메뉴 건너뛰기




Volumn 429, Issue 2, 2010, Pages 291-302

Kinase-related protein/telokin inhibits Ca2+-independent contraction in Triton-skinned guinea pig taenia coli

Author keywords

Kinase related protein (KRP); Myosin light chain kinase (MLCK); Myosin light chain phosphatase (MLCP); Phosphorylation; Smooth muscle contraction; Telokin

Indexed keywords

CONSTITUTIVELY ACTIVES; GUINEA PIGS; HEAVY MEROMYOSIN; IN-VITRO; MICROCYSTINS; MYOSIN LIGHT CHAIN KINASE; MYOSIN LIGHT CHAIN PHOSPHATASE ( MLCP); MYOSIN LIGHT CHAINS; PHOSPHATASE INHIBITORS; PHOSPHORYLATION SITES; SMOOTH MUSCLE CONTRACTION; SMOOTH MUSCLES;

EID: 77954747598     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20090819     Document Type: Article
Times cited : (7)

References (48)
  • 1
    • 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
  • 2
    • 4444303564 scopus 로고    scopus 로고
    • Role of protein phosphatase type 1 in contractile functions: Myosin phosphatase
    • Hartshorne, D. J., Ito, M. and Erdodi, 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    Erdodi, F.3
  • 3
    • 0141751697 scopus 로고    scopus 로고
    • 2+ sensitivity of smooth muscle and nonmuscle myosin II: Modulated by G proteins, kinases, and myosin phosphatase
    • 2+ sensitivity of smooth muscle and nonmuscle myosin II: modulated 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
  • 4
    • 0034976775 scopus 로고    scopus 로고
    • Regulation of myosin phosphorylation in smooth muscle
    • Pfitzer, G. (2001) Regulation of myosin phosphorylation in smooth muscle. J. Appl. Physiol. 91, 497-503
    • (2001) J. Appl. Physiol. , vol.91 , pp. 497-503
    • Pfitzer, G.1
  • 5
    • 0033134836 scopus 로고    scopus 로고
    • 2+-independent phosphorylation of myosin in rat caudal artery and chicken gizzard myofilaments
    • 2+-independent phosphorylation of myosin in rat caudal artery and chicken gizzard myofilaments. J. Physiol. 516, 805-824
    • (1999) J. Physiol. , vol.516 , pp. 805-824
    • Weber, L.P.1    Van Lierop, J.E.2    Walsh, M.P.3
  • 9
    • 33646848052 scopus 로고    scopus 로고
    • Gi-coupled receptors mediate phosphorylation of CPI-17 and MLC20 via preferential activation of the PI3K/ILK pathway
    • Huang, J., Mahavadi, S., Sriwai, W., Hu, W. and Murthy, K. S. (2006) Gi-coupled receptors mediate phosphorylation of CPI-17 and MLC20 via preferential activation of the PI3K/ILK pathway. Biochem. J. 396, 193-200
    • (2006) Biochem. J. , vol.396 , pp. 193-200
    • Huang, J.1    Mahavadi, S.2    Sriwai, W.3    Hu, W.4    Murthy, K.S.5
  • 11
    • 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
  • 12
    • 0035800862 scopus 로고    scopus 로고
    • 2+-free smooth muscle contraction via myosin light chain phosphorylation
    • 2+-free smooth muscle contraction via myosin light chain phosphorylation. J. Biol. Chem. 276, 29567-29574
    • (2001) J. Biol. Chem. , vol.276 , pp. 29567-29574
    • Niiro, N.1    Ikebe, M.2
  • 13
    • 73949121819 scopus 로고    scopus 로고
    • Regulation of smooth muscle contraction by small GTPases
    • Bethesda
    • Puetz, S., Lubomirov, L. T. and Pfitzer, G. (2009) Regulation of smooth muscle contraction by small GTPases. Physiology (Bethesda) 24, 342-356
    • (2009) Physiology , vol.24 , pp. 342-356
    • Puetz, S.1    Lubomirov, L.T.2    Pfitzer, G.3
  • 17
    • 0024330080 scopus 로고
    • Identification in turkey gizzard of an acidic protein related to the C-terminal portion of smooth muscle myosin light chain kinase
    • Ito, M., Dabrowska, R., Guerriero, Jr, V. and Hartshorne, D. J. (1989) Identification in turkey gizzard of an acidic protein related to the C-terminal portion of smooth muscle myosin light chain kinase. J. Biol. Chem. 264, 13971-13974
    • (1989) J. Biol. Chem. , vol.264 , pp. 13971-13974
    • Ito, M.1    Dabrowska, R.2    Guerriero Jr., V.3    Hartshorne, D.J.4
  • 18
    • 0026643660 scopus 로고
    • Structure and expression of a calcium-binding protein gene contained within a calmodulin-regulated protein kinase gene
    • Collinge, M., Matrisian, P. E., Zimmer, W. E., Shattuck, R. L., Lukas, T. J., Van Eldik, L. J. and Watterson, D. M. (1992) Structure and expression of a calcium-binding protein gene contained within a calmodulin-regulated protein kinase gene. Mol. Cell. Biol. 12, 2359-2371
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 2359-2371
    • Collinge, M.1    Matrisian, P.E.2    Zimmer, W.E.3    Shattuck, R.L.4    Lukas, T.J.5    Van Eldik, L.J.6    Watterson, D.M.7
  • 19
    • 0026343743 scopus 로고
    • The carboxyl terminus of the smooth muscle myosin light chain kinase is expressed as an independent protein, telokin
    • Gallagher, P. J. and Herring, B. P. (1991) The carboxyl terminus of the smooth muscle myosin light chain kinase is expressed as an independent protein, telokin. J. Biol. Chem. 266, 23945-23952
    • (1991) J. Biol. Chem. , vol.266 , pp. 23945-23952
    • Gallagher, P.J.1    Herring, B.P.2
  • 23
    • 0026800671 scopus 로고
    • X-ray structure determination of telokin, the C-terminal domain of myosin light chain kinase, at 2.8 Å resolution
    • Holden, H. M., Ito, M., Hartshorne, D. J. and Rayment, I. (1992) X-ray structure determination of telokin, the C-terminal domain of myosin light chain kinase, at 2.8 Å resolution. J. Mol. Biol. 227, 840-851
    • (1992) J. Mol. Biol. , vol.227 , pp. 840-851
    • Holden, H.M.1    Ito, M.2    Hartshorne, D.J.3    Rayment, I.4
  • 27
    • 4444302915 scopus 로고    scopus 로고
    • Novel phosphospecific antibodies for monitoring phosphorylation of proteins encoded by the myosin light chain kinase genetic locus
    • Khapchaev, A. Y., Krymsky, M. A., Sidorova, M. V., Bespalova, Zh. D., Wang, C. L., Shirinsky, V. P. and Vorotnikov, A. V. (2004) Novel phosphospecific antibodies for monitoring phosphorylation of proteins encoded by the myosin light chain kinase genetic locus. Biochemistry 69, 789-798
    • (2004) Biochemistry , vol.69 , pp. 789-798
    • Khapchaev, A.Y.1    Krymsky, M.A.2    Sidorova, M.V.3    Bespalova, Zh.D.4    Wang, C.L.5    Shirinsky, V.P.6    Vorotnikov, A.V.7
  • 28
    • 0034683163 scopus 로고    scopus 로고
    • Phosphorylation of telokin by cyclic nucleotide kinases and the identification of in vivo phosphorylation sites in smooth muscle
    • DOI 10.1016/S0014-5793(00)01884-6, PII S0014579300018846
    • MacDonald, J. A., Walker, L. A., Nakamoto, R. K., Gorenne, I., Somlyo, A. V., Somlyo, A. P. and Haystead, T. A. (2000) Phosphorylation of telokin by cyclic nucleotide kinases and the identification of in vivo phosphorylation sites in smooth muscle. FEBS Lett. 479, 83-88 (Pubitemid 30616411)
    • (2000) FEBS Letters , vol.479 , Issue.3 , pp. 83-88
    • MacDonald, J.A.1    Walker, L.A.2    Nakamoto, R.K.3    Gorenne, I.4    Somlyo, A.V.5    Somlyo, A.P.6    Haystead, T.A.J.7
  • 29
    • 0342851960 scopus 로고    scopus 로고
    • Kinase-related protein is phosphorylated both in vitro and in smooth muscle by mitogen-activated and cyclic AMP-dependent protein kinases
    • Vorotnikov, A. V., Silver, D. L., Sellers, J. R., Watterson, D. M. and Shirinsky, V. P. (1996) Kinase-related protein is phosphorylated both in vitro and in smooth muscle by mitogen-activated and cyclic AMP-dependent protein kinases. J. Muscle Res. Cell. Motil. 17, 153a
    • (1996) J. Muscle Res. Cell. Motil. , vol.17
    • Vorotnikov, A.V.1    Silver, D.L.2    Sellers, J.R.3    Watterson, D.M.4    Shirinsky, V.P.5
  • 31
    • 11144256526 scopus 로고    scopus 로고
    • Modulation of myosin filament activation by telokin in smooth muscle liberation of myosin kinase and phosphatase from supramolecular complexes
    • Sobieszek, A., Andruchov, O. Y., Grabarek, Z., Kulikova, N., Liebetrau, C. and Matusovsky, O. S. (2005) Modulation of myosin filament activation by telokin in smooth muscle liberation of myosin kinase and phosphatase from supramolecular complexes. Biophys. Chem. 113, 25-40
    • (2005) Biophys. Chem. , vol.113 , pp. 25-40
    • Sobieszek, A.1    Andruchov, O.Y.2    Grabarek, Z.3    Kulikova, N.4    Liebetrau, C.5    Matusovsky, O.S.6
  • 32
    • 0032080256 scopus 로고    scopus 로고
    • Acceleration of myosin light chain dephosphorylation and relaxation of smooth muscle by telokin. Synergism with cyclic nucleotide-activated kinase
    • Wu, X., Haystead, T. A., Nakamoto, R. K., Somlyo, A. V. and Somlyo, A. P. (1998) Acceleration of myosin light chain dephosphorylation and relaxation of smooth muscle by telokin. Synergism with cyclic nucleotide-activated kinase. J. Biol. Chem. 273, 11362-11369
    • (1998) J. Biol. Chem. , vol.273 , pp. 11362-11369
    • Wu, X.1    Haystead, T.A.2    Nakamoto, R.K.3    Somlyo, A.V.4    Somlyo, A.P.5
  • 33
    • 0031051767 scopus 로고    scopus 로고
    • Telokin (kinase-related protein) modulates the oligomeric state of smooth-muscle myosin light-chain kinase and its interaction with myosin filaments
    • Nieznanski, K. and Sobieszek, A. (1997) Telokin (kinase-related protein) modulates the oligomeric state of smooth-muscle myosin light-chain kinase and its interaction with myosin filaments. Biochem. J. 322, 65-71 (Pubitemid 127732387)
    • (1997) Biochemical Journal , vol.322 , Issue.1 , pp. 65-71
    • Nieznanski, K.1    Sobieszek, A.2
  • 34
    • 0030762886 scopus 로고    scopus 로고
    • Kinase-related prote a smooth muscle myosin-binding protein
    • Vorotnikov, A. V. (1997) Kinase-related protein: a smooth muscle myosin-binding protein. Int. J. Biochem. Cell Biol. 29, 727-730
    • (1997) Int. J. Biochem. Cell Biol. , vol.29 , pp. 727-730
    • Vorotnikov, A.V.1
  • 37
    • 0020023991 scopus 로고
    • Purification of smooth muscle myosin light-chain kinase
    • Adelstein, R. S. and Klee, C. B. (1982) Purification of smooth muscle myosin light-chain kinase. Methods Enzymol. 85, 298-308
    • (1982) Methods Enzymol. , vol.85 , pp. 298-308
    • Adelstein, R.S.1    Klee, C.B.2
  • 38
    • 0019766908 scopus 로고
    • Reversible phosphorylation of smooth muscle myosin, heavy meromyosin, and platelet myosin
    • Sellers, J. R., Pato, M. D. and Adelstein, R. S. (1981) Reversible phosphorylation of smooth muscle myosin, heavy meromyosin, and platelet myosin. J. Biol. Chem. 256, 13137-13142
    • (1981) J. Biol. Chem. , vol.256 , pp. 13137-13142
    • Sellers, J.R.1    Pato, M.D.2    Adelstein, R.S.3
  • 39
    • 0024537382 scopus 로고
    • Location of the inhibitory region of smooth muscle myosin light chain kinase
    • Ikebe, M., Maruta, S. and Reardon, S. (1989) Location of the inhibitory region of smooth muscle myosin light chain kinase. J. Biol. Chem. 264, 6967-6971
    • (1989) J. Biol. Chem. , vol.264 , pp. 6967-6971
    • Ikebe, M.1    Maruta, S.2    Reardon, S.3
  • 40
    • 0020493109 scopus 로고
    • 2+-induced hydrophobic site on calmodulin: Application for purification of calmodulin by phenyl-Sepharose affinity chromatography
    • 2+-induced hydrophobic site on calmodulin: application for purification of calmodulin by phenyl-Sepharose affinity chromatography. Biochem. Biophys. Res. Commun. 104, 830-836
    • (1982) Biochem. Biophys. Res. Commun. , vol.104 , pp. 830-836
    • Gopalakrishna, R.1    Anderson, W.B.2
  • 41
    • 0023019582 scopus 로고
    • Different phosphorylated forms of myosin in contracting tracheal smooth muscle
    • Persechini, A., Kamm, K. E. and Stull, J. T. (1986) Different phosphorylated forms of myosin in contracting tracheal smooth muscle. J. Biol. Chem. 261, 6293-6299
    • (1986) J. Biol. Chem. , vol.261 , pp. 6293-6299
    • Persechini, A.1    Kamm, K.E.2    Stull, J.T.3
  • 42
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 43
    • 0038511012 scopus 로고    scopus 로고
    • Inhibition of contraction and myosin light chain phosphorylation in guinea-pig smooth muscle by p21-activated kinase 1
    • Wirth, A., Schroeter, M., Kock-Hauser, C., Manser, E., Chalovich, J. M., De Lanerolle, P. and Pfitzer, G. (2003) Inhibition of contraction and myosin light chain phosphorylation in guinea-pig smooth muscle by p21-activated kinase 1. J. Physiol. 549, 489-500 (Pubitemid 36701760)
    • (2003) Journal of Physiology , vol.549 , Issue.2 , pp. 489-500
    • Wirth, A.1    Schroeter, M.2    Kock-Hauser, C.3    Manser, E.4    Chalovich, J.M.5    De Lanerolle, P.6    Pfitzer, G.7
  • 44
    • 0026322150 scopus 로고
    • Ion-specific and general ionic effects on contraction of skinned fast-twitch skeletal muscle from the rabbit
    • Andrews, M. A., Maughan, D. W., Nosek, T. M. and Godt, R. E. (1991) Ion-specific and general ionic effects on contraction of skinned fast-twitch skeletal muscle from the rabbit. J. Gen. Physiol. 98, 1105-1125
    • (1991) J. Gen. Physiol. , vol.98 , pp. 1105-1125
    • Andrews, M.A.1    Maughan, D.W.2    Nosek, T.M.3    Godt, R.E.4
  • 45
    • 0017045987 scopus 로고
    • The force generated by a visceral smooth muscle
    • Gabella, G. (1976) The force generated by a visceral smooth muscle. J. Physiol. 263, 199-213
    • (1976) J. Physiol. , vol.263 , pp. 199-213
    • Gabella, G.1
  • 46
    • 0028914008 scopus 로고
    • Autophosphorylation of smooth muscle myosin light chain kinase at its regulatory domain
    • Tokui, T., Ando, S. and Ikebe, M. (1995) Autophosphorylation of smooth muscle myosin light chain kinase at its regulatory domain. Biochemistry 34, 5173-5179
    • (1995) Biochemistry , vol.34 , pp. 5173-5179
    • Tokui, T.1    Ando, S.2    Ikebe, M.3
  • 48
    • 0017823252 scopus 로고
    • Differences in cellular contractile protein contents among porcine smooth muscles: Evidence for variation in the contractile system
    • Cohen, D. M. and Murphy, R. A. (1978) Differences in cellular contractile protein contents among porcine smooth muscles: evidence for variation in the contractile system. J. Gen. Physiol. 72, 369-380
    • (1978) J. Gen. Physiol. , vol.72 , pp. 369-380
    • Cohen, D.M.1    Murphy, R.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.