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Volumn 4, Issue 7, 2009, Pages

Biophysical mechanism for ras-nanocluster formation and signaling in plasma membrane

Author keywords

[No Author keywords available]

Indexed keywords

GOLD; RAS PROTEIN;

EID: 67650308484     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0006148     Document Type: Article
Times cited : (34)

References (54)
  • 1
    • 33748579946 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of the membrane skeleton at the plasma membrane interface by electron tomography
    • Morone N, Fujiwara T, Murase K, Kasai RS, Ike H, et al. (2006) Three-dimensional reconstruction of the membrane skeleton at the plasma membrane interface by electron tomography. J Cell Biol 174: 851-862.
    • (2006) J Cell Biol , vol.174 , pp. 851-862
    • Morone, N.1    Fujiwara, T.2    Murase, K.3    Kasai, R.S.4    Ike, H.5
  • 2
    • 0036709020 scopus 로고    scopus 로고
    • Fidelity and spatio-temporal control in MAP kinase (ERKs) signaling
    • Pouysségur J, Volmat V, Lenormand P (2002) Fidelity and spatio-temporal control in MAP kinase (ERKs) signaling. Biochem Pharmacol 64: 755-763.
    • (2002) Biochem Pharmacol , vol.64 , pp. 755-763
    • Pouysségur, J.1    Volmat, V.2    Lenormand, P.3
  • 3
    • 33747591249 scopus 로고    scopus 로고
    • Dynamics in the plasma membrane: How to combine fluidity and order
    • Marguet D, Lenne PF, Rigneault H, He HT (2006) Dynamics in the plasma membrane: how to combine fluidity and order. EMBO J 25: 3446-3457.
    • (2006) EMBO J , vol.25 , pp. 3446-3457
    • Marguet, D.1    Lenne, P.F.2    Rigneault, H.3    He, H.T.4
  • 4
    • 35649010379 scopus 로고    scopus 로고
    • Lipid rafts, fluid/fluid phase separation, and their relevance to plasma membrane structure and function
    • Sengupta P, Baird B, Holowka D (2007) Lipid rafts, fluid/fluid phase separation, and their relevance to plasma membrane structure and function. Sem Cell & Devel Biol 18: 583-590.
    • (2007) Sem Cell & Devel Biol , vol.18 , pp. 583-590
    • Sengupta, P.1    Baird, B.2    Holowka, D.3
  • 5
    • 0034644537 scopus 로고    scopus 로고
    • Ras and Rho GTPases: A family reunion
    • Bar-Sagi D, Hall A (2000) Ras and Rho GTPases: a family reunion. Cell 103: 227-238.
    • (2000) Cell , vol.103 , pp. 227-238
    • Bar-Sagi, D.1    Hall, A.2
  • 6
    • 18544407093 scopus 로고    scopus 로고
    • Ras GTPases: Singing in tune
    • Symons M, Takai Y (2001) Ras GTPases: singing in tune. Sci STKE 68: PE1.
    • (2001) Sci STKE , vol.68
    • Symons, M.1    Takai, Y.2
  • 7
    • 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
  • 8
    • 36248934768 scopus 로고    scopus 로고
    • Interactions of Ras proteins with the plasma membrane and their roles in signalling
    • Eisenberg S, Henis YI (2008) Interactions of Ras proteins with the plasma membrane and their roles in signalling. Cell Signal 20: 31-39.
    • (2008) Cell Signal , vol.20 , pp. 31-39
    • Eisenberg, S.1    Henis, Y.I.2
  • 9
    • 0033145517 scopus 로고    scopus 로고
    • Dominant-negative caveolin inhibits H-Ras function by disrupting cholesterol-rich plasma membrane domains
    • Roy S, Luetterforst R, Harding A, Apolloni A, Etheridge M, et al. (1999) Dominant-negative caveolin inhibits H-Ras function by disrupting cholesterol-rich plasma membrane domains. Nat Cell Biol 1: 98-105.
    • (1999) Nat Cell Biol , vol.1 , pp. 98-105
    • Roy, S.1    Luetterforst, R.2    Harding, A.3    Apolloni, A.4    Etheridge, M.5
  • 10
    • 0035067187 scopus 로고    scopus 로고
    • GTP-dependent segregation of H-ras from lipid rafts is required for biological activity
    • Prior IA, Harding A, Yan J, Sluimer J, Parton RG, et al. (2001) GTP-dependent segregation of H-ras from lipid rafts is required for biological activity. Nat Cell Biol 3: 368-375.
    • (2001) Nat Cell Biol , vol.3 , pp. 368-375
    • Prior, I.A.1    Harding, A.2    Yan, J.3    Sluimer, J.4    Parton, R.G.5
  • 11
    • 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
    • Plowman SJ, Muncke C, Parton RG, Hancock JF (2005) 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 102: 15500-15505.
    • (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
  • 12
    • 0344585437 scopus 로고    scopus 로고
    • Lipid rafts: Elusive or illusive?
    • Munro S (2003) Lipid rafts: elusive or illusive? Cell 115: 377-388.
    • (2003) Cell , vol.115 , pp. 377-388
    • Munro, S.1
  • 13
    • 0035908493 scopus 로고    scopus 로고
    • Blocking oncogenic ras signaling for cancer therapy
    • Adjei AA (2001) Blocking oncogenic ras signaling for cancer therapy. J Nat Canc Inst 93: 1062-1074.
    • (2001) J Nat Canc Inst , vol.93 , pp. 1062-1074
    • Adjei, A.A.1
  • 14
    • 48849083854 scopus 로고    scopus 로고
    • Silent assassin: Oncogenic ras directs epigenetic inactivation of target genes
    • Cheng X (2008) Silent assassin: oncogenic ras directs epigenetic inactivation of target genes. Sci Signal 1: pe14.
    • (2008) Sci Signal 1: Pe14
    • Cheng, X.1
  • 16
    • 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
  • 18
    • 67650334765 scopus 로고    scopus 로고
    • Ras acylation, compartmentalization and signaling nanoclusters
    • Henis YI, Hancock JF, Prior IA (2008) Ras acylation, compartmentalization and signaling nanoclusters. Mol Membr Biol 29: 1-13.
    • (2008) Mol Membr Biol , vol.29 , pp. 1-13
    • Henis, Y.I.1    Hancock, J.F.2    Prior, I.A.3
  • 19
    • 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
  • 20
    • 0034667593 scopus 로고    scopus 로고
    • Kolch W (2000) Meaningful relationships: the regulation of the Ras/Raf/ MEK/ERK pathway by protein interactions. Biochem J 351: 289-305 (2000).
    • Kolch W (2000) Meaningful relationships: the regulation of the Ras/Raf/ MEK/ERK pathway by protein interactions. Biochem J 351: 289-305 (2000).
  • 22
    • 19444382673 scopus 로고    scopus 로고
    • Single-molecule diffusion measurements of H-Ras at the plasma membrane of live cells reveal microdomain localization upon activation
    • Lommerse PH, Snaar-Jagalska BE, Spaink HP, Schmidt T (2005) Single-molecule diffusion measurements of H-Ras at the plasma membrane of live cells reveal microdomain localization upon activation. J Cell Sci 118: 1799-1809.
    • (2005) J Cell Sci , vol.118 , pp. 1799-1809
    • Lommerse, P.H.1    Snaar-Jagalska, B.E.2    Spaink, H.P.3    Schmidt, T.4
  • 23
    • 22144479017 scopus 로고    scopus 로고
    • Ras plasma membrane signalling platforms
    • Hancock JF, Parton RG (2005) Ras plasma membrane signalling platforms. Biochem J 389: 1-11.
    • (2005) Biochem J , vol.389 , pp. 1-11
    • Hancock, J.F.1    Parton, R.G.2
  • 24
    • 34547561587 scopus 로고    scopus 로고
    • Plasma membrane nanoswitches generate high-fidelity Ras signal transduction
    • Tian T, Harding A, Inder K, Plowman S, Parton RG, et al. (2007) Plasma membrane nanoswitches generate high-fidelity Ras signal transduction. Nature Cell Biol 9: 905-914.
    • (2007) Nature Cell Biol , vol.9 , pp. 905-914
    • Tian, T.1    Harding, A.2    Inder, K.3    Plowman, S.4    Parton, R.G.5
  • 25
    • 48449092211 scopus 로고    scopus 로고
    • Using plasma membrane nanoclusters to build better signaling circuits
    • Harding AS, Hancock JF (2008) Using plasma membrane nanoclusters to build better signaling circuits. Trends Cell Biol 18: 364-371.
    • (2008) Trends Cell Biol , vol.18 , pp. 364-371
    • Harding, A.S.1    Hancock, J.F.2
  • 26
    • 40549111933 scopus 로고    scopus 로고
    • Ras nanoclusters: Combining digital and analog signaling
    • Harding A, Hancock JF (2008) Ras nanoclusters: combining digital and analog signaling. Cell Cycle 7: 127-134.
    • (2008) Cell Cycle , vol.7 , pp. 127-134
    • Harding, A.1    Hancock, J.F.2
  • 28
    • 23844500699 scopus 로고    scopus 로고
    • Compartmentalized signalling of Ras
    • Philips MR (2005) Compartmentalized signalling of Ras. Biochem Soc Trans 33: 657-661.
    • (2005) Biochem Soc Trans , vol.33 , pp. 657-661
    • Philips, M.R.1
  • 31
    • 0036696824 scopus 로고    scopus 로고
    • Lateral propagation of EGF signaling after local stimulation is dependent on receptor density
    • Sawano A, Takayama S, Matsuda M, Miyawaki A (2002) Lateral propagation of EGF signaling after local stimulation is dependent on receptor density. Dev Cell 3: 245-257.
    • (2002) Dev Cell , vol.3 , pp. 245-257
    • Sawano, A.1    Takayama, S.2    Matsuda, M.3    Miyawaki, A.4
  • 32
    • 0038732770 scopus 로고    scopus 로고
    • EGFR activation coupled to inhibition of tyrosine phosphatases causes lateral signal propagation
    • Reynolds AR, Tischer C, Verveer PJ, Rocks O, Bastiaens PI (2003) EGFR activation coupled to inhibition of tyrosine phosphatases causes lateral signal propagation. Nat Cell Biol 5: 447-453.
    • (2003) Nat Cell Biol , vol.5 , pp. 447-453
    • Reynolds, A.R.1    Tischer, C.2    Verveer, P.J.3    Rocks, O.4    Bastiaens, P.I.5
  • 33
    • 1342306818 scopus 로고    scopus 로고
    • Nanoscale organization of multiple GPI-anchored proteins in living cell membranes
    • Sharma P, Varma R, Sarasij RC, IraGousset K, et al. (2004) Nanoscale organization of multiple GPI-anchored proteins in living cell membranes. Cell 116: 577-589.
    • (2004) Cell , vol.116 , pp. 577-589
    • Sharma, P.1    Varma, R.2    Sarasij, R.C.3    IraGousset, K.4
  • 34
    • 37549035926 scopus 로고    scopus 로고
    • Clustering of membrane raft proteins by the actin cytoskeleton
    • Chichili GR, Rodgers W (2007) Clustering of membrane raft proteins by the actin cytoskeleton. J Biol Chem 282: 36682-36691.
    • (2007) J Biol Chem , vol.282 , pp. 36682-36691
    • Chichili, G.R.1    Rodgers, W.2
  • 35
    • 10044247245 scopus 로고    scopus 로고
    • Pattern formation during T-cell adhesion
    • Weikl TR, Lipowsky R (2004) Pattern formation during T-cell adhesion. Biophys J 87: 3665-3678.
    • (2004) Biophys J , vol.87 , pp. 3665-3678
    • Weikl, T.R.1    Lipowsky, R.2
  • 36
    • 18944374155 scopus 로고    scopus 로고
    • Graded mitogen-activated protein kinase activity precedes switch-like c-Fos induction in mammalian cells
    • Mackeigan JP, Murphy LO, Dimitri CA, Blenis J (2005) Graded mitogen-activated protein kinase activity precedes switch-like c-Fos induction in mammalian cells. Mol Cell Biol 25: 4676-4682.
    • (2005) Mol Cell Biol , vol.25 , pp. 4676-4682
    • Mackeigan, J.P.1    Murphy, L.O.2    Dimitri, C.A.3    Blenis, J.4
  • 37
    • 46149107301 scopus 로고    scopus 로고
    • Electrostatic interactions positively regulate K-Ras nanocluster formation and function
    • Plowman SJ, Ariotti N, Goodall A, Parton RG, Hancock JF (2008) Electrostatic interactions positively regulate K-Ras nanocluster formation and function. Mol Cell Biol 28: 4377-4385.
    • (2008) Mol Cell Biol , vol.28 , pp. 4377-4385
    • Plowman, S.J.1    Ariotti, N.2    Goodall, A.3    Parton, R.G.4    Hancock, J.F.5
  • 38
    • 9344238828 scopus 로고    scopus 로고
    • Membrane localization and flexibility of a lipidated ras peptide studied by molecular dynamics simulations
    • Gorfe AA, Pellarin R, Caflisch A (2004) Membrane localization and flexibility of a lipidated ras peptide studied by molecular dynamics simulations. J Am Chem Soc 126: 15277-15286.
    • (2004) J Am Chem Soc , vol.126 , pp. 15277-15286
    • Gorfe, A.A.1    Pellarin, R.2    Caflisch, A.3
  • 39
    • 33751395400 scopus 로고    scopus 로고
    • A curvature-mediated mechanism for localization of lipids to bacterial poles
    • Huang KC, Mukhopadhyay R, Wingreen NS (2006) A curvature-mediated mechanism for localization of lipids to bacterial poles. PLoS Comput Biol 2: e151.
    • (2006) PLoS Comput Biol , vol.2
    • Huang, K.C.1    Mukhopadhyay, R.2    Wingreen, N.S.3
  • 40
    • 50949133967 scopus 로고    scopus 로고
    • Arf family GTP loading is activated by, and generates, positive membrane curvature
    • Lundmark R, Doherty GJ, Vallis Y, Peter BJ, McMahon HT (2008) Arf family GTP loading is activated by, and generates, positive membrane curvature. Biochem J 414: 189-194.
    • (2008) Biochem J , vol.414 , pp. 189-194
    • Lundmark, R.1    Doherty, G.J.2    Vallis, Y.3    Peter, B.J.4    McMahon, H.T.5
  • 41
    • 0025327522 scopus 로고
    • Crystal structure of an active form of RAS protein, a complex of a GTP analog and the HRAS p21 catalytic domain
    • Brünger AT, Milburn MV, Tong L, deVos AM, Jancarik J, et al. (1990) Crystal structure of an active form of RAS protein, a complex of a GTP analog and the HRAS p21 catalytic domain. Proc Natl Acad Sci USA 87: 4849-4853.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4849-4853
    • Brünger, A.T.1    Milburn, M.V.2    Tong, L.3    deVos, A.M.4    Jancarik, J.5
  • 42
    • 67650334873 scopus 로고    scopus 로고
    • Activated K-Ras and H-Ras display different interactions with saturable nonraft sites at the surface of live cells
    • Niv H, Gutman O, Kloog Y, Henis YI (2004) Activated K-Ras and H-Ras display different interactions with saturable nonraft sites at the surface of live cells. J Cell Biol 165: 725-746.
    • (2004) J Cell Biol , vol.165 , pp. 725-746
    • Niv, H.1    Gutman, O.2    Kloog, Y.3    Henis, Y.I.4
  • 43
    • 33746725960 scopus 로고    scopus 로고
    • Single-molecule diffusion reveals similar mobility for the Lck, H-ras, and K-ras membrane anchors
    • Lommerse PH, Vastenhoud K, Pirinen NJ, Magee AI, Spaink HP, et al. (2006) Single-molecule diffusion reveals similar mobility for the Lck, H-ras, and K-ras membrane anchors. Biophys J 91: 1090-1097.
    • (2006) Biophys J , vol.91 , pp. 1090-1097
    • Lommerse, P.H.1    Vastenhoud, K.2    Pirinen, N.J.3    Magee, A.I.4    Spaink, H.P.5
  • 44
    • 33645241165 scopus 로고    scopus 로고
    • Identifying optimal lipid raft characteristics required to promote nanoscale protein-protein interactions on the plasma membrane
    • Nicolau Jr DV, Burrage K, Parton RG, Hancock JF (2006) Identifying optimal lipid raft characteristics required to promote nanoscale protein-protein interactions on the plasma membrane. Mol Cell Biol 26: 313-323.
    • (2006) Mol Cell Biol , vol.26 , pp. 313-323
    • Nicolau Jr, D.V.1    Burrage, K.2    Parton, R.G.3    Hancock, J.F.4
  • 45
  • 46
    • 58849115047 scopus 로고    scopus 로고
    • Polar chemoreceptor clustering by coupled trimers of dimers
    • Endres RG (2009) Polar chemoreceptor clustering by coupled trimers of dimers. Biophys J 96: 453-463.
    • (2009) Biophys J , vol.96 , pp. 453-463
    • Endres, R.G.1
  • 47
    • 65649122726 scopus 로고    scopus 로고
    • Lattices, rafts, and scaffolds: Domain regulation of receptor signaling at the plasma membrane
    • Lajoie P, Goetz JG, Dennis JW, Nabi IR (2009) Lattices, rafts, and scaffolds: domain regulation of receptor signaling at the plasma membrane. J Cell Biol 185: 381-385.
    • (2009) J Cell Biol , vol.185 , pp. 381-385
    • Lajoie, P.1    Goetz, J.G.2    Dennis, J.W.3    Nabi, I.R.4
  • 49
    • 22144479017 scopus 로고    scopus 로고
    • Ras plasma membrane signalling platforms
    • Hancock JF, Parton RG (2005) Ras plasma membrane signalling platforms. Biochem J 389: 1-11.
    • (2005) Biochem J , vol.389 , pp. 1-11
    • Hancock, J.F.1    Parton, R.G.2
  • 50
    • 33645944980 scopus 로고    scopus 로고
    • Dynamic polymorphism of Ras observed by single molecule FRET is the basis for molecular recognition
    • Arai Y, Iwane AH, Wazawa T, Yokota H, Ishii Y, et al. (2006) Dynamic polymorphism of Ras observed by single molecule FRET is the basis for molecular recognition. Biochem Biophys Res Commun 343: 809-815.
    • (2006) Biochem Biophys Res Commun , vol.343 , pp. 809-815
    • Arai, Y.1    Iwane, A.H.2    Wazawa, T.3    Yokota, H.4    Ishii, Y.5
  • 51
    • 51049112309 scopus 로고    scopus 로고
    • Lipid localization in bacterial cells through curvature-mediated microphase separation
    • Mukhopadhyay R, Huang KC, Wingreen NS (2008) Lipid localization in bacterial cells through curvature-mediated microphase separation. Biophys J 95: 1034-1049.
    • (2008) Biophys J , vol.95 , pp. 1034-1049
    • Mukhopadhyay, R.1    Huang, K.C.2    Wingreen, N.S.3
  • 52
    • 0000313850 scopus 로고
    • The second-order analysis of stationary point processes
    • Ripley BD (1976) The second-order analysis of stationary point processes. J App Prob 13: 255-266.
    • (1976) J App Prob , vol.13 , pp. 255-266
    • Ripley, B.D.1
  • 53
    • 33747100195 scopus 로고    scopus 로고
    • Statistical analysis of reduced pair correlation functions of capillaries in the prostate gland
    • Mattfeldt T, Eckel S, Fleischer F, Schmidt V (2006) Statistical analysis of reduced pair correlation functions of capillaries in the prostate gland. J Microsc 223: 107-119.
    • (2006) J Microsc , vol.223 , pp. 107-119
    • Mattfeldt, T.1    Eckel, S.2    Fleischer, F.3    Schmidt, V.4
  • 54
    • 29744439539 scopus 로고    scopus 로고
    • Explorative statistical analysis of planar point processes in microscopy
    • Mattfeldt T (2005) Explorative statistical analysis of planar point processes in microscopy. J Microscopy 220: 131-139.
    • (2005) J Microscopy , vol.220 , pp. 131-139
    • Mattfeldt, T.1


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