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Volumn 18, Issue 11, 2011, Pages 1463-1473

Allosteric regulation of protein kinase PKCζ by the N-terminal C1 domain and small compounds to the PIF-pocket

Author keywords

[No Author keywords available]

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; PROTEIN KINASE C; PROTEIN KINASE C ZETA;

EID: 80053904856     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2011.08.010     Document Type: Article
Times cited : (57)

References (43)
  • 1
    • 0037954572 scopus 로고    scopus 로고
    • Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions
    • DOI 10.1042/BJ20021641
    • R.M. Biondi, and A.R. Nebreda Signalling specificity of Ser/Thr protein kinases through docking-site-mediated interactions Biochem. J. 372 2003 1 13 (Pubitemid 36609602)
    • (2003) Biochemical Journal , vol.372 , Issue.1 , pp. 1-13
    • Biondi, R.M.1    Nebreda, A.R.2
  • 2
    • 0034161251 scopus 로고    scopus 로고
    • Identification of a pocket in the PDK1 kinase domain that interacts with PIF and the C-terminal residues of PKA
    • R.M. Biondi, P.C. Cheung, A. Casamayor, M. Deak, R.A. Currie, and D.R. Alessi Identification of a pocket in the PDK1 kinase domain that interacts with PIF and the C-terminal residues of PKA EMBO J. 19 2000 979 988 (Pubitemid 30119823)
    • (2000) EMBO Journal , vol.19 , Issue.5 , pp. 979-988
    • Biondi, R.M.1    Cheung, P.C.F.2    Casamayor, A.3    Deak, M.4    Currie, R.A.5    Alessi, D.R.6
  • 3
    • 0037102153 scopus 로고    scopus 로고
    • High resolution crystal structure of the human PDK1 catalytic domain defines the regulatory phosphopeptide docking site
    • R.M. Biondi, D. Komander, C.C. Thomas, J.M. Lizcano, M. Deak, D.R. Alessi, and D.M. van Aalten High resolution crystal structure of the human PDK1 catalytic domain defines the regulatory phosphopeptide docking site EMBO J. 21 2002 4219 4228
    • (2002) EMBO J. , vol.21 , pp. 4219-4228
    • Biondi, R.M.1    Komander, D.2    Thomas, C.C.3    Lizcano, J.M.4    Deak, M.5    Alessi, D.R.6    Van Aalten, D.M.7
  • 4
    • 0036527429 scopus 로고    scopus 로고
    • Protein kinases - The major drug targets of the twenty-first century?
    • P. Cohen Protein kinases - the major drug targets of the twenty-first century? Nat. Rev. Drug Discov. 1 2002 309 315 (Pubitemid 37361447)
    • (2002) Nature Reviews Drug Discovery , vol.1 , Issue.4 , pp. 309-315
    • Cohen, P.1
  • 9
    • 0037107414 scopus 로고    scopus 로고
    • A phosphoserine/threonine-binding pocket in AGC kinases and PDK1 mediates activation by hydrophobic motif phosphorylation
    • DOI 10.1093/emboj/cdf551
    • M. Frödin, T.L. Antal, B.A. Dümmler, C.J. Jensen, M. Deak, S. Gammeltoft, and R.M. Biondi A phosphoserine/threonine-binding pocket in AGC kinases and PDK1 mediates activation by hydrophobic motif phosphorylation EMBO J. 21 2002 5396 5407 (Pubitemid 35231019)
    • (2002) EMBO Journal , vol.21 , Issue.20 , pp. 5396-5407
    • Frodin, M.1    Antal, T.L.2    Dummler, B.A.3    Jensen, C.J.4    Deak, M.5    Gammeltoft, S.6    Biondi, R.M.7
  • 13
    • 0642376906 scopus 로고    scopus 로고
    • Protein kinase Cζ (PKCζ): Activation mechanisms and cellular functions
    • DOI 10.1093/jb/mvg017
    • T. Hirai, and K. Chida Protein kinase Czeta (PKCzeta): activation mechanisms and cellular functions J. Biochem. 133 2003 1 7 (Pubitemid 36240972)
    • (2003) Journal of Biochemistry , vol.133 , Issue.1 , pp. 1-7
    • Hirai, T.1    Chida, K.2
  • 14
    • 0023555557 scopus 로고
    • Protein kinase C contains a pseudosubstrate prototope in its regulatory domain
    • C. House, and B.E. Kemp Protein kinase C contains a pseudosubstrate prototope in its regulatory domain Science 238 1987 1726 1728 (Pubitemid 18046276)
    • (1987) Science , vol.238 , Issue.4834 , pp. 1726-1728
    • House, C.1    Kemp, B.E.2
  • 16
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • DOI 10.1016/S0092-8674(02)00741-9
    • M. Huse, and J. Kuriyan The conformational plasticity of protein kinases Cell 109 2002 275 282 (Pubitemid 34606870)
    • (2002) Cell , vol.109 , Issue.3 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 17
    • 0035421216 scopus 로고    scopus 로고
    • Novel modular domain PB1 recognizes pc motif to mediate functional protein-protein interactions
    • DOI 10.1093/emboj/20.15.3938
    • T. Ito, Y. Matsui, T. Ago, K. Ota, and H. Sumimoto Novel modular domain PB1 recognizes PC motif to mediate functional protein-protein interactions EMBO J. 20 2001 3938 3946 (Pubitemid 32751810)
    • (2001) EMBO Journal , vol.20 , Issue.15 , pp. 3938-3946
    • Ito, T.1    Matsui, Y.2    Ago, T.3    Ota, K.4    Sumimoto, H.5
  • 18
    • 0041845195 scopus 로고    scopus 로고
    • Inhibition of protein kinase C catalytic activity by additional regions within the human protein kinase Cα-regulatory domain lying outside of the pseudosubstrate sequence
    • DOI 10.1042/BJ20030011
    • A.F. Kirwan, A.C. Bibby, T. Mvilongo, H. Riedel, T. Burke, S.Z. Millis, and A.M. Parissenti Inhibition of protein kinase C catalytic activity by additional regions within the human protein kinase Calpha-regulatory domain lying outside of the pseudosubstrate sequence Biochem. J. 373 2003 571 581 (Pubitemid 36897859)
    • (2003) Biochemical Journal , vol.373 , Issue.2 , pp. 571-581
    • Kirwan, A.F.1    Bibby, A.C.2    Mvilongo, T.3    Riedel, H.4    Burke, T.5    Millis, S.Z.6    Parissenti, A.M.7
  • 19
    • 0025882867 scopus 로고
    • Crystallization studies of cAMP-dependent protein kinase. Cocrystals of the catalytic subunit with a 20 amino acid residue peptide inhibitor and MgATP diffract to 3.0 A resolution
    • D.R. Knighton, N.H. Xuong, S.S. Taylor, and J.M. Sowadski Crystallization studies of cAMP-dependent protein kinase. Cocrystals of the catalytic subunit with a 20 amino acid residue peptide inhibitor and MgATP diffract to 3.0 A resolution J. Mol. Biol. 220 1991 217 220
    • (1991) J. Mol. Biol. , vol.220 , pp. 217-220
    • Knighton, D.R.1    Xuong, N.H.2    Taylor, S.S.3    Sowadski, J.M.4
  • 20
    • 0026342401 scopus 로고
    • Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase
    • D.R. Knighton, J.H. Zheng, L.F. Ten Eyck, V.A. Ashford, N.H. Xuong, S.S. Taylor, and J.M. Sowadski Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase Science 253 1991 407 414 (Pubitemid 21917165)
    • (1991) Science , vol.253 , Issue.5018 , pp. 407-414
    • Knighton, D.R.1    Zheng, J.2    Ten Eyck, L.F.3    Ashford, V.A.4    Xuong, N.-H.5    Taylor, S.S.6    Sowadski, J.M.7
  • 21
    • 1542284650 scopus 로고    scopus 로고
    • Molecular mechanisms regulating protein kinase Cζ turnover and cellular transformation
    • DOI 10.1042/BJ20031194
    • J.A. Le Good, and D.N. Brindley Molecular mechanisms regulating protein kinase Czeta turnover and cellular transformation Biochem. J. 378 2004 83 92 (Pubitemid 38299546)
    • (2004) Biochemical Journal , vol.378 , Issue.1 , pp. 83-92
    • Le Good, J.A.1    Brindley, D.N.2
  • 22
    • 78650942010 scopus 로고    scopus 로고
    • Crystal structure and allosteric activation of protein kinase C βiI
    • T.A. Leonard, B. Róycki, L.F. Saidi, G. Hummer, and J.H. Hurley Crystal structure and allosteric activation of protein kinase C βII Cell 144 2011 55 66
    • (2011) Cell , vol.144 , pp. 55-66
    • Leonard, T.A.1    Róycki, B.2    Saidi, L.F.3    Hummer, G.4    Hurley, J.H.5
  • 23
    • 0035413599 scopus 로고    scopus 로고
    • Phosphoinositide-regulated kinases and phosphoinositide phosphatases
    • DOI 10.1021/cr000091i
    • N.R. Leslie, R.M. Biondi, and D.R. Alessi Phosphoinositide-regulated kinases and phosphoinositide phosphatases Chem. Rev. 101 2001 2365 2380 (Pubitemid 35373024)
    • (2001) Chemical Reviews , vol.101 , Issue.8 , pp. 2365-2380
    • Leslie, N.R.1    Biondi, R.M.2    Alessi, D.R.3
  • 24
    • 78650308842 scopus 로고    scopus 로고
    • Lysine methylation of the NF-κB subunit RelA by SETD6 couples activity of the histone methyltransferase GLP at chromatin to tonic repression of NF-κB signaling
    • D. Levy, A.J. Kuo, Y. Chang, U. Schaefer, C. Kitson, P. Cheung, A. Espejo, B.M. Zee, C.L. Liu, and S. Tangsombatvisit Lysine methylation of the NF-κB subunit RelA by SETD6 couples activity of the histone methyltransferase GLP at chromatin to tonic repression of NF-κB signaling Nat. Immunol. 12 2011 29 36
    • (2011) Nat. Immunol. , vol.12 , pp. 29-36
    • Levy, D.1    Kuo, A.J.2    Chang, Y.3    Schaefer, U.4    Kitson, C.5    Cheung, P.6    Espejo, A.7    Zee, B.M.8    Liu, C.L.9    Tangsombatvisit, S.10
  • 25
    • 24644488646 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of human atypical protein kinase C-iota reveals interaction mode of phosphorylation site in turn motif
    • DOI 10.1016/j.jmb.2005.07.060, PII S0022283605008612
    • A. Messerschmidt, S. Macieira, M. Velarde, M. Bädeker, C. Benda, A. Jestel, H. Brandstetter, T. Neuefeind, and M. Blaesse Crystal structure of the catalytic domain of human atypical protein kinase C-iota reveals interaction mode of phosphorylation site in turn motif J. Mol. Biol. 352 2005 918 931 (Pubitemid 41267077)
    • (2005) Journal of Molecular Biology , vol.352 , Issue.4 , pp. 918-931
    • Messerschmidt, A.1    Macieira, S.2    Velarde, M.3    Badeker, M.4    Benda, C.5    Jestel, A.6    Brandstetter, H.7    Neuefeind, T.8    Blaesse, M.9
  • 26
    • 0025743856 scopus 로고
    • Peptides that mimic the pseudosubstrate region of protein kinase C bind to acidic lipids in membranes
    • M. Mosior, and S. McLaughlin Peptides that mimic the pseudosubstrate region of protein kinase C bind to acidic lipids in membranes Biophys. J. 60 1991 149 159
    • (1991) Biophys. J. , vol.60 , pp. 149-159
    • Mosior, M.1    McLaughlin, S.2
  • 27
    • 0029003788 scopus 로고
    • PKC zeta is a molecular switch in signal transduction of TNF-alpha, bifunctionally regulated by ceramide and arachidonic acid
    • G. Müller, M. Ayoub, P. Storz, J. Rennecke, D. Fabbro, and K. Pfizenmaier PKC zeta is a molecular switch in signal transduction of TNF-alpha, bifunctionally regulated by ceramide and arachidonic acid EMBO J. 14 1995 1961 1969
    • (1995) EMBO J. , vol.14 , pp. 1961-1969
    • Müller, G.1    Ayoub, M.2    Storz, P.3    Rennecke, J.4    Fabbro, D.5    Pfizenmaier, K.6
  • 28
    • 0026658539 scopus 로고
    • Purification and characterization of the zeta isoform of protein kinase C from bovine kidney
    • H. Nakanishi, and J.H. Exton Purification and characterization of the zeta isoform of protein kinase C from bovine kidney J. Biol. Chem. 267 1992 16347 16354
    • (1992) J. Biol. Chem. , vol.267 , pp. 16347-16354
    • Nakanishi, H.1    Exton, J.H.2
  • 30
    • 0035213641 scopus 로고    scopus 로고
    • AGC protein kinase phosphorylation and protein kinase C
    • DOI 10.1042/0300-5127:0290860
    • P.J. Parker, and S.J. Parkinson AGC protein kinase phosphorylation and protein kinase C Biochem. Soc. Trans. 29 2001 860 863 (Pubitemid 33131794)
    • (2001) Biochemical Society Transactions , vol.29 , Issue.6 , pp. 860-863
    • Parker, P.J.1    Parkinson, S.J.2
  • 31
    • 20444383859 scopus 로고    scopus 로고
    • Protein phosphorylation in signaling - 50 Years and counting
    • DOI 10.1016/j.tibs.2005.04.013, PII S0968000405001210, Celebrating 50 Years of the IUBMB
    • T. Pawson, and J.D. Scott Protein phosphorylation in signaling - 50 years and counting Trends Biochem. Sci. 30 2005 286 290 (Pubitemid 40799044)
    • (2005) Trends in Biochemical Sciences , vol.30 , Issue.6 , pp. 286-290
    • Pawson, T.1    Scott, J.D.2
  • 35
    • 33847061197 scopus 로고    scopus 로고
    • Networks for the allosteric control of protein kinases
    • DOI 10.1016/j.sbi.2006.10.011, PII S0959440X06001849, Catalysis and Regulation / Proteins
    • Z. Shi, K.A. Resing, and N.G. Ahn Networks for the allosteric control of protein kinases Curr. Opin. Struct. Biol. 16 2006 686 692 (Pubitemid 44827734)
    • (2006) Current Opinion in Structural Biology , vol.16 , Issue.6 , pp. 686-692
    • Shi, Z.1    Resing, K.A.2    Ahn, N.G.3
  • 37
    • 68549123439 scopus 로고    scopus 로고
    • 3,5-Diphenylpent-2-enoic acids as allosteric activators of the protein kinase PDK1: Structure-activity relationships and thermodynamic characterization of binding as paradigms for PIF-binding pocket-targeting compounds
    • A. Stroba, F. Schaeffer, V. Hindie, L. Lopez-Garcia, I. Adrian, W. Fröhner, R.W. Hartmann, R.M. Biondi, and M. Engel 3,5-Diphenylpent-2-enoic acids as allosteric activators of the protein kinase PDK1: structure-activity relationships and thermodynamic characterization of binding as paradigms for PIF-binding pocket-targeting compounds J. Med. Chem. 52 2009 4683 4693
    • (2009) J. Med. Chem. , vol.52 , pp. 4683-4693
    • Stroba, A.1    Schaeffer, F.2    Hindie, V.3    Lopez-Garcia, L.4    Adrian, I.5    Fröhner, W.6    Hartmann, R.W.7    Biondi, R.M.8    Engel, M.9
  • 39
    • 77954316554 scopus 로고    scopus 로고
    • Design and synthesis of benzoazepin-2-one analogs as allosteric binders targeting the PIF pocket of PDK1
    • L.Y. Wei, X.Q. Gao, R. Warne, X.S. Hao, D. Bussiere, X.J. Gu, T. Uno, and Y. Liu Design and synthesis of benzoazepin-2-one analogs as allosteric binders targeting the PIF pocket of PDK1 Bioorg. Med. Chem. Lett. 20 2010 3897 3902
    • (2010) Bioorg. Med. Chem. Lett. , vol.20 , pp. 3897-3902
    • Wei, L.Y.1    Gao, X.Q.2    Warne, R.3    Hao, X.S.4    Bussiere, D.5    Gu, X.J.6    Uno, T.7    Liu, Y.8
  • 40
    • 77958576132 scopus 로고    scopus 로고
    • Crystal structure of human AKT1 with an allosteric inhibitor reveals a new mode of kinase inhibition
    • W.I. Wu, W.C. Voegtli, H.L. Sturgis, F.P. Dizon, G.P. Vigers, and B.J. Brandhuber Crystal structure of human AKT1 with an allosteric inhibitor reveals a new mode of kinase inhibition PLoS ONE 5 2010 e12913
    • (2010) PLoS ONE , vol.5 , pp. 12913
    • Wu, W.I.1    Voegtli, W.C.2    Sturgis, H.L.3    Dizon, F.P.4    Vigers, G.P.5    Brandhuber, B.J.6
  • 41
    • 18744373865 scopus 로고    scopus 로고
    • Crystal structure of an activated Akt/Protein Kinase B ternary complex with GSK3-peptide and AMP-PNP
    • DOI 10.1038/nsb870
    • J. Yang, P. Cron, V.M. Good, V. Thompson, B.A. Hemmings, and D. Barford Crystal structure of an activated Akt/protein kinase B ternary complex with GSK3-peptide and AMP-PNP Nat. Struct. Biol. 9 2002 940 944 (Pubitemid 35417064)
    • (2002) Nature Structural Biology , vol.9 , Issue.12 , pp. 940-944
    • Yang, J.1    Cron, P.2    Good, V.M.3    Thompson, V.4    Hemmings, B.A.5    Barford, D.6
  • 42
    • 0036295728 scopus 로고    scopus 로고
    • Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation
    • DOI 10.1016/S1097-2765(02)00550-6
    • J. Yang, P. Cron, V. Thompson, V.M. Good, D. Hess, B.A. Hemmings, and D. Barford Molecular mechanism for the regulation of protein kinase B/Akt by hydrophobic motif phosphorylation Mol. Cell 9 2002 1227 1240 (Pubitemid 34722302)
    • (2002) Molecular Cell , vol.9 , Issue.6 , pp. 1227-1240
    • Yang, J.1    Cron, P.2    Thompson, V.3    Good, V.M.4    Hess, D.5    Hemmings, B.A.6    Barford, D.7
  • 43
    • 77249169281 scopus 로고    scopus 로고
    • Turning enzymes on with small molecules
    • J.A. Zorn, and J.A. Wells Turning enzymes ON with small molecules Nat. Chem. Biol. 6 2010 179 188
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 179-188
    • Zorn, J.A.1    Wells, J.A.2


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