메뉴 건너뛰기




Volumn 3, Issue 4, 2012, Pages

What drives the clustering of membrane-bound Ras?

Author keywords

Lipid anchor; Lipid sorting; Membrane domain; Peptide association; Ras nanocluster

Indexed keywords

PEPTIDE; RAS PROTEIN; NANOMATERIAL;

EID: 84870233152     PISSN: 21541248     EISSN: 21541256     Source Type: Journal    
DOI: 10.4161/sgtp.21829     Document Type: Note
Times cited : (9)

References (37)
  • 1
    • 0037542854 scopus 로고    scopus 로고
    • Ras proteins: Different signals from different locations
    • PMID:12728271
    • Hancock JF. Ras proteins: different signals from different locations. Nat Rev Mol Cell Biol 2003; 4:373-84; PMID:12728271; http://dx.doi.org/10.1038/ n rm1105.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 373-384
    • Hancock, J.F.1
  • 2
    • 35648980477 scopus 로고    scopus 로고
    • Ras nano-clusters: Molecular structure and assembly
    • PMID:17897845
    • Abankwa D, Gorfe AA, Hancock JF. Ras nano-clusters: molecular structure and assembly. Semin Cell Dev Biol 2007; 18:599-607; PMID:17897845; http://dx.doi.org/10.1016/j.semcdb.2007.08.003.
    • (2007) Semin Cell Dev Biol , vol.18 , pp. 599-607
    • Abankwa, D.1    Gorfe, A.A.2    Hancock, J.F.3
  • 3
    • 45849130495 scopus 로고    scopus 로고
    • Ras oncogenes: Split personalities
    • PMID:18568040
    • Karnoub AE, Weinberg RA. Ras oncogenes: split personalities. Nat Rev Mol Cell Biol 2008; 9:517-31; PMID:18568040; http://dx.doi.org/10.1038/ nrm2438.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 517-531
    • Karnoub, A.E.1    Weinberg, R.A.2
  • 4
    • 3242657115 scopus 로고    scopus 로고
    • Three separable domains regulate GTP-dependent association of H-ras with the plasma membrane
    • PMID:15254246
    • Rotblat B, Prior IA, Muncke C, Parton RG, Kloog Y, Henis YI, et al. Three separable domains regulate GTP-dependent association of H-ras with the plasma membrane. Mol Cell Biol 2004; 24:6799-810; PMID:15254246; http://dx.doi.org/10.1128/ MCB.24.15.6799-6810.2004.
    • (2004) Mol Cell Biol , vol.24 , pp. 6799-6810
    • Rotblat, B.1    Prior, I.A.2    Muncke, C.3    Parton, R.G.4    Kloog, Y.5    Henis, Y.I.6
  • 5
    • 27344456331 scopus 로고    scopus 로고
    • H-ras, K-ras, and inner plasma membrane raft proteins operate in nanoclusters with differential dependence on the actin cytoskeleton
    • PMID:16223883
    • Plowman SJ, Muncke C, Parton RG, Hancock JF. H-ras, K-ras, and inner plasma membrane raft proteins operate in nanoclusters with differential dependence on the actin cytoskeleton. Proc Natl Acad Sci USA 2005; 102:15500-5; PMID:16223883; http:// dx.doi.org/10.1073/pnas.0504114102.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 15500-15505
    • Plowman, S.J.1    Muncke, C.2    Parton, R.G.3    Hancock, J.F.4
  • 6
    • 79851483766 scopus 로고    scopus 로고
    • Membrane-mediated induction and sorting of K-Ras microdomain signaling platforms
    • PMID:21141956
    • Weise K, Kapoor S, Denter C, Nikolaus J, Opitz N, Koch S, et al. Membrane-mediated induction and sorting of K-Ras microdomain signaling platforms. J Am Chem Soc 2011; 133:880-7; PMID:21141956; http://dx.doi.org/10.1021/ja107532q.
    • (2011) J Am Chem Soc , vol.133 , pp. 880-887
    • Weise, K.1    Kapoor, S.2    Denter, C.3    Nikolaus, J.4    Opitz, N.5    Koch, S.6
  • 7
    • 63149129301 scopus 로고    scopus 로고
    • Influence of the lipidation motif on the partitioning and association of N-Ras in model membrane subdomains
    • PMID:19133719
    • Weise K, Triola G, Brunsveld L, Waldmann H, Winter R. Influence of the lipidation motif on the partitioning and association of N-Ras in model membrane subdomains. J Am Chem Soc 2009; 131:1557-64; PMID:19133719; http://dx.doi.org/10.1021/ ja808691r.
    • (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
  • 8
    • 77954728132 scopus 로고    scopus 로고
    • Visualizing association of lipidated signaling proteins in heterogeneous membranes-partitioning into subdomains, lipid sorting, interfacial adsorption, and protein association
    • Weise K, Triola G, Janosch S, Waldmann H, Winter R. Visualizing association of lipidated signaling proteins in heterogeneous membranes-partitioning into subdomains, lipid sorting, interfacial adsorption, and protein association. Biochim Biophys Acta 2010; 1798: 1409-17.
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 1409-1417
    • Weise, K.1    Triola, G.2    Janosch, S.3    Waldmann, H.4    Winter, R.5
  • 9
    • 0024406286 scopus 로고
    • All ras proteins are polyisoprenylated but only some are palmitoylated
    • PMID:2661017
    • Hancock JF, Magee AI, Childs JE, Marshall CJ. All ras proteins are polyisoprenylated but only some are palmitoylated. Cell 1989; 57:1167-77; PMID:2661017; http://dx.doi.org/10.1016/0092-8674(89)90054-8.
    • (1989) Cell , vol.57 , pp. 1167-1177
    • Hancock, J.F.1    Magee, A.I.2    Childs, J.E.3    Marshall, C.J.4
  • 10
    • 78649474147 scopus 로고    scopus 로고
    • Ras history: The saga continues
    • PMID:21686117
    • Cox AD, Der CJ. Ras history: The saga continues. Small GTPases 2010; 1:2-27; PMID:21686117; http://dx.doi.org/10.4161/sgtp.1.1.12178.
    • (2010) Small GTPases , vol.1 , pp. 2-27
    • Cox, A.D.1    Der, C.J.2
  • 11
    • 36048957164 scopus 로고    scopus 로고
    • Free Energy Profile of H-ras Membrane Anchor upon Membrane Insertion
    • Gorfe A A, Babakhani A, McCammon JA. Free Energy Profile of H-ras Membrane Anchor upon Membrane Insertion. Angew Chem Int Ed 2007; 119:8382-5; http://dx.doi.org/10.1002/ange.200702379.
    • (2007) Angew Chem Int Ed , vol.119 , pp. 8382-8385
    • Gorfe, A.A.1    Babakhani, A.2    McCammon, J.A.3
  • 12
    • 9344238828 scopus 로고    scopus 로고
    • Membrane localization and flexibility of a lipidated ras peptide studied by molecular dynamics simulations
    • PMID:15548025
    • Gorfe AA, Pellarin R, Caflisch A. Membrane localization and flexibility of a lipidated ras peptide studied by molecular dynamics simulations. J Am Chem Soc 2004; 126:15277-86; PMID:15548025; http:// dx.doi.org/10.1021/ja046607n.
    • (2004) J Am Chem Soc , vol.126 , pp. 15277-15286
    • Gorfe, A.A.1    Pellarin, R.2    Caflisch, A.3
  • 13
    • 52449083121 scopus 로고    scopus 로고
    • Similar membrane affinity of mono- and Di-S-acylated ras membrane anchors: A new twist in the role of protein lipidation
    • PMID:18761454
    • Gorfe AA, McCammon JA. Similar membrane affinity of mono- and Di-S-acylated ras membrane anchors: a new twist in the role of protein lipidation. J Am Chem Soc 2008; 130:12624-5; PMID:18761454; http://dx.doi.org/10.1021/ja805110q.
    • (2008) J Am Chem Soc , vol.130 , pp. 12624-12625
    • Gorfe, A.A.1    McCammon, J.A.2
  • 14
    • 55949092407 scopus 로고    scopus 로고
    • Water-membrane partition thermodynamics of an amphi-philic lipopeptide: An enthalpy-driven hydrophobic ef fect
    • PMID:18621822
    • Gorfe AA, Baron R, McCammon JA. Water-membrane partition thermodynamics of an amphi-philic lipopeptide: an enthalpy-driven hydrophobic ef fect. Biophys J 2008; 95:3269-77; PMID:18621822; http://dx.doi.org/10.1529/biophysj.108.136481.
    • (2008) Biophys J , vol.95 , pp. 3269-3277
    • Gorfe, A.A.1    Baron, R.2    McCammon, J.A.3
  • 15
    • 58149197889 scopus 로고    scopus 로고
    • Membrane binding of lipidated ras peptides and proteins-the structural point of view
    • Brunsveld L, Waldmann H, Huster D. Membrane binding of lipidated ras peptides and proteins-the structural point of view. Biochim Biophys Acta 2009; 1788:273-88.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 273-288
    • Brunsveld, L.1    Waldmann, H.2    Huster, D.3
  • 16
    • 0037427329 scopus 로고    scopus 로고
    • Membrane insertion of a lipidated ras peptide studied by FTIR, solid-state NMR, and neutron diffraction spectroscopy
    • PMID:12670227
    • Huster D, Vogel A, Katzka C, Scheidt HA, Binder H, Dante S, et al. Membrane insertion of a lipidated ras peptide studied by FTIR, solid-state NMR, and neutron diffraction spectroscopy. J Am Chem Soc 2003; 125:4070-9; PMID:12670227; http://dx.doi. org/10.1021/ja0289245.
    • (2003) J Am Chem Soc , vol.125 , pp. 4070-4079
    • Huster, D.1    Vogel, A.2    Katzka, C.3    Scheidt, H.A.4    Binder, H.5    Dante, S.6
  • 17
    • 0035980238 scopus 로고    scopus 로고
    • Partitioning of lipidated peptide sequences into liquid-ordered lipid domains in model and biological membranes
    • PMID:11669641
    • Wang TY, Leventis R, Silvius JR. Partitioning of lipidated peptide sequences into liquid-ordered lipid domains in model and biological membranes. Biochemistry 2001; 40:13031-40; PMID:11669641; http://dx.doi.org/10.1021/bi0112311.
    • (2001) Biochemistry , vol.40 , pp. 13031-13040
    • Wang, T.Y.1    Leventis, R.2    Silvius, J.R.3
  • 18
    • 29144484142 scopus 로고    scopus 로고
    • Partitioning of membrane molecules between raft and non-raft domains: Insights from model-membrane studies
    • Silvius JR. Partitioning of membrane molecules between raft and non-raft domains: insights from model-membrane studies. Biochim Biophys Acta 2005; 1746:193-202.
    • (2005) Biochim Biophys Acta , vol.1746 , Issue.5 , pp. 193-202
    • Silvius, J.R.1
  • 19
    • 40949130399 scopus 로고    scopus 로고
    • A novel switch region regulates H-ras membrane orientation and signal output
    • PMID:18273062
    • Abankwa D, Hanzal-Bayer M, Ariotti N, Plowman SJ, Gorfe AA, Parton RG, et al. A novel switch region regulates H-ras membrane orientation and signal output. EMBO J 2008; 27:727-35; PMID:18273062; http://dx.doi.org/10.1038/emboj.2008.10.
    • (2008) EMBO J , vol.27 , pp. 727-735
    • Abankwa, D.1    Hanzal-Bayer, M.2    Ariotti, N.3    Plowman, S.J.4    Gorfe, A.A.5    Parton, R.G.6
  • 21
    • 33847413103 scopus 로고    scopus 로고
    • Structure and dynamics of the full-length lipid-modified H-Ras protein in a 1,2-dimyristoylglycero-3-phosphocholine bilayer
    • PMID:17263520
    • Gorfe AA, Hanzal-Bayer M, Abankwa D, Hancock JF, McCammon JA. Structure and dynamics of the full-length lipid-modified H-Ras protein in a 1,2-dimyristoylglycero-3-phosphocholine bilayer. J Med Chem 2007; 50:674-84; PMID:17263520; http://dx.doi.org/10.1021/jm061053f.
    • (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
  • 22
    • 75749150934 scopus 로고    scopus 로고
    • Ras membrane orientation and nanodomain localization generate isoform diversity
    • PMID:20080631
    • Abankwa D, Gorfe AA, Inder K, Hancock JF. Ras membrane orientation and nanodomain localization generate isoform diversity. Proc Natl Acad Sci USA 2010; 107:1130-5; PMID:20080631; http://dx.doi. org/10.1073/pnas.0903907107.
    • (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
  • 23
    • 35048822834 scopus 로고    scopus 로고
    • H-ras protein in a bilayer: Interaction and structure perturbation
    • PMID:17880077
    • Gorfe AA, Babakhani A, McCammon JA. H-ras protein in a bilayer: interaction and structure perturbation. J Am Chem Soc 2007; 129:12280-6; PMID:17880077; http://dx.doi.org/10.1021/ ja 0 739 49 v.
    • (2007) J Am Chem Soc , vol.129 , pp. 12280-12286
    • Gorfe, A.A.1    Babakhani, A.2    McCammon, J.A.3
  • 24
    • 35349022518 scopus 로고    scopus 로고
    • Flexibility of ras lipid modifications studied by 2H solid-state NMR and molecular dynamics simulations
    • PMID:17557790
    • Vogel A, Tan KT, Waldmann H, Feller SE, Brown MF, Huster D. Flexibility of ras lipid modifications studied by 2H solid-state NMR and molecular dynamics simulations. Biophys J 2007; 93:2697-712; PMID:17557790; http://dx.doi.org/10.1529/ biophysj.107.104562.
    • (2007) Biophys J , vol.93 , pp. 2697-2712
    • Vogel, A.1    Tan, K.T.2    Waldmann, H.3    Feller, S.E.4    Brown, M.F.5    Huster, D.6
  • 25
    • 78649821287 scopus 로고    scopus 로고
    • Segregation of negatively charged phospholipids by the polycationic and farnesylated membrane anchor of Kras
    • PMID:21112291
    • Janosi L, Gorfe AA. Segregation of negatively charged phospholipids by the polycationic and farnesylated membrane anchor of Kras. Biophys J 2010; 99:3666-74; PMID:21112291; http://dx.doi.org/10.1016/j. bpj.2010.10.031.
    • (2010) Biophys J , vol.99 , pp. 3666-3674
    • Janosi, L.1    Gorfe, A.A.2
  • 26
    • 79959844734 scopus 로고    scopus 로고
    • Dynamic structure formation of peripheral membrane proteins
    • PMID:21731477
    • Morozova D, Guigas G, Weiss M. Dynamic structure formation of peripheral membrane proteins. PLoS Comput Biol 2011; 7:e1002067; PMID:21731477; http://dx.doi.org/10.1371/journal.pcbi.1002067.
    • (2011) PLoS Comput Biol , vol.7
    • Morozova, D.1    Guigas, G.2    Weiss, M.3
  • 27
    • 77953011495 scopus 로고    scopus 로고
    • Cluster formation of anchored proteins induced by membrane-mediated interaction
    • PMID:20513399
    • Li S, Zhang X, Wang W. Cluster formation of anchored proteins induced by membrane-mediated interaction. Biophys J 2010; 98:2554-63; PMID:20513399; http://dx.doi.org/10.1016/j. bpj.2010.02.032.
    • (2010) Biophys J , vol.98 , pp. 2554-2563
    • Li, S.1    Zhang, X.2    Wang, W.3
  • 28
    • 78649712786 scopus 로고    scopus 로고
    • The relationship between membrane curvature generation and clustering of anchored proteins: A computer simulation study
    • Yue T, Li S, Zhang X, Wang W. The relationship between membrane curvature generation and clustering of anchored proteins: a computer simulation study. Soft Matter 2010; 6:6109-18; http://dx.doi. org/10.1039/c0sm00418a.
    • (2010) Soft Matter , vol.6 , pp. 6109-6118
    • Yue, T.1    Li, S.2    Zhang, X.3    Wang, W.4
  • 29
    • 24644498037 scopus 로고    scopus 로고
    • Lipid modifications of a Ras peptide exhibit altered packing and mobility versus host membrane as detected by 2H solid-state NMR
    • PMID:16131204
    • Vogel A, Katzka CP, Waldmann H, Arnold K, Brown MF, Huster D. Lipid modifications of a Ras peptide exhibit altered packing and mobility versus host membrane as detected by 2H solid-state NMR. J Am Chem Soc 2005; 127:12263-72; PMID:16131204; http: //dx.doi.org/10.1021/ja051856c.
    • (2005) J Am Chem Soc , vol.127 , pp. 12263-12272
    • Vogel, A.1    Katzka, C.P.2    Waldmann, H.3    Arnold, K.4    Brown, M.F.5    Huster, D.6
  • 30
    • 58149308560 scopus 로고    scopus 로고
    • Phenomenological model and phase behavior of saturated and unsaturated lipids and cholesterol
    • PMID:18708463
    • Putzel GG, Schick M. Phenomenological model and phase behavior of saturated and unsaturated lipids and cholesterol. Biophys J 2008; 95:4756-62; PMID:18708463; http://dx.doi.org/10.1529/bio-physj.108.136317.
    • (2008) Biophys J , vol.95 , pp. 4756-4762
    • Putzel, G.G.1    Schick, M.2
  • 31
    • 79952153989 scopus 로고    scopus 로고
    • Lipid packing drives the segregation of transmembrane helices into disordered lipid domains in model membranes
    • PMID:21205902
    • Schäfer LV, de Jong DH, Holt A, Rzepiela AJ, de Vries AH, Poolman B, et al. Lipid packing drives the segregation of transmembrane helices into disordered lipid domains in model membranes. Proc Natl Acad Sci USA 2011; 108:1343-8; PMID:21205902; http: //dx.doi.org/10.1073/pnas.1009362108.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 1343-1348
    • Schäfer, L.V.1    de Jong, D.H.2    Holt, A.3    Rzepiela, A.J.4    de Vries, A.H.5    Poolman, B.6
  • 32
    • 36049049559 scopus 로고    scopus 로고
    • Why are lipid rafts not observed in vivo?
    • PMID:17660324
    • Yethiraj A, Weisshaar JC. Why are lipid rafts not observed in vivo? Biophys J 2007; 93:3113-9; PMID:17660324; http://dx.doi.org/10.1529/bio-physj.106.101931.
    • (2007) Biophys J , vol.93 , pp. 3113-3119
    • Yethiraj, A.1    Weisshaar, J.C.2
  • 33
    • 33644786912 scopus 로고    scopus 로고
    • Phase diagram of a ternary mixture of cholesterol and saturated and unsatu-rated lipids calculated from a microscopic model
    • PMID:16606318
    • Elliott R, Szleifer I, Schick M. Phase diagram of a ternary mixture of cholesterol and saturated and unsatu-rated lipids calculated from a microscopic model. Phys Rev Lett 2006; 96:098101; PMID:16606318; http: //dx.doi.org/10.1103/PhysRevLett.96.098101.
    • (2006) Phys Rev Lett , vol.96 , pp. 098101
    • Elliott, R.1    Szleifer, I.2    Schick, M.3
  • 34
    • 50349098382 scopus 로고    scopus 로고
    • Molecular simulations of lipid-mediated protein-protein interactions
    • PMID:18487292
    • de Meyer FJM, Venturoli M, Smit B. Molecular simulations of lipid-mediated protein-protein interactions. Biophys J 2008; 95:1851-65; PMID:18487292; http: //dx.doi.org/10.1529/biophysj.107.124164.
    • (2008) Biophys J , vol.95 , pp. 1851-1865
    • de Meyer, F.J.M.1    Venturoli, M.2    Smit, B.3
  • 35
    • 21244431672 scopus 로고    scopus 로고
    • Simulation studies of protein-induced bilayer deformations, and lipid-induced protein tilting, on a mesoscopic model for lipid bilayers with embedded proteins
    • PMID:15738466
    • Venturoli M, Smit B, Sperotto MM. Simulation studies of protein-induced bilayer deformations, and lipid-induced protein tilting, on a mesoscopic model for lipid bilayers with embedded proteins. Biophys J 2005; 88:1778-98; PMID:15738466; http://dx.doi. org/10.1529/biophysj.104.050849.
    • (2005) Biophys J , vol.88 , pp. 1778-1798
    • Venturoli, M.1    Smit, B.2    Sperotto, M.M.3
  • 36
    • 84857648415 scopus 로고    scopus 로고
    • Transmembrane helices can induce domain formation in crowded model membranes
    • Domanski J, Marrink SJ, Schäfer LV. Transmembrane helices can induce domain formation in crowded model membranes. Biochim Biophys Acta 2011; 1818:984-94.
    • (2011) Biochim Biophys Acta , vol.1818 , pp. 984-994
    • Domanski, J.1    Marrink, S.J.2    Schäfer, L.V.3
  • 37
    • 79958235987 scopus 로고    scopus 로고
    • Clusters of proteins in biomembranes: Insights into the roles of interaction potential shapes and of protein diversity
    • PMID:21528886
    • Meilhac N, Destainville N. Clusters of proteins in biomembranes: insights into the roles of interaction potential shapes and of protein diversity. J Phys Chem B 2011; 115:7190-9; PMID:21528886; http://dx.doi. org/10.1021/jp1099865.
    • (2011) J Phys Chem B , vol.115 , pp. 7190-7199
    • Meilhac, N.1    Destainville, N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.