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Volumn 99, Issue 2, 2010, Pages 534-543

Mathematical modeling of K-Ras nanocluster formation on the plasma membrane

Author keywords

[No Author keywords available]

Indexed keywords

GALECTIN 3; GUANOSINE TRIPHOSPHATE; NANOMATERIAL; RAS PROTEIN;

EID: 77955213426     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.04.055     Document Type: Article
Times cited : (40)

References (40)
  • 1
    • 1642553461 scopus 로고    scopus 로고
    • The dark side of Ras: Regulation of apoptosis
    • Cox, A. D., and C. J. Der. 2003. The dark side of Ras: regulation of apoptosis. Oncogene, 22:8999-9006.
    • (2003) Oncogene , vol.22 , pp. 8999-9006
    • Cox, A.D.1    Der, C.J.2
  • 2
    • 0037264633 scopus 로고    scopus 로고
    • Targeting RAS signalling pathways in cancer therapy
    • Downward, J. 2003. Targeting RAS signalling pathways in cancer therapy. Nat. Rev. Cancer. 3:11-22.
    • (2003) Nat. Rev. Cancer. , vol.3 , pp. 11-22
    • Downward, J.1
  • 3
    • 0029790351 scopus 로고    scopus 로고
    • Ultrasensitivity in the mitogen-activated protein kinase cascade
    • Huang, C. Y., and J. E. Ferrell, Jr. 1996. Ultrasensitivity in the mitogen- activated protein kinase cascade. Proc. Natl. Acad. Sci USA. 93: 10078-10083.
    • (1996) Proc. Natl. Acad. Sci USA , vol.93 , pp. 10078-10083
    • Huang, C.Y.1    Ferrell Jr., J.E.2
  • 4
    • 0037047611 scopus 로고    scopus 로고
    • MAP kinase phospha-tase as a locus of flexibility in a mitogen-activated protein kinase signaling network
    • Bhalla, U. S., P. T. Ram, and R. Iyengar. 2002. MAP kinase phospha- tase as a locus of flexibility in a mitogen-activated protein kinase signaling network. Science. 297:1018-1023.
    • (2002) Science. , vol.297 , pp. 1018-1023
    • Bhalla, U.S.1    Ram, P.T.2    Iyengar, R.3
  • 5
    • 34547561587 scopus 로고    scopus 로고
    • Plasma membrane nano- Switches generate high-fidelity Ras signal transduction
    • Tian, T., A. Harding, ..., J. F. Hancock. 2007. Plasma membrane nano- switches generate high-fidelity Ras signal transduction. Nat. Cell Biol. 9:905-914.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 905-914
    • Tian, T.1    Harding, A.2    Hancock, J.F.3
  • 6
    • 27744486991 scopus 로고    scopus 로고
    • Current challenges in quantitative modeling of epidermal growth factor signaling
    • Breitling, R., and D. Hoeller. 2005. Current challenges in quantitative modeling of epidermal growth factor signaling. FEBS Lett. 579: 6289-6294.
    • (2005) FEBS Lett. , vol.579 , pp. 6289-6294
    • Breitling, R.1    Hoeller, D.2
  • 7
    • 0037455589 scopus 로고    scopus 로고
    • Direct visualization of Ras proteins in spatially distinct cell surface microdomains
    • Prior, I. A., C Muncke, ..., J. F. Hancock. 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    Hancock, J.F.3
  • 8
    • 27344456331 scopus 로고    scopus 로고
    • H-ras, K-ras, and inner plasma membrane raft proteins operate in nanoclusters with differ- Ential dependence on the actin cytoskeleton
    • Plowman, S. J., C Muncke, ..., J. F. Hancock. 2005. H-ras, K-ras, and inner plasma membrane raft proteins operate in nanoclusters with differ- ential 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    Hancock, J.F.3
  • 9
    • 22144479017 scopus 로고    scopus 로고
    • Ras plasma membrane signalling platforms
    • Hancock, J. F., and R. G. Parton. 2005. Ras plasma membrane signal- ling platforms. Biochem. J. 389:1-11.
    • (2005) Biochem. J. , vol.389 , pp. 1-11
    • Hancock, J.F.1    Parton, R.G.2
  • 10
    • 2442538177 scopus 로고    scopus 로고
    • Single-molecule imaging analysis of Ras activation in living cells
    • Murakoshi, H., R. lino, ..., A. Kusumi. 2004. Single-molecule imaging analysis of Ras activation in living cells. Proc Natl. Acad. Sci USA. 101:7317-7322.
    • (2004) Proc Natl. Acad. Sci USA , vol.101 , pp. 7317-7322
    • Murakoshi, H.1    Lino, R.2    Kusumi, A.3
  • 11
    • 46149107301 scopus 로고    scopus 로고
    • Electrostatic interactions positively regulate K-Ras nanocluster formation and function
    • Plowman, S. J., N. Ariotti, ..., J. F. Hancock. 2008. Electrostatic inter- actions 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    Hancock, J.F.3
  • 12
    • 48449092211 scopus 로고    scopus 로고
    • Using plasma membrane nano-clusters to build better signaling circuits
    • Harding, A. S., and J. F. Hancock. 2008. Using plasma membrane nano- clusters 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
  • 13
    • 53049098385 scopus 로고    scopus 로고
    • K-ras nano-clustering is subverted by overexpression of the scaffold protein galectin-3
    • Shalom-Feuerstein, R., S. J. Plowman, ..., Y. Kloog. 2008. K-ras nano- clustering is subverted by overexpression of the scaffold protein galec- tin-3. Cancer Res. 68:6608-6616.
    • (2008) Cancer Res. , vol.68 , pp. 6608-6616
    • Shalom-Feuerstein, R.1    Plowman, S.J.2    Kloog, Y.3
  • 14
    • 4544295231 scopus 로고    scopus 로고
    • Galectin-3 augments K-Ras activation, and triggers a Ras signal that attenuates ERK but not phosphoinositide 3-kinase activity
    • Elad-Sfadia, G., R. Haklai, ..., Y. Kloog. 2004. Galectin-3 augments K-Ras activation, and triggers a Ras signal that attenuates ERK but not phosphoinositide 3-kinase activity. J. Biol. Chem. 279: 34922-34930.
    • (2004) J. Biol. Chem. , vol.279 , pp. 34922-34930
    • Elad-Sfadia, G.1    Haklai, R.2    Kloog, Y.3
  • 16
    • 0028959434 scopus 로고
    • Cross-linking of galectin 3, a galactose-binding protein of mammalian cells, by tissue- Type transglutaminase
    • Mehul, B., S. Bawumia, and R. C. Hughes. 1995. Cross-linking of galectin 3, a galactose-binding protein of mammalian cells, by tissue- type transglutaminase. FEBS Lett. 360:160-164.
    • (1995) FEBS Lett. , vol.360 , pp. 160-164
    • Mehul, B.1    Bawumia, S.2    Hughes, R.C.3
  • 17
    • 1642483757 scopus 로고    scopus 로고
    • Galectin-3 precipi- Tates as a pentamer with synthetic multivalent carbohydrates and forms heterogeneous cross-linked complexes
    • Ahmad, N., H. J. Gabius, ..., C. F. Brewer. 2004. Galectin-3 precipi- tates as a pentamer with synthetic multivalent carbohydrates and forms heterogeneous cross-linked complexes. J. Biol. Chem. 279:10841-10847.
    • (2004) J. Biol. Chem. , vol.279 , pp. 10841-10847
    • Ahmad, N.1    Gabius, H.J.2    Brewer, C.F.3
  • 18
    • 36849040950 scopus 로고    scopus 로고
    • Lateral compartmen- Talization of T cell receptor versus CD45 by galectin-N-glycan binding and microfilaments coordinate basal and activation signaling
    • Chen, I. J., H. L. Chen, and M. Demetriou. 2007. Lateral compartmen- talization of T cell receptor versus CD45 by galectin-N-glycan binding and microfilaments coordinate basal and activation signaling. J. Biol. Chem. 282:35361-35372.
    • (2007) J. Biol. Chem. , vol.282 , pp. 35361-35372
    • Chen, I.J.1    Chen, H.L.2    Demetriou, M.3
  • 19
    • 35549010724 scopus 로고    scopus 로고
    • Plasma membrane domain organization regulates EGFR. signaling in tumor cells
    • Lajoie, P., E. A. Partridge, ..., I. R. Nabi. 2007. Plasma membrane domain organization regulates EGFR. signaling in tumor cells. J. Cell Biol. 179:341-356.
    • (2007) J. Cell Biol. , vol.179 , pp. 341-356
    • Lajoie, P.1    Partridge, E.A.2    Nabi, I.R.3
  • 20
    • 33847718338 scopus 로고    scopus 로고
    • Visualization of galectin-3 oligomerization on the surface of neutrophils and endothelial cells using fluorescence resonance energy transfer
    • Nieminen, J., A. Kuno, ..., S. Sato. 2007. Visualization of galectin-3 oligomerization on the surface of neutrophils and endothelial cells using fluorescence resonance energy transfer. J. Biol, Chem. 282:1374-1383.
    • (2007) J. Biol, Chem. , vol.282 , pp. 1374-1383
    • Nieminen, J.1    Kuno, A.2    Sato, S.3
  • 21
    • 34548333580 scopus 로고    scopus 로고
    • Modelling and simulation techniques for membrane biology
    • Burrage, K., J. Hancock, ..., D. V. Nicolau, Jr. 2007. Modelling and simulation techniques for membrane biology. Brief. Bioinform. 8:234-244.
    • (2007) Brief. Bioinform. , vol.8 , pp. 234-244
    • Burrage, K.1    Hancock, J.2    Nicolau Jr., D.V.3
  • 22
    • 2342469914 scopus 로고    scopus 로고
    • Stochastic model of protein-protein interaction: Why signaling proteins need to be colocalized
    • Batada, N. N., L. A. Shepp, and D. O. Siegmund. 2004. Stochastic model of protein-protein interaction: why signaling proteins need to be colocalized. Proc. Natl. Acad. Sci. USA. 101:6445-6449.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 6445-6449
    • Batada, N.N.1    Shepp, L.A.2    Siegmund, D.O.3
  • 23
    • 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, P. H., B. E. Snaar-Jagalska, ..., T. Schmidt. 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    Schmidt, T.3
  • 24
    • 33746725960 scopus 로고    scopus 로고
    • Single-molecule diffusion reveals similar mobility for the Lck, H-ras, and K-ras membrane anchors
    • Lommerse, P. H., K. Vastenhoud, ..., T. Schmidt. 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    Schmidt, T.3
  • 25
  • 26
    • 33645241165 scopus 로고    scopus 로고
    • Identifying optimal lipid raft characteristics required to promote nanoscale protein-protein interactions on the plasma membrane
    • Nicolau, Jr., D. V, ...., K. Burrage, J. F. Hancock. 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    Hancock, J.F.3
  • 27
    • 33947647996 scopus 로고    scopus 로고
    • Sources of anomalous diffusion on cell membranes: A Monte Carlo study
    • Nicolau, Jr., D. V., J. F. Hancock, and K. Burrage. 2007. Sources of anomalous diffusion on cell membranes: a Monte Carlo study. Biophys. J. 92:1975-1987.
    • (2007) Biophys. J. , vol.92 , pp. 1975-1987
    • Nicolau Jr., D.V.1    Hancock, J.F.2    Burrage, K.3
  • 28
    • 33747033205 scopus 로고    scopus 로고
    • Spatial modeling of dimerization reaction dynamics in the plasma membrane: Monte Carlo vs. continuum differential equations
    • Mayawala, K., D. G. Vlachos, and J. S. Edwards. 2006. Spatial modeling of dimerization reaction dynamics in the plasma membrane: Monte Carlo vs. continuum differential equations. Biophys. Chem. 121:194-208.
    • (2006) Biophys. Chem. , vol.121 , pp. 194-208
    • Mayawala, K.1    Vlachos, D.G.2    Edwards, J.S.3
  • 29
    • 28844467280 scopus 로고    scopus 로고
    • Nonequilibrium raftlike membrane domains under continuous recycling
    • Turner, M. S., P. Sens, and N. D. Socci. 2005. Nonequilibrium raftlike membrane domains under continuous recycling. Phys. Rev. Lett. 95:168301.
    • (2005) Phys. Rev. Lett. , vol.95 , pp. 168301
    • Turner, M.S.1    Sens, P.2    Socci, N.D.3
  • 30
    • 34250358345 scopus 로고    scopus 로고
    • Toward a mathematical model of the assembly and disassembly of membrane microdomains: Comparison with experimental models
    • Richardson, G., L. J. Cummings, ..., P. O'Shea. 2007. Toward a mathematical model of the assembly and disassembly of membrane microdomains: comparison with experimental models. Biophys. J. 92:4145-4156.
    • (2007) Biophys. J. , vol.92 , pp. 4145-4156
    • Richardson, G.1    Cummings, L.J.2    O'Shea, P.3
  • 31
    • 40149107726 scopus 로고    scopus 로고
    • A quantitative model for the all-or-none permeabilization of phospholipid vesicles by the antimicrobial peptide cecropin A
    • Gregory, S. M., A. Cavenaugh, ..., P. F. Almeida. 2008. A quantitative model for the all-or-none permeabilization of phospholipid vesicles by the antimicrobial peptide cecropin A. Biophys. J. 94:1667-1680.
    • (2008) Biophys. J. , vol.94 , pp. 1667-1680
    • Gregory, S.M.1    Cavenaugh, A.2    Almeida, P.F.3
  • 32
    • 0037182579 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., O. Gutman, ..., Y. I. Henis. 2002. Activated K-Ras and H-Ras display different interactions with saturable nonraft sites at the surface of live cells. J. Cell Biol. 157:865-872.
    • (2002) J. Cell Biol. , vol.157 , pp. 865-872
    • Niv, H.1    Gutman, O.2    Henis, Y.I.3
  • 33
    • 77957083058 scopus 로고
    • Structure and dynamics of membranes
    • R. Lipowsky and E. Sackmann, editors. Elsevier.
    • Almeida, P. F. F., and W. L. C. Vaz. 1995. Structure and dynamics of membranes. In From Cells to Vesicles. R. Lipowsky and E. Sackmann, editors. Elsevier. 305-357.
    • (1995) From Cells to Vesicles. , pp. 305-357
    • Almeida, P.F.F.1    Vaz, W.L.C.2
  • 35
    • 17844397967 scopus 로고    scopus 로고
    • CADLIVE dynamic simulator: Direct link of biochemical networks to dynamic models
    • Kurata, H., K, Masaki, ..., R. Iwasaki. 2005. CADLIVE dynamic simu- lator: direct link of biochemical networks to dynamic models. Genome Res. 15:590-600.
    • (2005) Genome Res. , vol.15 , pp. 590-600
    • Kurata, H.1    Masaki, K.2    Iwasaki, R.3
  • 36
    • 0037072757 scopus 로고    scopus 로고
    • Lateral sequestration of phosphatidylinositol 4,5-bisphosphate by the basic effector domain of myristoylated alanine-rich C kinase substrate is due to nonspecific electrostatic interactions
    • Wang, J., A. Gambhir, ..., S. McLaughlin. 2002. Lateral sequestration of phosphatidylinositol 4,5-bisphosphate by the basic effector domain of myristoylated alanine-rich C kinase substrate is due to nonspecific electrostatic interactions. J. Biol. Chem. 277:34401-34412.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34401-34412
    • Wang, J.1    Gambhir, A.2    McLaughlin, S.3
  • 37
    • 23844534708 scopus 로고    scopus 로고
    • Galectin-3 regu- Lates a molecular switch from N-Ras to K-Ras usage in human, breast carcinoma cells
    • Shalom-Feuerstein, R., T. Cooks, ..., Y. Kloog. 2005. Galectin-3 regu- lates a molecular switch from N-Ras to K-Ras usage in human, breast carcinoma cells. Cancer Res. 65:7292-7300.
    • (2005) Cancer Res. , vol.65 , pp. 7292-7300
    • Shalom-Feuerstein, R.1    Cooks, T.2    Kloog, Y.3
  • 39
    • 1342306818 scopus 로고    scopus 로고
    • Nanoscale organization of multiple GPI-anchored proteins in living cell membranes
    • Sharma, P., R. Varma, ..., S. Mayor. 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    Mayor, S.3
  • 40
    • 33745801153 scopus 로고    scopus 로고
    • Lipid rafts: Contentious only from simplistic stand-points
    • Hancock, J. F. 2006. Lipid rafts: contentious only from simplistic stand- points. Nat. Rev. Mol. Cell Biol. 7:456-462.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 456-462
    • Hancock, J.F.1


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