메뉴 건너뛰기




Volumn 351, Issue 5, 2005, Pages 1110-1122

Catalytic independent functions of a protein kinase as revealed by a kinase-dead mutant: Study of the Lys72His mutant of cAMP-dependent kinase

Author keywords

cAMP dependent protein kinase; Catalytic mechanism; Hydrogen deuterium exchange; Phosphorylation; Protein dynamics

Indexed keywords

ADENOSINE TRIPHOSPHATE; CYCLIC AMP; DEUTERIUM; LYSINE; MUTANT PROTEIN; PHOSPHOINOSITIDE DEPENDENT PROTEIN KINASE; PROTEIN KINASE; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

EID: 23644439447     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.06.011     Document Type: Article
Times cited : (71)

References (42)
  • 1
    • 0000187410 scopus 로고
    • Conversion of phosphorylase b to phosphorylase a in muscle extracts
    • E.H. Fischer, and E.G. Krebs Conversion of phosphorylase b to phosphorylase a in muscle extracts J. Biol. Chem. 216 1955 121 132
    • (1955) J. Biol. Chem. , vol.216 , pp. 121-132
    • Fischer, E.H.1    Krebs, E.G.2
  • 2
    • 0029020282 scopus 로고
    • Protein kinases 6. the eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • S.K. Hanks, and T. Hunter Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification FASEB J. 9 1995 576 596
    • (1995) FASEB J. , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 4
    • 0019877649 scopus 로고
    • Affinity labeling of cAMP-dependent protein kinase with p-fluorosulfonylbenzoyl adenosine. Covalent modification of lysine 71
    • M.J. Zoller, N.C. Nelson, and S.S. Taylor Affinity labeling of cAMP-dependent protein kinase with p-fluorosulfonylbenzoyl adenosine. Covalent modification of lysine 71 J. Biol. Chem. 256 1981 10837 10842
    • (1981) J. Biol. Chem. , vol.256 , pp. 10837-10842
    • Zoller, M.J.1    Nelson, N.C.2    Taylor, S.S.3
  • 5
    • 0025739664 scopus 로고
    • Rational scanning mutagenesis of a protein kinase identifies functional regions involved in catalysis and substrate interactions
    • C.S. Gibbs, and M.J. Zoller Rational scanning mutagenesis of a protein kinase identifies functional regions involved in catalysis and substrate interactions J. Biol. Chem. 266 1991 8923 8931
    • (1991) J. Biol. Chem. , vol.266 , pp. 8923-8931
    • Gibbs, C.S.1    Zoller, M.J.2
  • 6
    • 0023885305 scopus 로고
    • The protein kinase family: Conserved features and deduced phylogeny of the catalytic domains
    • S.K. Hanks, A.M. Quinn, and T. Hunter The protein kinase family: conserved features and deduced phylogeny of the catalytic domains Science 241 1988 42 52
    • (1988) Science , vol.241 , pp. 42-52
    • Hanks, S.K.1    Quinn, A.M.2    Hunter, T.3
  • 7
    • 0021151496 scopus 로고
    • Direct evidence that oncogenic tyrosine kinases and cyclic AMP-dependent protein kinase have homologous ATP-binding sites
    • M.P. Kamps, S.S. Taylor, and B.M. Sefton Direct evidence that oncogenic tyrosine kinases and cyclic AMP-dependent protein kinase have homologous ATP-binding sites Nature 310 1984 589 592
    • (1984) Nature , vol.310 , pp. 589-592
    • Kamps, M.P.1    Taylor, S.S.2    Sefton, B.M.3
  • 8
    • 0021760630 scopus 로고
    • Adenosine cyclic 3′,5′-monophosphate dependent protein kinase: Nucleotide binding to the chemically modified catalytic subunit
    • D. Bhatnagar, F.T. Hartl, R. Roskoski Jr, R.A. Lessor, and N.J. Leonard Adenosine cyclic 3′,5′-monophosphate dependent protein kinase: nucleotide binding to the chemically modified catalytic subunit Biochemistry 23 1984 4350 4357
    • (1984) Biochemistry , vol.23 , pp. 4350-4357
    • Bhatnagar, D.1    Hartl, F.T.2    Roskoski Jr., R.3    Lessor, R.A.4    Leonard, N.J.5
  • 9
    • 0021266855 scopus 로고
    • Evaluation of the intramolecular stacking of the fluorosulfonylbenzoyl derivatives of 1,-6-ethanoadenosine, adenosine, and guanosine
    • M.A. Jacobson, and R.F. Colman Evaluation of the intramolecular stacking of the fluorosulfonylbenzoyl derivatives of 1,-6-ethanoadenosine, adenosine, and guanosine J. Biol. Chem. 259 1984 1454 1460
    • (1984) J. Biol. Chem. , vol.259 , pp. 1454-1460
    • Jacobson, M.A.1    Colman, R.F.2
  • 10
    • 0024564749 scopus 로고
    • Differential labeling of the catalytic subunit of cAMP-dependent protein kinase with acetic anhydride: Substrate-induced conformational changes
    • J.A. Buechler, and S.S. Taylor Differential labeling of the catalytic subunit of cAMP-dependent protein kinase with acetic anhydride: substrate-induced conformational changes Biochemistry 28 1989 2065 2070
    • (1989) Biochemistry , vol.28 , pp. 2065-2070
    • Buechler, J.A.1    Taylor, S.S.2
  • 12
    • 0035958029 scopus 로고    scopus 로고
    • Structural characterization of protein kinase a as a function of nucleotide binding. Hydrogen-deuterium exchange studies using matrix-assisted laser desorption ionization-time of flight mass spectrometry detection
    • M.D. Andersen, J. Shaffer, P.A. Jennings, and J.A. Adams Structural characterization of protein kinase A as a function of nucleotide binding. Hydrogen-deuterium exchange studies using matrix-assisted laser desorption ionization-time of flight mass spectrometry detection J. Biol. Chem. 276 2001 14204 14211
    • (2001) J. Biol. Chem. , vol.276 , pp. 14204-14211
    • Andersen, M.D.1    Shaffer, J.2    Jennings, P.A.3    Adams, J.A.4
  • 13
    • 0027439438 scopus 로고
    • The conserved lysine of the catalytic domain of protein kinases is actively involved in the phosphotransfer reaction and not required for anchoring ATP
    • A.C. Carrera, K. Alexandrov, and T.M. Roberts The conserved lysine of the catalytic domain of protein kinases is actively involved in the phosphotransfer reaction and not required for anchoring ATP Proc. Natl Acad. Sci. USA 90 1993 442 446
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 442-446
    • Carrera, A.C.1    Alexandrov, K.2    Roberts, T.M.3
  • 14
  • 15
    • 0027529263 scopus 로고
    • Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation
    • Z. Zhang, and D.L. Smith Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation Protein Sci. 2 1993 522 531
    • (1993) Protein Sci. , vol.2 , pp. 522-531
    • Zhang, Z.1    Smith, D.L.2
  • 16
    • 0344392715 scopus 로고    scopus 로고
    • Identification of the protein kinase a regulatory RIalpha-catalytic subunit interface by amide H/2H exchange and protein docking
    • G.S. Anand, D. Law, J.G. Mandell, A.N. Snead, I. Tsigelny, and S.S. Taylor Identification of the protein kinase A regulatory RIalpha-catalytic subunit interface by amide H/2H exchange and protein docking Proc. Natl Acad. Sci. USA 100 2003 13264 13269
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 13264-13269
    • Anand, G.S.1    Law, D.2    Mandell, J.G.3    Snead, A.N.4    Tsigelny, I.5    Taylor, S.S.6
  • 18
    • 12344334691 scopus 로고    scopus 로고
    • Allosteric network of cAMP-dependent protein kinase revealed by mutation of Tyr204 in the P+1 loop
    • J. Yang, S.M. Garrod, M.S. Deal, G.S. Anand, J. Woods, L. Virgil, and S. Taylor Allosteric network of cAMP-dependent protein kinase revealed by mutation of Tyr204 in the P+1 loop J. Mol. Biol 2005 In the press
    • (2005) J. Mol. Biol
    • Yang, J.1    Garrod, S.M.2    Deal, M.S.3    Anand, G.S.4    Woods, J.5    Virgil, L.6    Taylor, S.7
  • 19
    • 0035969987 scopus 로고    scopus 로고
    • Changes in protein conformational mobility upon activation of extracellular regulated protein kinase-2 as detected by hydrogen exchange
    • A.N. Hoofnagle, K.A. Resing, E.J. Goldsmith, and N.G. Ahn Changes in protein conformational mobility upon activation of extracellular regulated protein kinase-2 as detected by hydrogen exchange Proc. Natl Acad. Sci. USA 98 2001 956 961
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 956-961
    • Hoofnagle, A.N.1    Resing, K.A.2    Goldsmith, E.J.3    Ahn, N.G.4
  • 20
    • 33645179040 scopus 로고    scopus 로고
    • Consequences of lysine 72 mutation on the phosphorylation and activation state of PKA
    • G.H. Iyer, M.J. Moore, and S.S. Taylor Consequences of lysine 72 mutation on the phosphorylation and activation state of PKA J. Biol. Chem. 2004 In the press
    • (2004) J. Biol. Chem.
    • Iyer, G.H.1    Moore, M.J.2    Taylor, S.S.3
  • 21
    • 0033815252 scopus 로고    scopus 로고
    • Insights into nucleotide binding in protein kinase a using fluorescent adenosine derivatives
    • Q. Ni, J. Shaffer, and J.A. Adams Insights into nucleotide binding in protein kinase A using fluorescent adenosine derivatives Protein Sci. 9 2000 1818 1827
    • (2000) Protein Sci. , vol.9 , pp. 1818-1827
    • Ni, Q.1    Shaffer, J.2    Adams, J.A.3
  • 22
    • 0029932259 scopus 로고    scopus 로고
    • Active site mutations define the pathway for the cooperative activation of cAMP-dependent protein kinase
    • F.W. Herberg, S.S. Taylor, and W.R.G. Dostmann Active site mutations define the pathway for the cooperative activation of cAMP-dependent protein kinase Biochemistry 35 1996 2934 2942
    • (1996) Biochemistry , vol.35 , pp. 2934-2942
    • Herberg, F.W.1    Taylor, S.S.2    Dostmann, W.R.G.3
  • 25
    • 0026640184 scopus 로고
    • Systematic mutational analysis of cAMP-dependent protein kinase identifies unregulated catalytic subunits and defines regions important for the recognition of the regulatory subunit
    • C.S. Gibbs, D.R. Knighton, J.M. Sowadski, S.S. Taylor, and M.J. Zoller Systematic mutational analysis of cAMP-dependent protein kinase identifies unregulated catalytic subunits and defines regions important for the recognition of the regulatory subunit J. Biol. Chem. 267 1992 4806 4814
    • (1992) J. Biol. Chem. , vol.267 , pp. 4806-4814
    • Gibbs, C.S.1    Knighton, D.R.2    Sowadski, J.M.3    Taylor, S.S.4    Zoller, M.J.5
  • 26
    • 0026098765 scopus 로고
    • A kinase-negative mutant of S49 mouse lymphoma cells is defective in posttranslational maturation of catalytic subunit of cyclic AMP-dependent protein kinase
    • R.A. Steinberg A kinase-negative mutant of S49 mouse lymphoma cells is defective in posttranslational maturation of catalytic subunit of cyclic AMP-dependent protein kinase Mol. Cell. Biol. 11 1991 705 712
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 705-712
    • Steinberg, R.A.1
  • 27
    • 0037436388 scopus 로고    scopus 로고
    • Dynamic features of cAMP-dependent protein kinase revealed by apoenzyme crystal structure
    • P. Akamine, Wu J. Madhusudan, N.H. Xuong, L.F. Ten Eyck, and S.S. Taylor Dynamic features of cAMP-dependent protein kinase revealed by apoenzyme crystal structure J. Mol. Biol 327 2003 159 171
    • (2003) J. Mol. Biol , vol.327 , pp. 159-171
    • Akamine, P.1    Madhusudan Wu, J.2    Xuong, N.H.3    Ten Eyck, L.F.4    Taylor, S.S.5
  • 28
  • 30
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • F. Sicheri, I. Moarefi, and J. Kuriyan Crystal structure of the Src family tyrosine kinase Hck Nature 385 1997 602 609
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 31
    • 0028898390 scopus 로고
    • Phosphorylation modulates catalytic function and regulation in the cAMP-dependent protein kinase
    • J.A. Adams, M.L. McGlone, R. Gibson, and S.S. Taylor Phosphorylation modulates catalytic function and regulation in the cAMP-dependent protein kinase Biochemistry 34 1995 2447 2454
    • (1995) Biochemistry , vol.34 , pp. 2447-2454
    • Adams, J.A.1    McGlone, M.L.2    Gibson, R.3    Taylor, S.S.4
  • 33
    • 3142748521 scopus 로고    scopus 로고
    • Casein kinase Iepsilon plays a functional role in the transforming growth factor-beta signaling pathway
    • D.S. Waddell, N.T. Liberati, X. Guo, J.P. Frederick, and X.-F. Wang Casein kinase Iepsilon plays a functional role in the transforming growth factor-beta signaling pathway J. Biol. Chem 279 2004 27965 27970
    • (2004) J. Biol. Chem , vol.279 , pp. 27965-27970
    • Waddell, D.S.1    Liberati, N.T.2    Guo, X.3    Frederick, J.P.4    Wang, X.-F.5
  • 34
    • 3142619126 scopus 로고    scopus 로고
    • EphB1-mediated cell migration requires the phosphorylation of paxillin at Y31/Y118
    • C. Vindis, T. Teli, D.P. Cerretti, C.E. Turner, and U. Huynh-Do EphB1-mediated cell migration requires the phosphorylation of paxillin at Y31/Y118 J. Biol. Chem 279 2004 29236 29246
    • (2004) J. Biol. Chem , vol.279 , pp. 29236-29246
    • Vindis, C.1    Teli, T.2    Cerretti, D.P.3    Turner, C.E.4    Huynh-Do, U.5
  • 35
    • 1942480203 scopus 로고    scopus 로고
    • A dominant negative mutant of TLK1 causes chromosome missegregation and aneuploidy in normal breast epithelial cells
    • G. Sunavala-Dossabhoy, Y. Li, B. Williams, and A. De Benedetti A dominant negative mutant of TLK1 causes chromosome missegregation and aneuploidy in normal breast epithelial cells BMC Cell. Biol. 4 2003 16
    • (2003) BMC Cell. Biol. , vol.4 , pp. 16
    • Sunavala-Dossabhoy, G.1    Li, Y.2    Williams, B.3    De Benedetti, A.4
  • 36
    • 0037033032 scopus 로고    scopus 로고
    • Phosphorylation of the catalytic subunit of protein kinase A. Autophosphorylation versus phosphorylation by phosphoinositide-dependent kinase-1
    • M.J. Moore, J.R. Kanter, K.C. Jones, and S.S. Taylor Phosphorylation of the catalytic subunit of protein kinase A. Autophosphorylation versus phosphorylation by phosphoinositide-dependent kinase-1 J. Biol. Chem. 277 2002 47878 47884
    • (2002) J. Biol. Chem. , vol.277 , pp. 47878-47884
    • Moore, M.J.1    Kanter, J.R.2    Jones, K.C.3    Taylor, S.S.4
  • 38
    • 0038810081 scopus 로고    scopus 로고
    • Protein structure change studied by hydrogen-deuterium exchange, functional labeling, and mass spectrometry
    • J.J. Englander, C. Del Mar, W. Li, S.W. Englander, J.S. Kim, and D.D. Stranz Protein structure change studied by hydrogen-deuterium exchange, functional labeling, and mass spectrometry Proc. Natl Acad. Sci. USA 100 2003 7057 7062
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 7057-7062
    • Englander, J.J.1    Del Mar, C.2    Li, W.3    Englander, S.W.4    Kim, J.S.5    Stranz, D.D.6
  • 39
    • 1642514905 scopus 로고    scopus 로고
    • Rapid refinement of crystallographic protein construct definition employing enhanced hydrogen/deuterium exchange mass spectrometry (DXMS)
    • D. Pantazatos, J.S. Kim, H.E. Klock, R.C. Stevens, I.A. Wilson, S.A. Lesley, and V.L. Woods Jr Rapid refinement of crystallographic protein construct definition employing enhanced hydrogen/deuterium exchange mass spectrometry (DXMS) Proc. Natl Acad. Sci. USA 101 2004 751 756
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 751-756
    • Pantazatos, D.1    Kim, J.S.2    Klock, H.E.3    Stevens, R.C.4    Wilson, I.A.5    Lesley, S.A.6    Woods Jr., V.L.7
  • 40
    • 15744369881 scopus 로고    scopus 로고
    • High resolution, high throughput amide deuterium exchange mass spectrometry (DXMS) determination of the dynamics and structure of protein-protein interactions
    • V.J. Woods High resolution, high throughput amide deuterium exchange mass spectrometry (DXMS) determination of the dynamics and structure of protein-protein interactions J. Am. Soc. Mass Spectrom. 13 2002 14S
    • (2002) J. Am. Soc. Mass Spectrom. , vol.13
    • Woods, V.J.1
  • 41
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • C.N. Pace Determination and analysis of urea and guanidine hydrochloride denaturation curves Methods Enzymol. 131 1986 266 280
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 42
    • 0028305073 scopus 로고
    • Crosstalk between domains in the regulatory subunit of cAMP-dependent protein kinase: Influence of amino terminus on cAMP binding and holoenzyme formation
    • F.W. Herberg, W.R. Dostmann, M. Zorn, S.J. Davis, and S.S. Taylor Crosstalk between domains in the regulatory subunit of cAMP-dependent protein kinase: influence of amino terminus on cAMP binding and holoenzyme formation Biochemistry 33 1994 7485 7494
    • (1994) Biochemistry , vol.33 , pp. 7485-7494
    • Herberg, F.W.1    Dostmann, W.R.2    Zorn, M.3    Davis, S.J.4    Taylor, S.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.