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Volumn 402, Issue 2, 2010, Pages 301-310

Membrane docking geometry and target lipid stoichiometry of membrane-bound PKCα C2 domain: A combined molecular dynamics and experimental study

Author keywords

Conserved membrane targeting domain; Molecular dynamics; Phosphatidylinositol 4,5 bisphosphate regulation; Positive cooperativity; Protein kinase C activation

Indexed keywords

CALCIUM ION; LIPID; MEMBRANE PROTEIN; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE; PHOSPHATIDYLSERINE; PROTEIN KINASE C ALPHA; CALCIUM; DIVALENT CATION; MEMBRANE LIPID; PROTEIN BINDING;

EID: 77956789005     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.07.037     Document Type: Article
Times cited : (51)

References (30)
  • 1
    • 66349096059 scopus 로고    scopus 로고
    • Lipid activation of protein kinases
    • Newton A.C. Lipid activation of protein kinases. J. Lipid Res. 2009, 50:S266-S271.
    • (2009) J. Lipid Res. , vol.50
    • Newton, A.C.1
  • 2
    • 38549092474 scopus 로고    scopus 로고
    • Membrane recognition by phospholipid-binding domains
    • Lemmon M.A. Membrane recognition by phospholipid-binding domains. Nat. Rev. Mol. Cell Biol. 2008, 9:99-111.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 99-111
    • Lemmon, M.A.1
  • 4
    • 0030467967 scopus 로고    scopus 로고
    • The C2 domain calcium-binding motif: structural and functional diversity
    • Nalefski E.A., Falke J.J. The C2 domain calcium-binding motif: structural and functional diversity. Protein Sci. 1996, 5:2375-2390.
    • (1996) Protein Sci. , vol.5 , pp. 2375-2390
    • Nalefski, E.A.1    Falke, J.J.2
  • 5
    • 0029060391 scopus 로고
    • Protein kinase C and lipid signaling for sustained cellular responses
    • Nishizuka Y. Protein kinase C and lipid signaling for sustained cellular responses. FASEB J. 1995, 9:484-496.
    • (1995) FASEB J. , vol.9 , pp. 484-496
    • Nishizuka, Y.1
  • 9
    • 49449113683 scopus 로고    scopus 로고
    • 2 binding on the membrane docking geometry of PKCα C2 domain: an EPR site-directed spin-labeling and relaxation study
    • 2 binding on the membrane docking geometry of PKCα C2 domain: an EPR site-directed spin-labeling and relaxation study. Biochemistry 2008, 47:8301-8316.
    • (2008) Biochemistry , vol.47 , pp. 8301-8316
    • Landgraf, K.E.1    Malmberg, N.J.2    Falke, J.J.3
  • 10
    • 0037167614 scopus 로고    scopus 로고
    • C2 domains of protein kinase C isoforms α, β, and γ: activation parameters and calcium stoichiometries of the membrane-bound state
    • Kohout S.C., Corbalan-Garcia S., Torrecillas A., Gomez-Fernandez J.C., Falke J.J. C2 domains of protein kinase C isoforms α, β, and γ: activation parameters and calcium stoichiometries of the membrane-bound state. Biochemistry 2002, 41:11411-11424.
    • (2002) Biochemistry , vol.41 , pp. 11411-11424
    • Kohout, S.C.1    Corbalan-Garcia, S.2    Torrecillas, A.3    Gomez-Fernandez, J.C.4    Falke, J.J.5
  • 11
    • 0242401834 scopus 로고    scopus 로고
    • Membrane-docking loops of the cPLA2 C2 domain: detailed structural analysis of the protein-membrane interface via site-directed spin-labeling
    • Malmberg N.J., Van Buskirk D.R., Falke J.J. Membrane-docking loops of the cPLA2 C2 domain: detailed structural analysis of the protein-membrane interface via site-directed spin-labeling. Biochemistry 2003, 42:13227-13240.
    • (2003) Biochemistry , vol.42 , pp. 13227-13240
    • Malmberg, N.J.1    Van Buskirk, D.R.2    Falke, J.J.3
  • 15
    • 58149196187 scopus 로고    scopus 로고
    • Tracking microdomain dynamics in cell membranes
    • Day C.A., Kenworthy A.K. Tracking microdomain dynamics in cell membranes. Biochim. Biophys. Acta 2009, 1788:245-253.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 245-253
    • Day, C.A.1    Kenworthy, A.K.2
  • 16
    • 0004016501 scopus 로고
    • Comparison of simple potential functions for simulating liquid water
    • Jorgensen W.L., Chandrasekhar J., Madura J.D. Comparison of simple potential functions for simulating liquid water. J. Chem. Phys. 1983, 79:926-935.
    • (1983) J. Chem. Phys. , vol.79 , pp. 926-935
    • Jorgensen, W.L.1    Chandrasekhar, J.2    Madura, J.D.3
  • 17
    • 33846451059 scopus 로고    scopus 로고
    • Self-induced docking site of a deeply embedded peripheral membrane protein
    • Jaud S., Tobias D.J., Falke J.J., White S.H. Self-induced docking site of a deeply embedded peripheral membrane protein. Biophys. J. 2007, 92:517-524.
    • (2007) Biophys. J. , vol.92 , pp. 517-524
    • Jaud, S.1    Tobias, D.J.2    Falke, J.J.3    White, S.H.4
  • 18
    • 33750037303 scopus 로고    scopus 로고
    • Direct observation of Bin/amphiphysin/Rvs (BAR) domain-induced membrane curvature by means of molecular dynamics simulations
    • Blood P.D., Voth G.A. Direct observation of Bin/amphiphysin/Rvs (BAR) domain-induced membrane curvature by means of molecular dynamics simulations. Proc. Natl Acad. Sci. USA 2006, 103:15068-15072.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 15068-15072
    • Blood, P.D.1    Voth, G.A.2
  • 20
    • 0034250744 scopus 로고    scopus 로고
    • An improved empirical potential energy function for molecular simulations of phospholipids
    • Feller S.E., MacKerell A.D. An improved empirical potential energy function for molecular simulations of phospholipids. J. Phys. Chem. B 2000, 104:7510-7515.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 7510-7515
    • Feller, S.E.1    MacKerell, A.D.2
  • 22
    • 36449007836 scopus 로고
    • Constant pressure molecular dynamics simulation: the Langevin piston method
    • Feller S.E., Zhang Y., Pastor R.W., Brooks B.R. Constant pressure molecular dynamics simulation: the Langevin piston method. J. Chem. Phys. 1995, 103:4613-4621.
    • (1995) J. Chem. Phys. , vol.103 , pp. 4613-4621
    • Feller, S.E.1    Zhang, Y.2    Pastor, R.W.3    Brooks, B.R.4
  • 23
    • 33846823909 scopus 로고
    • Particle mesh Ewald: an N-log(N) method for Ewald sums in large systems
    • Darden T., York D., Pedersen L. Particle mesh Ewald: an N-log(N) method for Ewald sums in large systems. J. Chem. Phys. 1993, 98:10089-10092.
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 24
    • 84986440341 scopus 로고
    • SETTLE: an analytical version of the SHAKE and RATTLE algorithm for rigid water models
    • Miyamoto S., Kollman P.A. SETTLE: an analytical version of the SHAKE and RATTLE algorithm for rigid water models. J. Comput. Chem. 1992, 13:952-962.
    • (1992) J. Comput. Chem. , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.A.2
  • 26
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual Molecular Dynamics.
    • Humphrey, W., Dalke, A. & Schulten, K. (1996). VMD: Visual Molecular Dynamics. J. Mol. Graphics, 14, 27-28, 33-38.
    • (1996) J. Mol. Graphics , vol.14 , Issue.27-28 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 28
    • 28444477387 scopus 로고    scopus 로고
    • Plasma membrane phosphoinositide organization by protein electrostatics
    • McLaughlin S., Murray D. Plasma membrane phosphoinositide organization by protein electrostatics. Nature 2005, 438:605-611.
    • (2005) Nature , vol.438 , pp. 605-611
    • McLaughlin, S.1    Murray, D.2
  • 29
    • 70350061531 scopus 로고    scopus 로고
    • Ionization properties of phosphatidylinositol polyphosphates in mixed model membranes
    • Kooijman E.E., King K.E., Gangoda M., Gericke A. Ionization properties of phosphatidylinositol polyphosphates in mixed model membranes. Biochemistry 2009, 48:9360-9371.
    • (2009) Biochemistry , vol.48 , pp. 9360-9371
    • Kooijman, E.E.1    King, K.E.2    Gangoda, M.3    Gericke, A.4
  • 30
    • 56749168073 scopus 로고    scopus 로고
    • Molecular mechanism of an oncogenic mutation that alters membrane targeting: Glu17Lys modifies the PIP lipid specificity of AKT1 PH domain
    • Landgraf K.E., Pilling C., Falke J.J. Molecular mechanism of an oncogenic mutation that alters membrane targeting: Glu17Lys modifies the PIP lipid specificity of AKT1 PH domain. Biochemistry 2008, 47:12260-12269.
    • (2008) Biochemistry , vol.47 , pp. 12260-12269
    • Landgraf, K.E.1    Pilling, C.2    Falke, J.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.