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Volumn 52, Issue 28, 2013, Pages 4820-4829

The PH domain of phosphoinositide-dependent kinase-1 exhibits a novel, phospho-regulated monomer-dimer equilibrium with important implications for kinase domain activation: Single-molecule and ensemble studies

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION MECHANISMS; ELECTROSTATIC CONTROL; MEMBRANE AFFINITY; MOLECULAR PICTURES; MONOMER-DIMER EQUILIBRIUM; OLIGOMERIC STATE; SIGNALING LIPIDS; SINGLE-MOLECULE ANALYSIS;

EID: 84880534471     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400488f     Document Type: Article
Times cited : (29)

References (36)
  • 1
    • 33745759303 scopus 로고    scopus 로고
    • Role of the PH domain in regulating in vitro autophosphorylation events required for reconstitution of PDK1 catalytic activity
    • Gao, X. and Harris, T. K. (2006) Role of the PH domain in regulating in vitro autophosphorylation events required for reconstitution of PDK1 catalytic activity Bioorg. Chem. 34, 200-223
    • (2006) Bioorg. Chem. , vol.34 , pp. 200-223
    • Gao, X.1    Harris, T.K.2
  • 3
    • 84865641259 scopus 로고    scopus 로고
    • Role of the C-terminal regulatory domain in the allosteric inhibition of PKB/Akt
    • Calleja, V., Laguerre, M., and Larijani, B. (2011) Role of the C-terminal regulatory domain in the allosteric inhibition of PKB/Akt Adv. Enzyme Regul. 52, 46-57
    • (2011) Adv. Enzyme Regul. , vol.52 , pp. 46-57
    • Calleja, V.1    Laguerre, M.2    Larijani, B.3
  • 4
    • 77958576132 scopus 로고    scopus 로고
    • Crystal structure of human AKT1 with an allosteric inhibitor reveals a new mode of kinase inhibition
    • Wu, W. I., Voegtli, W. C., Sturgis, H. L., Dizon, F. P., Vigers, G. P., and Brandhuber, B. J. (2010) Crystal structure of human AKT1 with an allosteric inhibitor reveals a new mode of kinase inhibition PLoS One 5, 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
  • 5
    • 77349122303 scopus 로고    scopus 로고
    • Protein kinase C: Poised to signal
    • Newton, A. C. (2010) Protein kinase C: Poised to signal Am. J. Physiol. 298, E395-E402
    • (2010) Am. J. Physiol. , vol.298
    • Newton, A.C.1
  • 6
    • 79952110243 scopus 로고    scopus 로고
    • PDK1: The major transducer of PI 3-kinase actions
    • Bayascas, J. R. (2010) PDK1: The major transducer of PI 3-kinase actions Curr. Top. Microbiol. Immunol. 346, 9-29
    • (2010) Curr. Top. Microbiol. Immunol. , vol.346 , pp. 9-29
    • Bayascas, J.R.1
  • 7
  • 9
    • 33750942901 scopus 로고    scopus 로고
    • Signaling networks in neuronal polarization
    • Yoshimura, T., Arimura, N., and Kaibuchi, K. (2006) Signaling networks in neuronal polarization J. Neurosci. 26, 10626-10630
    • (2006) J. Neurosci. , vol.26 , pp. 10626-10630
    • Yoshimura, T.1    Arimura, N.2    Kaibuchi, K.3
  • 11
    • 0042734621 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase signalling: Which way to target?
    • Wymann, M. P., Zvelebil, M., and Laffargue, M. (2003) Phosphoinositide 3-kinase signalling: Which way to target? Trends Pharmacol. Sci. 24, 366-376
    • (2003) Trends Pharmacol. Sci. , vol.24 , pp. 366-376
    • Wymann, M.P.1    Zvelebil, M.2    Laffargue, M.3
  • 12
    • 76649137613 scopus 로고    scopus 로고
    • 5-Stabilized phosphatidylinositol 3,4,5-trisphosphate analogues bind Grp1 PH, inhibit phosphoinositide phosphatases, and block neutrophil migration
    • Zhang, H., He, J., Kutateladze, T. G., Sakai, T., Sasaki, T., Markadieu, N., Erneux, C., and Prestwich, G. D. (2010) 5-Stabilized phosphatidylinositol 3,4,5-trisphosphate analogues bind Grp1 PH, inhibit phosphoinositide phosphatases, and block neutrophil migration ChemBioChem 11, 388-395
    • (2010) ChemBioChem , vol.11 , pp. 388-395
    • Zhang, H.1    He, J.2    Kutateladze, T.G.3    Sakai, T.4    Sasaki, T.5    Markadieu, N.6    Erneux, C.7    Prestwich, G.D.8
  • 13
    • 79959365543 scopus 로고    scopus 로고
    • Targeting PDK1 in cancer
    • Raimondi, C. and Falasca, M. (2011) Targeting PDK1 in cancer Curr. Med. Chem. 18, 2763-2769
    • (2011) Curr. Med. Chem. , vol.18 , pp. 2763-2769
    • Raimondi, C.1    Falasca, M.2
  • 16
    • 57549101230 scopus 로고    scopus 로고
    • Small-molecule inhibitors of PDK1
    • Peifer, C. and Alessi, D. R. (2008) Small-molecule inhibitors of PDK1 ChemMedChem 3, 1810-1838
    • (2008) ChemMedChem , vol.3 , pp. 1810-1838
    • Peifer, C.1    Alessi, D.R.2
  • 17
    • 27844469655 scopus 로고    scopus 로고
    • Selective cellular effects of overexpressed pleckstrin-homology domains that recognize PtdIns(3,4,5)P3 suggest their interaction with protein binding partners
    • Varnai, P., Bondeva, T., Tamas, P., Toth, B., Buday, L., Hunyady, L., and Balla, T. (2005) Selective cellular effects of overexpressed pleckstrin-homology domains that recognize PtdIns(3,4,5)P3 suggest their interaction with protein binding partners J. Cell Sci. 118, 4879-4888
    • (2005) J. Cell Sci. , vol.118 , pp. 4879-4888
    • Varnai, P.1    Bondeva, T.2    Tamas, P.3    Toth, B.4    Buday, L.5    Hunyady, L.6    Balla, T.7
  • 18
    • 38549092474 scopus 로고    scopus 로고
    • Membrane recognition by phospholipid-binding domains
    • Lemmon, M. A. (2008) Membrane recognition by phospholipid-binding domains Nat. Rev. Mol. Cell Biol. 9, 99-111
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 99-111
    • Lemmon, M.A.1
  • 19
    • 42949124488 scopus 로고    scopus 로고
    • Comprehensive identification of PIP3-regulated PH domains from C. elegans to H. sapiens by model prediction and live imaging
    • Park, W. S., Heo, W. D., Whalen, J. H., O'Rourke, N. A., Bryan, H. M., Meyer, T., and Teruel, M. N. (2008) Comprehensive identification of PIP3-regulated PH domains from C. elegans to H. sapiens by model prediction and live imaging Mol. Cell 30, 381-392
    • (2008) Mol. Cell , vol.30 , pp. 381-392
    • Park, W.S.1    Heo, W.D.2    Whalen, J.H.3    O'Rourke, N.A.4    Bryan, H.M.5    Meyer, T.6    Teruel, M.N.7
  • 20
    • 68949110664 scopus 로고    scopus 로고
    • Molecular dynamics simulations of PIP2 and PIP3 in lipid bilayers: Determination of ring orientation, and the effects of surface roughness on a Poisson-Boltzmann description
    • Li, Z., Venable, R. M., Rogers, L. A., Murray, D., and Pastor, R. W. (2009) Molecular dynamics simulations of PIP2 and PIP3 in lipid bilayers: Determination of ring orientation, and the effects of surface roughness on a Poisson-Boltzmann description Biophys. J. 97, 155-163
    • (2009) Biophys. J. , vol.97 , pp. 155-163
    • Li, Z.1    Venable, R.M.2    Rogers, L.A.3    Murray, D.4    Pastor, R.W.5
  • 22
    • 58849094579 scopus 로고    scopus 로고
    • Single-molecule fluorescence studies of a PH domain: New insights into the membrane docking reaction
    • Knight, J. D. and Falke, J. J. (2009) Single-molecule fluorescence studies of a PH domain: New insights into the membrane docking reaction Biophys. J. 96, 566-582
    • (2009) Biophys. J. , vol.96 , pp. 566-582
    • Knight, J.D.1    Falke, J.J.2
  • 23
    • 84857597124 scopus 로고    scopus 로고
    • Assembly of membrane-bound protein complexes: Detection and analysis by single molecule diffusion
    • Ziemba, B. P., Knight, J. D., and Falke, J. J. (2012) Assembly of membrane-bound protein complexes: Detection and analysis by single molecule diffusion Biochemistry 51, 1638-1647
    • (2012) Biochemistry , vol.51 , pp. 1638-1647
    • Ziemba, B.P.1    Knight, J.D.2    Falke, J.J.3
  • 24
    • 56749168073 scopus 로고    scopus 로고
    • Molecular mechanism of an oncogenic mutation that alters membrane targeting: Glu17Lys modifies the PIP lipid specificity of the AKT1 PH domain
    • Landgraf, K. E., Pilling, C., and Falke, J. J. (2008) Molecular mechanism of an oncogenic mutation that alters membrane targeting: Glu17Lys modifies the PIP lipid specificity of the AKT1 PH domain Biochemistry 47, 12260-12269
    • (2008) Biochemistry , vol.47 , pp. 12260-12269
    • Landgraf, K.E.1    Pilling, C.2    Falke, J.J.3
  • 26
    • 34250670453 scopus 로고    scopus 로고
    • Site-specific protein labeling by Sfp phosphopantetheinyl transferase
    • Yin, J., Lin, A. J., Golan, D. E., and Walsh, C. T. (2006) Site-specific protein labeling by Sfp phosphopantetheinyl transferase Nat. Protoc. 1, 280-285
    • (2006) Nat. Protoc. , vol.1 , pp. 280-285
    • Yin, J.1    Lin, A.J.2    Golan, D.E.3    Walsh, C.T.4
  • 27
    • 78249261241 scopus 로고    scopus 로고
    • Single molecule diffusion of membrane-bound proteins: Window into lipid contacts and bilayer dynamics
    • Knight, J. D., Lerner, M. G., Marcano-Velazquez, J. G., Pastor, R. W., and Falke, J. J. (2010) Single molecule diffusion of membrane-bound proteins: Window into lipid contacts and bilayer dynamics Biophys. J. 99, 2879-2887
    • (2010) Biophys. J. , vol.99 , pp. 2879-2887
    • Knight, J.D.1    Lerner, M.G.2    Marcano-Velazquez, J.G.3    Pastor, R.W.4    Falke, J.J.5
  • 28
    • 11144292734 scopus 로고    scopus 로고
    • GRP1 pleckstrin homology domain: Activation parameters and novel search mechanism for rare target lipid
    • Corbin, J. A., Dirkx, R. A., and Falke, J. J. (2004) GRP1 pleckstrin homology domain: Activation parameters and novel search mechanism for rare target lipid Biochemistry 43, 16161-16173
    • (2004) Biochemistry , vol.43 , pp. 16161-16173
    • Corbin, J.A.1    Dirkx, R.A.2    Falke, J.J.3
  • 29
    • 0033804075 scopus 로고    scopus 로고
    • Tracking single proteins within cells
    • Goulian, M. and Simon, S. M. (2000) Tracking single proteins within cells Biophys. J. 79, 2188-2198
    • (2000) Biophys. J. , vol.79 , pp. 2188-2198
    • Goulian, M.1    Simon, S.M.2
  • 30
    • 84879200786 scopus 로고    scopus 로고
    • Lateral diffusion of peripheral membrane proteins on supported lipid bilayers is controlled by the additive frictional drags of 1) bound lipids and 2) protein domains penetrating into the bilayer hydrocarbon core
    • Ziemba, B. P. and Falke, J. J. (2013) Lateral diffusion of peripheral membrane proteins on supported lipid bilayers is controlled by the additive frictional drags of 1) bound lipids and 2) protein domains penetrating into the bilayer hydrocarbon core Chem. Phys. Lipids DOI: 10.1016/j.chemphyslip.2013.04. 005
    • (2013) Chem. Phys. Lipids
    • Ziemba, B.P.1    Falke, J.J.2
  • 31
    • 84859137660 scopus 로고    scopus 로고
    • Membrane docking geometry of GRP1 PH domain bound to a target lipid bilayer: An EPR site-directed spin-labeling and relaxation study
    • Chen, H. C., Ziemba, B. P., Landgraf, K. E., Corbin, J. A., and Falke, J. J. (2012) Membrane docking geometry of GRP1 PH domain bound to a target lipid bilayer: An EPR site-directed spin-labeling and relaxation study PLoS One 7, e33640
    • (2012) PLoS One , vol.7 , pp. 33640
    • Chen, H.C.1    Ziemba, B.P.2    Landgraf, K.E.3    Corbin, J.A.4    Falke, J.J.5
  • 32
    • 82355164165 scopus 로고    scopus 로고
    • Phosphatidylserine binding is essential for plasma membrane recruitment and signaling function of 3-phosphoinositide-dependent kinase-1
    • Lucas, N. and Cho, W. (2011) Phosphatidylserine binding is essential for plasma membrane recruitment and signaling function of 3-phosphoinositide- dependent kinase-1 J. Biol. Chem. 286, 41265-41272
    • (2011) J. Biol. Chem. , vol.286 , pp. 41265-41272
    • Lucas, N.1    Cho, W.2
  • 33
    • 84863322867 scopus 로고    scopus 로고
    • Contributions to membrane-embedded-protein diffusion beyond hydrodynamic theories
    • Camley, B. A. and Brown, F. L. (2012) Contributions to membrane-embedded-protein diffusion beyond hydrodynamic theories Phys. Rev. E: Stat., Nonlinear, Soft Matter Phys. 85, 061921
    • (2012) Phys. Rev. E: Stat., Nonlinear, Soft Matter Phys. , vol.85 , pp. 061921
    • Camley, B.A.1    Brown, F.L.2
  • 34
    • 49449113683 scopus 로고    scopus 로고
    • Effect of PIP2 binding on the membrane docking geometry of PKCα C2 domain: An EPR site-directed spin-labeling and relaxation study
    • Landgraf, K. E., Malmberg, N. J., and Falke, J. J. (2008) Effect of PIP2 binding on the membrane docking geometry of PKCα C2 domain: An EPR site-directed spin-labeling and relaxation study Biochemistry 47, 8301-8316
    • (2008) Biochemistry , vol.47 , pp. 8301-8316
    • Landgraf, K.E.1    Malmberg, N.J.2    Falke, J.J.3
  • 35
    • 77956789005 scopus 로고    scopus 로고
    • Membrane docking geometry and target lipid stoichiometry of membrane-bound PKCα C2 domain: A combined molecular dynamics and experimental study
    • Lai, C. L., Landgraf, K. E., Voth, G. A., and Falke, J. J. (2010) Membrane docking geometry and target lipid stoichiometry of membrane-bound PKCα C2 domain: A combined molecular dynamics and experimental study J. Mol. Biol. 402, 301-310
    • (2010) J. Mol. Biol. , vol.402 , pp. 301-310
    • Lai, C.L.1    Landgraf, K.E.2    Voth, G.A.3    Falke, J.J.4
  • 36
    • 0037102153 scopus 로고    scopus 로고
    • High resolution crystal structure of the human PDK1 catalytic domain defines the regulatory phosphopeptide docking site
    • Biondi, R. M., Komander, D., Thomas, C. C., Lizcano, J. M., Deak, M., Alessi, D. R., and van Aalten, D. M. (2002) High resolution crystal structure of the human PDK1 catalytic domain defines the regulatory phosphopeptide docking site EMBO J. 21, 4219-4228
    • (2002) EMBO J. , vol.21 , pp. 4219
    • 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


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