메뉴 건너뛰기




Volumn 242, Issue 3, 1996, Pages 454-459

Substrate specificity and inhibitor sensitivity of Ca2+/S100-dependent twitchin kinases

Author keywords

Calmodulin; Protein kinase; S100; Titin; Twitchin

Indexed keywords

CONNECTIN; PROTEIN KINASE; RECOMBINANT PROTEIN;

EID: 0030424963     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.454rr.x     Document Type: Article
Times cited : (25)

References (25)
  • 1
    • 0024422164 scopus 로고
    • Sequence of an unusually large protein implicated in regulation of myosin activity in C. elegans
    • Benian, G. M., Kiff, J. E., Neckleman, N., Moerman, D. G. & Waterston, R. H. (1989) Sequence of an unusually large protein implicated in regulation of myosin activity in C. elegans, Nature 342, 45-50.
    • (1989) Nature , vol.342 , pp. 45-50
    • Benian, G.M.1    Kiff, J.E.2    Neckleman, N.3    Moerman, D.G.4    Waterston, R.H.5
  • 2
    • 0028824480 scopus 로고
    • Titins: Giant proteins in charge of muscle ultrastructure and elasticity
    • Labeit, S. & Kolmerer, B. (1995) Titins: giant proteins in charge of muscle ultrastructure and elasticity, Science 270, 293-296.
    • (1995) Science , vol.270 , pp. 293-296
    • Labeit, S.1    Kolmerer, B.2
  • 3
    • 0028897497 scopus 로고
    • Both synchronous and asynchronous muscle isoforms of projectin (the Drosophila bent locus product) contain functional kinase domains
    • Ayme-Southgate, A., Southgate, R., Saide, J., Benian, G. M. & Pardue, M. L. (1995) Both synchronous and asynchronous muscle isoforms of projectin (the Drosophila bent locus product) contain functional kinase domains, J. Cell Biol. 128, 393-403.
    • (1995) J. Cell Biol. , vol.128 , pp. 393-403
    • Ayme-Southgate, A.1    Southgate, R.2    Saide, J.3    Benian, G.M.4    Pardue, M.L.5
  • 4
    • 0028955760 scopus 로고
    • Structure and function of titin and nebulin
    • Keller, T. C. S. III (1995) Structure and function of titin and nebulin, Curr. Opin. Cell Biol. 7, 32-38.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 32-38
    • Keller III, T.C.S.1
  • 5
    • 0027990826 scopus 로고
    • The protein kinase domain of twitchin has protein kinase activity and an autoinhibitory region
    • Lei, J., Tang, X., Chamber, T. C. Pohl, J. & Benian, G. M. (1994) The protein kinase domain of twitchin has protein kinase activity and an autoinhibitory region, J. Biol. Chem. 269, 21 078-21 085.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21078-21085
    • Lei, J.1    Tang, X.2    Chamber, T.C.3    Pohl, J.4    Benian, G.M.5
  • 6
    • 0028841580 scopus 로고
    • Phosphorylation of myosin regulatory light chains by the molluscan twitchin kinase
    • Heierhorst, J., Probst, W. C., Kohanski, R. A., Buku, A. & Weiss, K. R. (1995) Phosphorylation of myosin regulatory light chains by the molluscan twitchin kinase, Eur. J. Biochem. 233, 426-431.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 426-431
    • Heierhorst, J.1    Probst, W.C.2    Kohanski, R.A.3    Buku, A.4    Weiss, K.R.5
  • 8
    • 0027980973 scopus 로고
    • Autophosphorylation of molluscan twitchin and interaction of its kinase domain with calcium/calmodulin
    • Heierhorst, J., Probst, W. C., Vilim, F. S., Buku, A. & Weiss, K. R. (1994) Autophosphorylation of molluscan twitchin and interaction of its kinase domain with calcium/calmodulin, J. Biol. Chem. 269, 21 086-21 093.
    • (1994) J. Biol. Chem. , vol.269 , pp. 21086-21093
    • Heierhorst, J.1    Probst, W.C.2    Vilim, F.S.3    Buku, A.4    Weiss, K.R.5
  • 9
    • 0028287635 scopus 로고
    • Insights into autoregulation from the crystal structure of twitchin kinase
    • Hu, S.-H., Parker, M. W., Lei, J. Y., Wilce, M. C. J., Benian, G. M. & Kemp, B. E. (1994) Insights into autoregulation from the crystal structure of twitchin kinase, Nature 369, 581-584.
    • (1994) Nature , vol.369 , pp. 581-584
    • Hu, S.-H.1    Parker, M.W.2    Lei, J.Y.3    Wilce, M.C.J.4    Benian, G.M.5    Kemp, B.E.6
  • 11
    • 0026329843 scopus 로고
    • Design and use of peptide substrates for protein kinases
    • Kemp, B. E. & Pearson, R. (1991) Design and use of peptide substrates for protein kinases, Methods Enzymol. 200, 121-134.
    • (1991) Methods Enzymol. , vol.200 , pp. 121-134
    • Kemp, B.E.1    Pearson, R.2
  • 12
    • 0020491386 scopus 로고
    • Phosphorylation of a synthetic heptadecapeptide by smooth muscle myosin light chain kinase
    • Kemp, B. E., Pearson, R. B. & House, C. (1982) Phosphorylation of a synthetic heptadecapeptide by smooth muscle myosin light chain kinase, J. Biol. Chem. 257, 13 349-13 353.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13349-13353
    • Kemp, B.E.1    Pearson, R.B.2    House, C.3
  • 13
    • 0242534533 scopus 로고
    • Role of basic residues in the phosphorylation of synthetic peptides by myosin light chain kinase
    • Kemp, B. E., Pearson, R. B. & House, C. (1983) Role of basic residues in the phosphorylation of synthetic peptides by myosin light chain kinase, Proc. Natl Acatl. Sci. USA 80, 7471-7475.
    • (1983) Proc. Natl Acatl. Sci. USA , vol.80 , pp. 7471-7475
    • Kemp, B.E.1    Pearson, R.B.2    House, C.3
  • 14
    • 0022002613 scopus 로고
    • Spatial requirements for location of basic residues in peptide substrates for smooth muscle myosin light chain kinase
    • Kemp, B. E. & Pearson, R. B. (1985) Spatial requirements for location of basic residues in peptide substrates for smooth muscle myosin light chain kinase, J. Biol. Chem. 260, 3355-3359.
    • (1985) J. Biol. Chem. , vol.260 , pp. 3355-3359
    • Kemp, B.E.1    Pearson, R.B.2
  • 15
    • 0022633832 scopus 로고
    • Smooth muscle myosin kinase requires residues on the COOH-terminal side of the phosphorylation site
    • Pearson, R. B., Misconi, L. Y. & Kemp, B. E. (1986) Smooth muscle myosin kinase requires residues on the COOH-terminal side of the phosphorylation site, J. Biol. Chem. 261, 25-27.
    • (1986) J. Biol. Chem. , vol.261 , pp. 25-27
    • Pearson, R.B.1    Misconi, L.Y.2    Kemp, B.E.3
  • 16
    • 0023028510 scopus 로고
    • Phosphorylation of synthetic peptides by skeletal muscle myosin light chain kinases
    • Michnoff, C. H., Kemp, B. E. & Stull, J. T. (1986) Phosphorylation of synthetic peptides by skeletal muscle myosin light chain kinases, J. Biol. Chem. 261, 8320-8326.
    • (1986) J. Biol. Chem. , vol.261 , pp. 8320-8326
    • Michnoff, C.H.1    Kemp, B.E.2    Stull, J.T.3
  • 18
    • 0023644877 scopus 로고
    • Selective inhibition of catalytic activity of smooth muscle myosin light chain kinase
    • Saitoh, M., Ishikawa, T., Matsushima, S., Naka, M, & Hidaka, H. (1987) Selective inhibition of catalytic activity of smooth muscle myosin light chain kinase, J. Biol. Chem. 262, 7796-7801.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7796-7801
    • Saitoh, M.1    Ishikawa, T.2    Matsushima, S.3    Naka, M.4    Hidaka, H.5
  • 19
    • 0025159272 scopus 로고
    • How calmodulin hinds its targets: Sequence independent recognition of amphiphilic α-helices
    • O'Neil, K. T. & DeGrado, W. F. (1990) How calmodulin hinds its targets: sequence independent recognition of amphiphilic α-helices, Trends Biochem. Sci. 15, 59-64.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 59-64
    • O'Neil, K.T.1    DeGrado, W.F.2
  • 20
    • 0024257797 scopus 로고
    • Regulatory myosin light-chain genes of Caenorhabditis elegans
    • Cummins, C. & Anderson, P. (1988) Regulatory myosin light-chain genes of Caenorhabditis elegans, Mol. Cell. Biol. 8, 5339-5349.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 5339-5349
    • Cummins, C.1    Anderson, P.2
  • 21
    • 0023776666 scopus 로고
    • Identification and intracellular localization of the unc-22 gene product of Caenorhabditis elegans
    • Moerman, D. G., Benian, G. M., Barstead, R. J., Schriefer, L. A. & Waterston, R. H. (1988) Identification and intracellular localization of the unc-22 gene product of Caenorhabditis elegans, Genes & Dev. 2, 93-105.
    • (1988) Genes & Dev. , vol.2 , pp. 93-105
    • Moerman, D.G.1    Benian, G.M.2    Barstead, R.J.3    Schriefer, L.A.4    Waterston, R.H.5
  • 22
    • 0027748233 scopus 로고
    • Mini-titins in striated and smooth molluscan muscles: Structure, location and immunological crossreactivity
    • Vibert, P., Edelstein, S. M., Castellani, L. & Elliot, B. W. Jr (1993) Mini-titins in striated and smooth molluscan muscles: structure, location and immunological crossreactivity, J. Muscle Res. Cell Motil. 14, 598-607.
    • (1993) J. Muscle Res. Cell Motil. , vol.14 , pp. 598-607
    • Vibert, P.1    Edelstein, S.M.2    Castellani, L.3    Elliot Jr., B.W.4
  • 24
    • 0029669991 scopus 로고    scopus 로고
    • The S100 family of EF-hand calcium-binding proteins: Functions and pathology
    • Schäfer, B. W. & Heizmann, C. W. (1996) The S100 family of EF-hand calcium-binding proteins: functions and pathology, Trends Biochem. Sci. 21, 134-140.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 134-140
    • Schäfer, B.W.1    Heizmann, C.W.2
  • 25
    • 0022373739 scopus 로고
    • Substrate specificity of a multifunctional calmodulin-dependent protein kinase
    • Pearson, R. B., Woodgett, J. R., Cohen, P. & Kemp, B. E. (1985) Substrate specificity of a multifunctional calmodulin-dependent protein kinase, J. Biol. Chem. 260, 14 471-14 476.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14471-14476
    • Pearson, R.B.1    Woodgett, J.R.2    Cohen, P.3    Kemp, B.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.