메뉴 건너뛰기




Volumn 19, Issue 9, 2012, Pages 1152-1163

Substrate-selective inhibition of protein kinase PDK1 by small compounds that bind to the PIF-pocket allosteric docking site

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHOINOSITIDE DEPENDENT PROTEIN KINASE 1; PIF PROTEIN; PROTEIN KINASE; PROTEIN KINASE B; PROTEIN KINASE INHIBITOR; PS 182; PS 210; PS 423; S6 KINASE; UNCLASSIFIED DRUG;

EID: 84866652604     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2012.07.017     Document Type: Article
Times cited : (65)

References (43)
  • 1
    • 79955664598 scopus 로고    scopus 로고
    • Chronically increased S6K1 is associated with impaired IRS1 signaling in skeletal muscle of GDM women with impaired glucose tolerance postpartum
    • L.A. Barbour, C.E. McCurdy, T.L. Hernandez, and J.E. Friedman Chronically increased S6K1 is associated with impaired IRS1 signaling in skeletal muscle of GDM women with impaired glucose tolerance postpartum J. Clin. Endocrinol. Metab. 96 2011 1431 1441
    • (2011) J. Clin. Endocrinol. Metab. , vol.96 , pp. 1431-1441
    • Barbour, L.A.1    McCurdy, C.E.2    Hernandez, T.L.3    Friedman, J.E.4
  • 2
    • 0034625161 scopus 로고    scopus 로고
    • Snapping of the carboxyl terminal tail of the catalytic subunit of PKA onto its core: Characterization of the sites by mutagenesis
    • DOI 10.1021/bi000153z
    • M. Batkin, I. Schvartz, and S. Shaltiel Snapping of the carboxyl terminal tail of the catalytic subunit of PKA onto its core: characterization of the sites by mutagenesis Biochemistry 39 2000 5366 5373 (Pubitemid 30257076)
    • (2000) Biochemistry , vol.39 , Issue.18 , pp. 5366-5373
    • Batkin, M.1    Schvartz, I.2    Shaltiel, S.3
  • 4
    • 1542286168 scopus 로고    scopus 로고
    • Phosphoinositide-dependent protein kinase 1, a sensor of protein conformation
    • DOI 10.1016/j.tibs.2004.01.005, PII S0968000404000222
    • R.M. Biondi Phosphoinositide-dependent protein kinase 1, a sensor of protein conformation Trends Biochem. Sci. 29 2004 136 142 (Pubitemid 38314859)
    • (2004) Trends in Biochemical Sciences , vol.29 , Issue.3 , pp. 136-142
    • Biondi, R.M.1
  • 5
    • 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
  • 6
    • 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
  • 7
    • 0035882103 scopus 로고    scopus 로고
    • The PIF-binding pocket in PDK1 is essential for activation of S6K and SGK, but not PKB
    • DOI 10.1093/emboj/20.16.4380
    • R.M. Biondi, A. Kieloch, R.A. Currie, M. Deak, and D.R. Alessi The PIF-binding pocket in PDK1 is essential for activation of S6K and SGK, but not PKB EMBO J. 20 2001 4380 4390 (Pubitemid 32772032)
    • (2001) EMBO Journal , vol.20 , Issue.16 , pp. 4380-4390
    • Biondi, R.M.1    Kieloch, A.2    Currie, R.A.3    Deak, M.4    Alessi, D.R.5
  • 8
    • 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
  • 10
    • 65649098029 scopus 로고    scopus 로고
    • Phosphorylation of IRS proteins, insulin action, and insulin resistance
    • S. Boura-Halfon, and Y. Zick Phosphorylation of IRS proteins, insulin action, and insulin resistance Am. J. Physiol. Endocrinol. Metab. 296 2009 E581 E591
    • (2009) Am. J. Physiol. Endocrinol. Metab. , vol.296
    • Boura-Halfon, S.1    Zick, Y.2
  • 11
    • 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
  • 12
    • 0042967831 scopus 로고    scopus 로고
    • In vivo role of the PIF-binding docking site of PDK1 defined by knock-in mutation
    • DOI 10.1093/emboj/cdg407
    • B.J. Collins, M. Deak, J.S. Arthur, L.J. Armit, and D.R. Alessi In vivo role of the PIF-binding docking site of PDK1 defined by knock-in mutation EMBO J. 22 2003 4202 4211 (Pubitemid 37021748)
    • (2003) EMBO Journal , vol.22 , Issue.16 , pp. 4202-4211
    • Collins, B.J.1    Deak, M.2    Arthur, J.S.C.3    Armit, L.J.4    Alessi, D.R.5
  • 13
    • 27944482145 scopus 로고    scopus 로고
    • In vivo role of the phosphate groove of PDK1 defined by knockin mutation
    • DOI 10.1242/jcs.02617
    • B.J. Collins, M. Deak, V. Murray-Tait, K.G. Storey, and D.R. Alessi In vivo role of the phosphate groove of PDK1 defined by knockin mutation J. Cell Sci. 118 2005 5023 5034 (Pubitemid 41672433)
    • (2005) Journal of Cell Science , vol.118 , Issue.21 , pp. 5023-5034
    • Collins, B.J.1    Deak, M.2    Murray-Tait, V.3    Storey, K.G.4    Alessi, D.R.5
  • 15
    • 0030865577 scopus 로고    scopus 로고
    • The catalytic subunit of Dictyostelium cAMP-dependent protein kinase. Role of the N-terminal domain and of the C-terminal residues in catalytic activity and stability
    • L.C. Etchebehere, M.X. Van Bemmelen, C. Anjard, F. Traincard, K. Assemat, C. Reymond, and M. Véron The catalytic subunit of Dictyostelium cAMP-dependent protein kinase - role of the N-terminal domain and of the C-terminal residues in catalytic activity and stability Eur. J. Biochem. 248 1997 820 826 (Pubitemid 27400037)
    • (1997) European Journal of Biochemistry , vol.248 , Issue.3 , pp. 820-826
    • Etchebehere, L.C.1    Van Bemmelen, M.X.P.2    Anjard, C.3    Traincard, F.4    Assemat, K.5    Reymond, C.6    Veron, M.7
  • 17
    • 0034969088 scopus 로고    scopus 로고
    • A common phosphate binding site explains the unique substrate specificity of GSK3 and its inactivation by phosphorylation
    • DOI 10.1016/S1097-2765(01)00253-2
    • S. Frame, P. Cohen, and R.M. Biondi A common phosphate binding site explains the unique substrate specificity of GSK3 and its inactivation by phosphorylation Mol. Cell 7 2001 1321 1327 (Pubitemid 32607364)
    • (2001) Molecular Cell , vol.7 , Issue.6 , pp. 1321-1327
    • Frame, S.1    Cohen, P.2    Biondi, R.M.3
  • 18
    • 0242612949 scopus 로고    scopus 로고
    • A phosphoserine-regulated docking site in the protein kinase RSK2 that recruits and activates PDK1
    • M. Frödin, C.J. Jensen, K. Merienne, and S. Gammeltoft A phosphoserine-regulated docking site in the protein kinase RSK2 that recruits and activates PDK1 EMBO J. 19 2000 2924 2934 (Pubitemid 30386764)
    • (2000) EMBO Journal , vol.19 , Issue.12 , pp. 2924-2934
    • Frodin, M.1    Jensen, C.J.2    Merienne, K.3    Gammeltoft, S.4
  • 19
    • 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
  • 24
    • 0035413607 scopus 로고    scopus 로고
    • Structural basis for control by phosphorylation
    • DOI 10.1021/cr000225s
    • L.N. Johnson, and R.J. Lewis Structural basis for control by phosphorylation Chem. Rev. 101 2001 2209 2242 (Pubitemid 35373017)
    • (2001) Chemical Reviews , vol.101 , Issue.8 , pp. 2209-2242
    • Johnson, L.N.1    Lewis, R.J.2
  • 25
    • 79959568260 scopus 로고    scopus 로고
    • Hydrophobic motif phosphorylation is not required for activation loop phosphorylation of p70 ribosomal protein S6 kinase 1 (S6K1)
    • M.M. Keshwani, S. von Daake, A.C. Newton, T.K. Harris, and S.S. Taylor Hydrophobic motif phosphorylation is not required for activation loop phosphorylation of p70 ribosomal protein S6 kinase 1 (S6K1) J. Biol. Chem. 286 2011 23552 23558
    • (2011) J. Biol. Chem. , vol.286 , pp. 23552-23558
    • Keshwani, M.M.1    Von Daake, S.2    Newton, A.C.3    Harris, T.K.4    Taylor, S.S.5
  • 26
    • 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
  • 27
    • 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
  • 28
    • 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
  • 30
    • 78651284004 scopus 로고    scopus 로고
    • Characterization of GSK2334470, a novel and highly specific inhibitor of PDK1
    • A. Najafov, E.M. Sommer, J.M. Axten, M.P. Deyoung, and D.R. Alessi Characterization of GSK2334470, a novel and highly specific inhibitor of PDK1 Biochem. J. 433 2011 357 369
    • (2011) Biochem. J. , vol.433 , pp. 357-369
    • Najafov, A.1    Sommer, E.M.2    Axten, J.M.3    Deyoung, M.P.4    Alessi, D.R.5
  • 31
    • 0037337159 scopus 로고    scopus 로고
    • Regulation of the ABC kinases by phosphorylation: Protein kinase C as a paradigm
    • DOI 10.1042/BJ20021626
    • A.C. Newton Regulation of the ABC kinases by phosphorylation: protein kinase C as a paradigm Biochem. J. 370 2003 361 371 (Pubitemid 36315124)
    • (2003) Biochemical Journal , vol.370 , Issue.2 , pp. 361-371
    • Newton, A.C.1
  • 32
    • 37249005205 scopus 로고    scopus 로고
    • The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
    • DOI 10.1038/nprot.2007.321, PII NPROT.2007.321
    • F.H. Niesen, H. Berglund, and M. Vedadi The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability Nat. Protoc. 2 2007 2212 2221 (Pubitemid 351565860)
    • (2007) Nature Protocols , vol.2 , Issue.9 , pp. 2212-2221
    • Niesen, F.H.1    Berglund, H.2    Vedadi, M.3
  • 33
    • 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
    • 0036909402 scopus 로고    scopus 로고
    • Regulation of protein kinases in insulin, growth factor and Wnt signalling
    • DOI 10.1016/S0959-440X(02)00386-X
    • L.H. Pearl, and D. Barford Regulation of protein kinases in insulin, growth factor and Wnt signalling Curr. Opin. Struct. Biol. 12 2002 761 767 (Pubitemid 36009493)
    • (2002) Current Opinion in Structural Biology , vol.12 , Issue.6 , pp. 761-767
    • Pearl, L.H.1    Barford, D.2
  • 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
  • 40
    • 33744505375 scopus 로고    scopus 로고
    • Nutrient overload, insulin resistance, and ribosomal protein S6 kinase 1, S6K1
    • DOI 10.1016/j.cmet.2006.05.003, PII S1550413106001586
    • S.H. Um, D. D'Alessio, and G. Thomas Nutrient overload, insulin resistance, and ribosomal protein S6 kinase 1, S6K1 Cell Metab. 3 2006 393 402 (Pubitemid 43811780)
    • (2006) Cell Metabolism , vol.3 , Issue.6 , pp. 393-402
    • Um, S.H.1    D'Alessio, D.2    Thomas, G.3
  • 41
    • 0034653608 scopus 로고    scopus 로고
    • The PI3K-PBK1 connection: More than just a road to PKB
    • DOI 10.1042/0264-6021:3460561
    • B. Vanhaesebroeck, and D.R. Alessi The PI3K-PDK1 connection: more than just a road to PKB Biochem. J. 346 2000 561 576 (Pubitemid 30171014)
    • (2000) Biochemical Journal , vol.346 , Issue.3 , pp. 561-576
    • Vanhaesebroeck, B.1    Alessi, D.R.2
  • 42
    • 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
  • 43
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.