) J. Biol. Chem. , vol.272 , pp. 13856-13863
    • Favre, B.1    Turowski, P.2    Hemmings, B.A.3
  • 59
    • 0028950664 scopus 로고
    • Inhibition of specific binding of okadaic acid to protein phosphatase 2A by microcystin-LR, calyculin-A and tautomycin: Method of analysis of interactions of tight-binding ligands with target protein
    • Takai, A., Sasaki, K., Nagai, H., Mieskes, G., Isobe, M., Isono, K., and Yasumoto, T. (1995) Inhibition of specific binding of okadaic acid to protein phosphatase 2A by microcystin-LR, calyculin-A and tautomycin: method of analysis of interactions of tight-binding ligands with target protein. Biochem. J. 306, 657-665
    • (1995) Biochem. J. , vol.306 , pp. 657-665
    • Takai, A.1    Sasaki, K.2    Nagai, H.3    Mieskes, G.4    Isobe, M.5    Isono, K.6    Yasumoto, T.7
  • 60
    • 0021099627 scopus 로고
    • Purification and characterization of a multisubunit phosphatase from turkey gizzard smooth muscle. The effect of calmodulin binding to myosin light chain kinase on dephosphorylation
    • Pato, M. D., and Adelstein, R. S. (1983) Purification and characterization of a multisubunit phosphatase from turkey gizzard smooth muscle. The effect of calmodulin binding to myosin light chain kinase on dephosphorylation. J. Biol. Chem. 258, 7047-7054
    • (1983) J. Biol. Chem. , vol.258 , pp. 7047-7054
    • Pato, M.D.1    Adelstein, R.S.2


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