메뉴 건너뛰기




Volumn 41, Issue 10, 2012, Pages 801-813

The role of G-domain orientation and nucleotide state on the Ras isoform-specific membrane interaction

Author keywords

Membrane protein interaction; Model biomembranes; Ras; Signalling

Indexed keywords

GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; ISOPROTEIN; PROTEIN P21;

EID: 84867572593     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-012-0841-5     Document Type: Article
Times cited : (57)

References (49)
  • 1
    • 50849107378 scopus 로고    scopus 로고
    • Mechanisms of Ras membrane organization and signalling: Ras on a rocker
    • Abankwa D, Gorfe AA, Hancock JF (2008a) Mechanisms of Ras membrane organization and signalling: Ras on a rocker. Cell Cycle 7:2667-2673
    • (2008) Cell Cycle , vol.7 , pp. 2667-2673
    • Abankwa, D.1    Gorfe, A.A.2    Hancock, J.F.3
  • 3
    • 75749150934 scopus 로고    scopus 로고
    • Ras membrane orientation and nanodomain localization generate isoform diversity
    • Abankwa D, Gorfe AA, Inder K, Hancock JF (2010) Ras membrane orientation and nanodomain localization generate isoform diversity. Proc Natl Acad Sci USA 107:1130-1135
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 1130-1135
    • Abankwa, D.1    Gorfe, A.A.2    Inder, K.3    Hancock, J.F.4
  • 4
    • 78650627501 scopus 로고    scopus 로고
    • Membrane docking of the C2 domain from protein kinase C alpha as seen by polarized ATR-IR. The role of PIP2
    • Ausili A, Corbalan-Garcia S, Gomez-Fernandez JC, Marsh D (2011) Membrane docking of the C2 domain from protein kinase C alpha as seen by polarized ATR-IR. The role of PIP2. Biochim Biophys Acta Biomembr 1808:684-695
    • (2011) Biochim Biophys Acta Biomembr , vol.1808 , pp. 684-695
    • Ausili, A.1    Corbalan-Garcia, S.2    Gomez-Fernandez, J.C.3    Marsh, D.4
  • 5
    • 0030422901 scopus 로고    scopus 로고
    • Orientational order determination by internal reflection infrared spectroscopy
    • Axelsen PH, Citra MJ (1996) Orientational order determination by internal reflection infrared spectroscopy. Prog Biophys Mol Biol 66:227-253
    • (1996) Prog Biophys Mol Biol , vol.66 , pp. 227-253
    • Axelsen, P.H.1    Citra, M.J.2
  • 6
    • 0032909033 scopus 로고    scopus 로고
    • Membrane helix orientation from linear dichroism of infrared attenuated total reflection spectra
    • Bechinger B, Ruysschaert JM, Goormaghtigh E (1999) Membrane helix orientation from linear dichroism of infrared attenuated total reflection spectra. Biophys J 76:552-563
    • (1999) Biophys J , vol.76 , pp. 552-563
    • Bechinger, B.1    Ruysschaert, J.M.2    Goormaghtigh, E.3
  • 7
    • 0024376173 scopus 로고
    • Ras oncogenes in human cancer - A review
    • Bos JL (1989) Ras oncogenes in human cancer - a review. Cancer Res 49:4682-4689
    • (1989) Cancer Res , vol.49 , pp. 4682-4689
    • Bos, J.L.1
  • 10
    • 58149197889 scopus 로고    scopus 로고
    • Membrane binding of lipidated Ras peptides and proteins: The structural point of view
    • Brunsveld L, Waldmann H, Huster D (2009) Membrane binding of lipidated Ras peptides and proteins: the structural point of view. Biochim Biophys Acta Biomembr 1788:273-288
    • (2009) Biochim Biophys Acta Biomembr , vol.1788 , pp. 273-288
    • Brunsveld, L.1    Waldmann, H.2    Huster, D.3
  • 12
    • 84856696581 scopus 로고    scopus 로고
    • Detection of lipid raft domains in neutral and anionic Langmuir monolayers and bilayers of complex lipid composition
    • Evers F, Jeworrek C, Weise K, Tolan M, Winter R (2012) Detection of lipid raft domains in neutral and anionic Langmuir monolayers and bilayers of complex lipid composition. Soft Matter 8:2170-2175
    • (2012) Soft Matter , vol.8 , pp. 2170-2175
    • Evers, F.1    Jeworrek, C.2    Weise, K.3    Tolan, M.4    Winter, R.5
  • 13
    • 0032968077 scopus 로고    scopus 로고
    • Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes
    • Goormaghtigh E, Raussens V, Ruysschaert JM (1999) Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes. Biochim Biophys Acta Rev Biomembr 1422:105-185
    • (1999) Biochim Biophys Acta Rev Biomembr , vol.1422 , pp. 105-185
    • Goormaghtigh, E.1    Raussens, V.2    Ruysschaert, J.M.3
  • 14
    • 35048822834 scopus 로고    scopus 로고
    • H-Ras protein in a bilayer: Interaction and structure perturbation
    • Gorfe AA, Babakhani A, McCammon JA (2007a) H-Ras protein in a bilayer: interaction and structure perturbation. J Am Chem Soc 129:12280-12286
    • (2007) J Am Chem Soc , vol.129 , pp. 12280-12286
    • Gorfe, A.A.1    Babakhani, A.2    McCammon, J.A.3
  • 15
    • 33847413103 scopus 로고    scopus 로고
    • Structure and dynamics of the full-length lipidmodified H-Ras protein in a 1,2-dimyristoylglycero-3-phosphocholine bilayer
    • Gorfe AA, Hanzal-Bayer M, Abankwa D, Hancock JF, McCammon JA (2007b) Structure and dynamics of the full-length lipidmodified H-Ras protein in a 1,2-dimyristoylglycero-3-phosphocholine bilayer. J Med Chem 50:674-684
    • (2007) J Med Chem , vol.50 , pp. 674-684
    • Gorfe, A.A.1    Hanzal-Bayer, M.2    Abankwa, D.3    Hancock, J.F.4    McCammon, J.A.5
  • 17
    • 0037542854 scopus 로고    scopus 로고
    • Ras proteins: Different signals from different locations
    • Hancock JF (2003) Ras proteins: different signals from different locations. Nat Rev Mol Cell Biol 4:373-384
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 373-384
    • Hancock, J.F.1
  • 18
    • 22144479017 scopus 로고    scopus 로고
    • Ras plasma membrane signaling platforms
    • Hancock JF, Parton RG (2005) Ras plasma membrane signaling platforms. Biochem J 389:1-11
    • (2005) Biochem J , vol.389 , pp. 1-11
    • Hancock, J.F.1    Parton, R.G.2
  • 19
    • 0025013547 scopus 로고
    • A Polybasic domain or palmitoylation is required in addition to the Caax motif to localize p21 Ras to the plasma membrane
    • Hancock JF, Paterson H, Marshall CJ (1990) A Polybasic domain or palmitoylation is required in addition to the Caax motif to localize p21 Ras to the plasma membrane. Cell 63:133-139
    • (1990) Cell , vol.63 , pp. 133-139
    • Hancock, J.F.1    Paterson, H.2    Marshall, C.J.3
  • 20
    • 0026021456 scopus 로고
    • Methylation and proteolysis are essential for efficient membrane binding of prenylated p21 K-Ras(B)
    • Hancock JF, Cadwallader K, Marshall CJ (1991) Methylation and proteolysis are essential for efficient membrane binding of prenylated p21 K-Ras(B). EMBO J 10:641-646
    • (1991) EMBO J , vol.10 , pp. 641-646
    • Hancock, J.F.1    Cadwallader, K.2    Marshall, C.J.3
  • 22
    • 0035857550 scopus 로고    scopus 로고
    • H-1 high-resolution magic angle spinning NMR spectroscopy for the investigation of a Ras lipopeptide in a lipid membrane
    • Huster D, Kuhn K, Kadereit D, Waldmann H, Arnold K (2001) H-1 high-resolution magic angle spinning NMR spectroscopy for the investigation of a Ras lipopeptide in a lipid membrane. Angew Chem Int Edit 40:1056-1058
    • (2001) Angew Chem Int Edit , vol.40 , pp. 1056-1058
    • Huster, D.1    Kuhn, K.2    Kadereit, D.3    Waldmann, H.4    Arnold, K.5
  • 23
    • 79951559073 scopus 로고    scopus 로고
    • Temperature-pressure phase diagram of a heterogeneous anionic model biomembrane system: Results from a combined calorimetry, spectroscopy and microscopy study
    • Kapoor S, Werkmüller A, Denter C, Zhai Y, Markgraf J, Weise K, Opitz N, Winter R (2011) Temperature-pressure phase diagram of a heterogeneous anionic model biomembrane system: results from a combined calorimetry, spectroscopy and microscopy study. Biochim Biophys Acta Biomembr 1808:1187-1195
    • (2011) Biochim Biophys Acta Biomembr , vol.1808 , pp. 1187-1195
    • Kapoor, S.1    Werkmüller, A.2    Denter, C.3    Zhai, Y.4    Markgraf, J.5    Weise, K.6    Opitz, N.7    Winter, R.8
  • 24
    • 84856005311 scopus 로고    scopus 로고
    • Kapoor S,TriolaG,Vetter IR,ErlkampM,WaldmannH,WinterR(2012) Revealing conformational substates of lipidated N-Ras protein by pressure modulation
    • Kapoor S,TriolaG,Vetter IR,ErlkampM,WaldmannH,WinterR(2012) Revealing conformational substates of lipidated N-Ras protein by pressure modulation. Proc Natl Acad Sci USA 109:460-465
    • Proc Natl Acad Sci USA , vol.109 , pp. 460-465
  • 27
    • 0026511938 scopus 로고
    • Structures of the subgel phases of n-saturated diacyl phosphatidylcholine bilayers: FTIR spectroscopic studies of 13C=O and 2H labeled lipids
    • Lewis RN, McElhaney RN (1992) Structures of the subgel phases of n-saturated diacyl phosphatidylcholine bilayers: FTIR spectroscopic studies of 13C=O and 2H labeled lipids. Biophys J 61:63-77
    • (1992) Biophys J , vol.61 , pp. 63-77
    • Lewis, R.N.1    McElhaney, R.N.2
  • 29
    • 0032734050 scopus 로고    scopus 로고
    • Quantitation of secondary structure in ATR infrared spectroscopy
    • Marsh D (1999) Quantitation of secondary structure in ATR infrared spectroscopy. Biophys J 77:2630-2637
    • (1999) Biophys J , vol.77 , pp. 2630-2637
    • Marsh, D.1
  • 30
    • 33746858605 scopus 로고    scopus 로고
    • Insertion of lipidated Ras proteins into lipid monolayers studied by infrared reflection absorption spectroscopy (IRRAS)
    • Meister A, Nicolini C, Waldmann H, Kuhlmann J, Kerth A, Winter R, Blume A (2006) Insertion of lipidated Ras proteins into lipid monolayers studied by infrared reflection absorption spectroscopy (IRRAS). Biophys J 91:1388-1401
    • (2006) Biophys J , vol.91 , pp. 1388-1401
    • Meister, A.1    Nicolini, C.2    Waldmann, H.3    Kuhlmann, J.4    Kerth, A.5    Winter, R.6    Blume, A.7
  • 31
    • 77449130066 scopus 로고    scopus 로고
    • Infrared reflectionabsorption spectroscopy: Principles and applications to lipid-protein interaction in Langmuir films
    • Mendelsohn R, Mao GR, Flach CR (2010) Infrared reflectionabsorption spectroscopy: principles and applications to lipid-protein interaction in Langmuir films. Biochim Biophys Acta Biomembr 1798:788-800
    • (2010) Biochim Biophys Acta Biomembr , vol.1798 , pp. 788-800
    • Mendelsohn, R.1    Mao, G.R.2    Flach, C.R.3
  • 33
    • 0017194357 scopus 로고
    • Studies on membrane-fusion. 2. Induction of fusion in pure phospholipids membranes by calcium ions and other divalent metals
    • Papahadjopoulos D, Vail WJ, Pangborn WA, Poste G (1976) Studies on membrane-fusion. 2. Induction of fusion in pure phospholipids membranes by calcium ions and other divalent metals. Biochim Biophys Acta 448:265-283
    • (1976) Biochim Biophys Acta , vol.448 , pp. 265-283
    • Papahadjopoulos, D.1    Vail, W.J.2    Pangborn, W.A.3    Poste, G.4
  • 34
    • 0037455589 scopus 로고    scopus 로고
    • Direct visualization of Ras proteins in spatially distinct cell surface microdomains
    • Prior IA, Muncke C, Parton RG, Hancock JF (2003) Direct visualization of Ras proteins in spatially distinct cell surface microdomains. J Cell Biol 160:165-170
    • (2003) J Cell Biol , vol.160 , pp. 165-170
    • Prior, I.A.1    Muncke, C.2    Parton, R.G.3    Hancock, J.F.4
  • 35
    • 33846207546 scopus 로고    scopus 로고
    • Deregulated Ras signaling in developmental disorders: New tricks for an old dog
    • Shannon K
    • Schubbert S, Bollag G, Shannon K (2007) Deregulated Ras signaling in developmental disorders: new tricks for an old dog. Curr Opin Genet Dev 17:15-22
    • (2007) Curr Opin Genet Dev , vol.17 , pp. 15-22
    • Schubbert, S.1    Bollag, G.2
  • 36
    • 0034304851 scopus 로고    scopus 로고
    • Lipid rafts and signal transduction
    • Simons K, Toomre D (2000) Lipid rafts and signal transduction. Nat Rev Mol Cell Biol 1:31-39
    • (2000) Nat Rev Mol Cell Biol , vol.1 , pp. 31-39
    • Simons, K.1    Toomre, D.2
  • 37
    • 0026443739 scopus 로고
    • Interfacial conformation of dipalmitoylglycerol and dipalmitoylphosphatidylcholine in phospholipid bilayers
    • Smith SO, Kustanovich I, Bhamidipati S, Salmon A, Hamilton JA (1992) Interfacial conformation of dipalmitoylglycerol and dipalmitoylphosphatidylcholine in phospholipid bilayers. Biochemistry 31:11660-11664
    • (1992) Biochemistry , vol.31 , pp. 11660-11664
    • Smith, S.O.1    Kustanovich, I.2    Bhamidipati, S.3    Salmon, A.4    Hamilton, J.A.5
  • 40
    • 0029809315 scopus 로고    scopus 로고
    • What's new in ras genes? Physiological role of ras genes in signal transduction and significance of ras gene activation in tumorigenesis
    • Waldmann V, Rabes HM (1996) What's new in ras genes? Physiological role of ras genes in signal transduction and significance of ras gene activation in tumorigenesis. Pathol Res Pract 192:883-891
    • (1996) Pathol Res Pract , vol.192 , pp. 883-891
    • Waldmann, V.1    Rabes, H.M.2
  • 41
    • 0035844149 scopus 로고    scopus 로고
    • Differential activation of the pac pathway by Ha-Ras and K-Ras
    • Walsh AB, Bar-Sagi D (2001) Differential activation of the pac pathway by Ha-Ras and K-Ras. J Biol Chem 276:15609-15615
    • (2001) J Biol Chem , vol.276 , pp. 15609-15615
    • Walsh, A.B.1    Bar-Sagi, D.2
  • 42
    • 63149129301 scopus 로고    scopus 로고
    • Influence of the lipidation motif on the partitioning and association of N-Ras in model membrane subdomains
    • Weise K, Triola G, Brunsveld L, Waldmann H, Winter R (2009) Influence of the lipidation motif on the partitioning and association of N-Ras in model membrane subdomains. J Am Chem Soc 131:1557-1564
    • (2009) J Am Chem Soc , vol.131 , pp. 1557-1564
    • Weise, K.1    Triola, G.2    Brunsveld, L.3    Waldmann, H.4    Winter, R.5
  • 45
    • 0019828883 scopus 로고
    • Solid-state C-13 nuclear magnetic-resonance of the lecithin gel to liquid-crystalline phase-transition
    • Wittebort RJ, Schmidt CF, Griffin RG (1981) Solid-state C-13 nuclear magnetic-resonance of the lecithin gel to liquid-crystalline phase-transition. Biochemistry 20:4223-4228
    • (1981) Biochemistry , vol.20 , pp. 4223-4228
    • Wittebort, R.J.1    Schmidt, C.F.2    Griffin, R.G.3
  • 46
    • 0025740753 scopus 로고
    • The structure of Ras protein - Amodel for a universal molecular switch
    • Wittinghofer A, Pai EF (1991) The structure of Ras protein - amodel for a universal molecular switch. Trends Biochem Sci 16:382-387
    • (1991) Trends Biochem Sci , vol.16 , pp. 382-387
    • Wittinghofer, A.1    Pai, E.F.2
  • 47
    • 0034605862 scopus 로고    scopus 로고
    • Ras - A molecular switch involved in tumor formation
    • Wittinghofer A, Waldmann H (2000) Ras - a molecular switch involved in tumor formation. Angew Chem Int Edit 39:4193-4214
    • (2000) Angew Chem Int Edit , vol.39 , pp. 4193-4214
    • Wittinghofer, A.1    Waldmann, H.2
  • 48
    • 0032508517 scopus 로고    scopus 로고
    • Ras isoforms vary in their ability to activate Raf-1 and phosphoinositide 3-kinase
    • Yan J, Roy S, Apolloni A, Lane A, Hancock JF (1998) Ras isoforms vary in their ability to activate Raf-1 and phosphoinositide 3-kinase. J Biol Chem 273:24052-24056
    • (1998) J Biol Chem , vol.273 , pp. 24052-24056
    • Yan, J.1    Roy, S.2    Apolloni, A.3    Lane, A.4    Hancock, J.F.5
  • 49
    • 79955963495 scopus 로고    scopus 로고
    • Applications of pressure perturbation calorimetry in biophysical studies
    • Zhai Y, Okoro L, Cooper A, Winter R (2011) Applications of pressure perturbation calorimetry in biophysical studies. Biophys Chem 156:13-23
    • (2011) Biophys Chem , vol.156 , pp. 13-23
    • Zhai, Y.1    Okoro, L.2    Cooper, A.3    Winter, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.