메뉴 건너뛰기




Volumn 53, Issue 1, 2014, Pages 140-147

Identification of a Major Determinant for Serine-Threonine Kinase Phosphoacceptor Specificity

Author keywords

[No Author keywords available]

Indexed keywords

P21 ACTIVATED KINASE 4; PROTEIN KINASE C; PROTEIN SERINE THREONINE KINASE; MST4 PROTEIN, HUMAN; P21 ACTIVATED KINASE; PAK4 PROTEIN, HUMAN; PEPTIDE;

EID: 84892364761     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2013.11.013     Document Type: Article
Times cited : (80)

References (37)
  • 1
    • 0034682564 scopus 로고    scopus 로고
    • Serine-53 at the tip of the glycine-rich loop of cAMP-dependent protein kinase: role in catalysis, P-site specificity, and interaction with inhibitors
    • Aimes R.T., Hemmer W., Taylor S.S. Serine-53 at the tip of the glycine-rich loop of cAMP-dependent protein kinase: role in catalysis, P-site specificity, and interaction with inhibitors. Biochemistry 2000, 39:8325-8332.
    • (2000) Biochemistry , vol.39 , pp. 8325-8332
    • Aimes, R.T.1    Hemmer, W.2    Taylor, S.S.3
  • 3
    • 0037422596 scopus 로고    scopus 로고
    • Structural basis and prediction of substrate specificity in protein serine/threonine kinases
    • Brinkworth R.I., Breinl R.A., Kobe B. Structural basis and prediction of substrate specificity in protein serine/threonine kinases. Proc. Natl. Acad. Sci. USA 2003, 100:74-79.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 74-79
    • Brinkworth, R.I.1    Breinl, R.A.2    Kobe, B.3
  • 4
    • 0033224309 scopus 로고    scopus 로고
    • The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases
    • Brown N.R., Noble M.E., Endicott J.A., Johnson L.N. The structural basis for specificity of substrate and recruitment peptides for cyclin-dependent kinases. Nat. Cell Biol. 1999, 1:438-443.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 438-443
    • Brown, N.R.1    Noble, M.E.2    Endicott, J.A.3    Johnson, L.N.4
  • 6
    • 0033638454 scopus 로고    scopus 로고
    • The molecular basis of FHA domain:phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms
    • Durocher D., Taylor I.A., Sarbassova D., Haire L.F., Westcott S.L., Jackson S.P., Smerdon S.J., Yaffe M.B. The molecular basis of FHA domain:phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms. Mol. Cell 2000, 6:1169-1182.
    • (2000) Mol. Cell , vol.6 , pp. 1169-1182
    • Durocher, D.1    Taylor, I.A.2    Sarbassova, D.3    Haire, L.F.4    Westcott, S.L.5    Jackson, S.P.6    Smerdon, S.J.7    Yaffe, M.B.8
  • 8
    • 0035185571 scopus 로고    scopus 로고
    • Structure and autoregulation of the insulin-like growth factor 1 receptor kinase
    • Favelyukis S., Till J.H., Hubbard S.R., Miller W.T. Structure and autoregulation of the insulin-like growth factor 1 receptor kinase. Nat. Struct. Biol. 2001, 8:1058-1063.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 1058-1063
    • Favelyukis, S.1    Till, J.H.2    Hubbard, S.R.3    Miller, W.T.4
  • 9
    • 0021792133 scopus 로고
    • Distinct structural requirements of Ca2+/phospholipid-dependent protein kinase (protein kinase C) and cAMP-dependent protein kinase as evidenced by synthetic peptide substrates
    • Ferrari S., Marchiori F., Borin G., Pinna L.A. Distinct structural requirements of Ca2+/phospholipid-dependent protein kinase (protein kinase C) and cAMP-dependent protein kinase as evidenced by synthetic peptide substrates. FEBS Lett. 1985, 184:72-77.
    • (1985) FEBS Lett. , vol.184 , pp. 72-77
    • Ferrari, S.1    Marchiori, F.2    Borin, G.3    Pinna, L.A.4
  • 10
    • 0035957986 scopus 로고    scopus 로고
    • The serine/threonine kinase PAK4 prevents caspase activation and protects cells from apoptosis
    • Gnesutta N., Qu J., Minden A. The serine/threonine kinase PAK4 prevents caspase activation and protects cells from apoptosis. J. Biol. Chem. 2001, 276:14414-14419.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14414-14419
    • Gnesutta, N.1    Qu, J.2    Minden, A.3
  • 11
    • 36849043083 scopus 로고    scopus 로고
    • Substrate and docking interactions in serine/threonine protein kinases
    • Goldsmith E.J., Akella R., Min X., Zhou T., Humphreys J.M. Substrate and docking interactions in serine/threonine protein kinases. Chem. Rev. 2007, 107:5065-5081.
    • (2007) Chem. Rev. , vol.107 , pp. 5065-5081
    • Goldsmith, E.J.1    Akella, R.2    Min, X.3    Zhou, T.4    Humphreys, J.M.5
  • 13
    • 84857047339 scopus 로고    scopus 로고
    • PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse
    • Database issue
    • Hornbeck P.V., Kornhauser J.M., Tkachev S., Zhang B., Skrzypek E., Murray B., Latham V., Sullivan M. PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse. Nucleic Acids Res. 2012, 40(Database issue):D261-D270.
    • (2012) Nucleic Acids Res. , vol.40
    • Hornbeck, P.V.1    Kornhauser, J.M.2    Tkachev, S.3    Zhang, B.4    Skrzypek, E.5    Murray, B.6    Latham, V.7    Sullivan, M.8
  • 14
    • 0023146453 scopus 로고
    • The influence of basic residues on the substrate specificity of protein kinase C
    • House C., Wettenhall R.E., Kemp B.E. The influence of basic residues on the substrate specificity of protein kinase C. J. Biol. Chem. 1987, 262:772-777.
    • (1987) J. Biol. Chem. , vol.262 , pp. 772-777
    • House, C.1    Wettenhall, R.E.2    Kemp, B.E.3
  • 15
    • 0030766163 scopus 로고    scopus 로고
    • Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog
    • Hubbard S.R. Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog. EMBO J. 1997, 16:5572-5581.
    • (1997) EMBO J. , vol.16 , pp. 5572-5581
    • Hubbard, S.R.1
  • 17
    • 0017638132 scopus 로고
    • Role of multiple basic residues in determining the substrate specificity of cyclic AMP-dependent protein kinase
    • Kemp B.E., Graves D.J., Benjamini E., Krebs E.G. Role of multiple basic residues in determining the substrate specificity of cyclic AMP-dependent protein kinase. J. Biol. Chem. 1977, 252:4888-4894.
    • (1977) J. Biol. Chem. , vol.252 , pp. 4888-4894
    • Kemp, B.E.1    Graves, D.J.2    Benjamini, E.3    Krebs, E.G.4
  • 18
    • 84868676090 scopus 로고    scopus 로고
    • Reciprocal phosphorylation of yeast glycerol-3-phosphate dehydrogenases in adaptation to distinct types of stress
    • Lee Y.J., Jeschke G.R., Roelants F.M., Thorner J., Turk B.E. Reciprocal phosphorylation of yeast glycerol-3-phosphate dehydrogenases in adaptation to distinct types of stress. Mol. Cell. Biol. 2012, 32:4705-4717.
    • (2012) Mol. Cell. Biol. , vol.32 , pp. 4705-4717
    • Lee, Y.J.1    Jeschke, G.R.2    Roelants, F.M.3    Thorner, J.4    Turk, B.E.5
  • 19
    • 0037447059 scopus 로고    scopus 로고
    • Amino acids determining enzyme-substrate specificity in prokaryotic and eukaryotic protein kinases
    • Li L., Shakhnovich E.I., Mirny L.A. Amino acids determining enzyme-substrate specificity in prokaryotic and eukaryotic protein kinases. Proc. Natl. Acad. Sci. USA 2003, 100:4463-4468.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4463-4468
    • Li, L.1    Shakhnovich, E.I.2    Mirny, L.A.3
  • 23
    • 0032878249 scopus 로고    scopus 로고
    • Tyrosine versus serine/threonine phosphorylation by protein kinase casein kinase-2. A study with peptide substrates derived from immunophilin Fpr3
    • Marin O., Meggio F., Sarno S., Cesaro L., Pagano M.A., Pinna L.A. Tyrosine versus serine/threonine phosphorylation by protein kinase casein kinase-2. A study with peptide substrates derived from immunophilin Fpr3. J. Biol. Chem. 1999, 274:29260-29265.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29260-29265
    • Marin, O.1    Meggio, F.2    Sarno, S.3    Cesaro, L.4    Pagano, M.A.5    Pinna, L.A.6
  • 28
    • 0030581751 scopus 로고    scopus 로고
    • How do protein kinases recognize their substratesα
    • Pinna L.A., Ruzzene M. How do protein kinases recognize their substratesα. Biochim. Biophys. Acta 1996, 1314:191-225.
    • (1996) Biochim. Biophys. Acta , vol.1314 , pp. 191-225
    • Pinna, L.A.1    Ruzzene, M.2
  • 31
    • 0035413602 scopus 로고    scopus 로고
    • Physiological substrates of cAMP-dependent protein kinase
    • Shabb J.B. Physiological substrates of cAMP-dependent protein kinase. Chem. Rev. 2001, 101:2381-2411.
    • (2001) Chem. Rev. , vol.101 , pp. 2381-2411
    • Shabb, J.B.1
  • 32
    • 0028818886 scopus 로고
    • How do protein kinases discriminate between serine/threonine and tyrosineα Structural insights from the insulin receptor protein-tyrosine kinase
    • Taylor S.S., Radzio-Andzelm E., Hunter T. How do protein kinases discriminate between serine/threonine and tyrosineα Structural insights from the insulin receptor protein-tyrosine kinase. FASEB J. 1995, 9:1255-1266.
    • (1995) FASEB J. , vol.9 , pp. 1255-1266
    • Taylor, S.S.1    Radzio-Andzelm, E.2    Hunter, T.3
  • 33
    • 34250878954 scopus 로고    scopus 로고
    • Mechanisms of specificity in protein phosphorylation
    • Ubersax J.A., Ferrell J.E. Mechanisms of specificity in protein phosphorylation. Nat. Rev. Mol. Cell Biol. 2007, 8:530-541.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 530-541
    • Ubersax, J.A.1    Ferrell, J.E.2
  • 35
    • 18744373865 scopus 로고    scopus 로고
    • Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-PNP
    • Yang J., Cron P., Good V.M., Thompson V., Hemmings B.A., Barford D. Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-PNP. Nat. Struct. Biol. 2002, 9:940-944.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 940-944
    • Yang, J.1    Cron, P.2    Good, V.M.3    Thompson, V.4    Hemmings, B.A.5    Barford, D.6
  • 36
    • 80051505743 scopus 로고    scopus 로고
    • Identification of specificity determining residues in peptide recognition domains using an information theoretic approach applied to large-scale binding maps
    • Yip K.Y., Utz L., Sitwell S., Hu X., Sidhu S.S., Turk B.E., Gerstein M., Kim P.M. Identification of specificity determining residues in peptide recognition domains using an information theoretic approach applied to large-scale binding maps. BMC Biol. 2011, 9:53.
    • (2011) BMC Biol. , vol.9 , pp. 53
    • Yip, K.Y.1    Utz, L.2    Sitwell, S.3    Hu, X.4    Sidhu, S.S.5    Turk, B.E.6    Gerstein, M.7    Kim, P.M.8
  • 37
    • 27744593477 scopus 로고    scopus 로고
    • A single pair of acidic residues in the kinase major groove mediates strong substrate preference for P-2 or P-5 arginine in the AGC, CAMK, and STE kinase families
    • Zhu G., Fujii K., Liu Y., Codrea V., Herrero J., Shaw S. A single pair of acidic residues in the kinase major groove mediates strong substrate preference for P-2 or P-5 arginine in the AGC, CAMK, and STE kinase families. J. Biol. Chem. 2005, 280:36372-36379.
    • (2005) J. Biol. Chem. , vol.280 , pp. 36372-36379
    • Zhu, G.1    Fujii, K.2    Liu, Y.3    Codrea, V.4    Herrero, J.5    Shaw, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.