메뉴 건너뛰기




Volumn 1853, Issue 4, 2015, Pages 841-849

Ras nanoclusters: Versatile lipid-based signaling platforms

Author keywords

Cholesterol; Lateral segregation; Nanoclusters; Phosphatidylserine; Ras proteins; Spatial cross talk

Indexed keywords

CHOLESTEROL; DIMER; FENDILINE; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; K RAS PROTEIN; LIPID; MONOMER; NONSTEROID ANTIINFLAMMATORY AGENT; RAS PROTEIN; STAUROSPORINE; NANOPARTICLE; PHOSPHATIDYLSERINE;

EID: 84923141003     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2014.09.008     Document Type: Review
Times cited : (181)

References (74)
  • 1
    • 0037542854 scopus 로고    scopus 로고
    • Ras proteins: different signals from different locations
    • Hancock J.F. Ras proteins: different signals from different locations. Nat. Rev. Mol. Cell Biol. 2003, 4:373-384.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 373-384
    • Hancock, J.F.1
  • 2
    • 33644864788 scopus 로고    scopus 로고
    • Compartmentalized Ras/MAPK signaling
    • Mor A., Philips M.R. Compartmentalized Ras/MAPK signaling. Annu. Rev. Immunol. 2006, 24:771-800.
    • (2006) Annu. Rev. Immunol. , vol.24 , pp. 771-800
    • Mor, A.1    Philips, M.R.2
  • 3
    • 0037264633 scopus 로고    scopus 로고
    • Targeting RAS signalling pathways in cancer therapy
    • Downward J. Targeting RAS signalling pathways in cancer therapy. Nat. Rev. Cancer 2003, 3:11-22.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 11-22
    • Downward, J.1
  • 4
    • 84861147473 scopus 로고    scopus 로고
    • A comprehensive survey of Ras mutations in cancer
    • Prior I.A., Lewis P.D., Mattos C. A comprehensive survey of Ras mutations in cancer. Cancer Res. 2012, 72:2457-2467.
    • (2012) Cancer Res. , vol.72 , pp. 2457-2467
    • Prior, I.A.1    Lewis, P.D.2    Mattos, C.3
  • 5
    • 84858796808 scopus 로고    scopus 로고
    • Ras trafficking, localization and compartmentalized signalling
    • Prior I.A., Hancock J.F. Ras trafficking, localization and compartmentalized signalling. Semin. Cell Dev. Biol. 2012, 23:145-153.
    • (2012) Semin. Cell Dev. Biol. , vol.23 , pp. 145-153
    • Prior, I.A.1    Hancock, J.F.2
  • 6
    • 0034998678 scopus 로고    scopus 로고
    • Compartmentalization of Ras proteins
    • Prior I.A., Hancock J.F. Compartmentalization of Ras proteins. J. Cell Sci. 2001, 114:1603-1608.
    • (2001) J. Cell Sci. , vol.114 , pp. 1603-1608
    • Prior, I.A.1    Hancock, J.F.2
  • 8
    • 0037455589 scopus 로고    scopus 로고
    • Direct visualization of Ras proteins in spatially distinct cell surface microdomains
    • Prior I.A., Muncke C., Parton R.G., Hancock J.F. Direct visualization of Ras proteins in spatially distinct cell surface microdomains. J. Cell Biol. 2003, 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
  • 9
    • 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 S.J., Muncke C., Parton R.G., Hancock J.F. H-ras, K-ras, and inner plasma membrane raft proteins operate in nanoclusters with differential dependence on the actin cytoskeleton. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:15500-15505.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 15500-15505
    • Plowman, S.J.1    Muncke, C.2    Parton, R.G.3    Hancock, J.F.4
  • 10
  • 11
    • 75749150934 scopus 로고    scopus 로고
    • Ras membrane orientation and nanodomain localization generate isoform diversity
    • Abankwa D., Gorfe A.A., Inder K., Hancock J.F. Ras membrane orientation and nanodomain localization generate isoform diversity. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:1130-1135.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 1130-1135
    • Abankwa, D.1    Gorfe, A.A.2    Inder, K.3    Hancock, J.F.4
  • 15
    • 77955213426 scopus 로고    scopus 로고
    • Mathematical modeling of K-Ras nanocluster formation on the plasma membrane
    • Tian T., Plowman S.J., Parton R.G., Kloog Y., Hancock J.F. Mathematical modeling of K-Ras nanocluster formation on the plasma membrane. Biophys. J. 2010, 99:534-543.
    • (2010) Biophys. J. , vol.99 , pp. 534-543
    • Tian, T.1    Plowman, S.J.2    Parton, R.G.3    Kloog, Y.4    Hancock, J.F.5
  • 16
    • 84861438588 scopus 로고    scopus 로고
    • Organization, dynamics, and segregation of Ras nanoclusters in membrane domains
    • Janosi L., Li Z., Hancock J.F., Gorfe A.A. Organization, dynamics, and segregation of Ras nanoclusters in membrane domains. Proc. Natl. Acad. Sci. U. S. A. 2012, 109:8097-8102.
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 8097-8102
    • Janosi, L.1    Li, Z.2    Hancock, J.F.3    Gorfe, A.A.4
  • 20
    • 29144528806 scopus 로고    scopus 로고
    • Ras signaling from plasma membrane and endomembrane microdomains
    • Plowman S.J., Hancock J.F. Ras signaling from plasma membrane and endomembrane microdomains. Biochim. Biophys. Acta 2005, 1746:274-283.
    • (2005) Biochim. Biophys. Acta , vol.1746 , pp. 274-283
    • Plowman, S.J.1    Hancock, J.F.2
  • 21
    • 46149107301 scopus 로고    scopus 로고
    • Electrostatic interactions positively regulate K-Ras nanocluster formation and function
    • Plowman S.J., Ariotti N., Goodall A., Parton R.G., Hancock J.F. Electrostatic interactions positively regulate K-Ras nanocluster formation and function. Mol. Cell. Biol. 2008, 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
  • 22
    • 35048822834 scopus 로고    scopus 로고
    • H-ras protein in a bilayer: interaction and structure perturbation
    • Gorfe A.A., Babakhani A., McCammon J.A. H-ras protein in a bilayer: interaction and structure perturbation. J. Am. Chem. Soc. 2007, 129:12280-12286.
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 12280-12286
    • Gorfe, A.A.1    Babakhani, A.2    McCammon, J.A.3
  • 24
    • 48449092211 scopus 로고    scopus 로고
    • Using plasma membrane nanoclusters to build better signaling circuits
    • Harding A.S., Hancock J.F. Using plasma membrane nanoclusters to build better signaling circuits. Trends Cell Biol. 2008, 18:364-371.
    • (2008) Trends Cell Biol. , vol.18 , pp. 364-371
    • Harding, A.S.1    Hancock, J.F.2
  • 27
    • 0025013547 scopus 로고
    • A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane
    • Hancock J.F., Paterson H., Marshall C.J. A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane. Cell 1990, 63:133-139.
    • (1990) Cell , vol.63 , pp. 133-139
    • Hancock, J.F.1    Paterson, H.2    Marshall, C.J.3
  • 28
    • 0024406286 scopus 로고
    • All ras proteins are polyisoprenylated but only some are palmitoylated
    • Hancock J.F., Magee A.I., Childs J.E., Marshall C.J. All ras proteins are polyisoprenylated but only some are palmitoylated. Cell 1989, 57:1167-1177.
    • (1989) Cell , vol.57 , pp. 1167-1177
    • Hancock, J.F.1    Magee, A.I.2    Childs, J.E.3    Marshall, C.J.4
  • 29
    • 0026037624 scopus 로고
    • A CAAX or a CAAL motif and a second signal are sufficient for plasma membrane targeting of ras proteins
    • Hancock J.F., Cadwallader K., Paterson H., Marshall C.J. A CAAX or a CAAL motif and a second signal are sufficient for plasma membrane targeting of ras proteins. EMBO J. 1991, 10:4033-4039.
    • (1991) EMBO J. , vol.10 , pp. 4033-4039
    • Hancock, J.F.1    Cadwallader, K.2    Paterson, H.3    Marshall, C.J.4
  • 30
    • 78649821287 scopus 로고    scopus 로고
    • Segregation of negatively charged phospholipids by the polycationic and farnesylated membrane anchor of Kras
    • Janosi L., Gorfe A.A. Segregation of negatively charged phospholipids by the polycationic and farnesylated membrane anchor of Kras. Biophys. J. 2010, 99:3666-3674.
    • (2010) Biophys. J. , vol.99 , pp. 3666-3674
    • Janosi, L.1    Gorfe, A.A.2
  • 31
    • 0344585437 scopus 로고    scopus 로고
    • Lipid rafts: elusive or illusive?
    • Munro S. Lipid rafts: elusive or illusive?. Cell 2003, 115:377-388.
    • (2003) Cell , vol.115 , pp. 377-388
    • Munro, S.1
  • 32
    • 33745801153 scopus 로고    scopus 로고
    • Lipid rafts: contentious only from simplistic standpoints
    • Hancock J.F. Lipid rafts: contentious only from simplistic standpoints. Nat. Rev. Mol. Cell Biol. 2006, 7:456-462.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 456-462
    • Hancock, J.F.1
  • 33
    • 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
    • Gorfe A.A., Hanzal-Bayer M., Abankwa D., Hancock J.F., McCammon J.A. Structure and dynamics of the full-length lipid-modified H-Ras protein in a 1,2-dimyristoylglycero-3-phosphocholine bilayer. J. Med. Chem. 2007, 50:674-684.
    • (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
  • 35
    • 50849107378 scopus 로고    scopus 로고
    • Mechanisms of Ras membrane organization and signalling: Ras on a rocker
    • Abankwa D., Gorfe A.A., Hancock J.F. Mechanisms of Ras membrane organization and signalling: Ras on a rocker. Cell Cycle 2008, 7:2667-2673.
    • (2008) Cell Cycle , vol.7 , pp. 2667-2673
    • Abankwa, D.1    Gorfe, A.A.2    Hancock, J.F.3
  • 36
    • 84898063580 scopus 로고    scopus 로고
    • The efficacy of Raf kinase recruitment to the GTPase H-ras depends on H-ras membrane conformer-specific nanoclustering
    • Guzman C., Solman M., Ligabue A., Blazevits O., Andrade D.M., Reymond L., Eggeling C., Abankwa D. The efficacy of Raf kinase recruitment to the GTPase H-ras depends on H-ras membrane conformer-specific nanoclustering. J. Biol. Chem. 2014, 289:9519-9533.
    • (2014) J. Biol. Chem. , vol.289 , pp. 9519-9533
    • Guzman, C.1    Solman, M.2    Ligabue, A.3    Blazevits, O.4    Andrade, D.M.5    Reymond, L.6    Eggeling, C.7    Abankwa, D.8
  • 37
    • 84867572593 scopus 로고    scopus 로고
    • The role of G-domain orientation and nucleotide state on the Ras isoform-specific membrane interaction
    • Kapoor S., Weise K., Erlkamp M., Triola G., Waldmann H., Winter R. The role of G-domain orientation and nucleotide state on the Ras isoform-specific membrane interaction. Eur. Biophys. J. 2012, 41:801-813.
    • (2012) Eur. Biophys. J. , vol.41 , pp. 801-813
    • Kapoor, S.1    Weise, K.2    Erlkamp, M.3    Triola, G.4    Waldmann, H.5    Winter, R.6
  • 40
    • 58149279827 scopus 로고    scopus 로고
    • Activation of the MAPK module from different spatial locations generates distinct system outputs
    • Inder K., Harding A., Plowman S.J., Philips M.R., Parton R.G., Hancock J.F. Activation of the MAPK module from different spatial locations generates distinct system outputs. Mol. Biol. Cell 2008, 19:4776-4784.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4776-4784
    • Inder, K.1    Harding, A.2    Plowman, S.J.3    Philips, M.R.4    Parton, R.G.5    Hancock, J.F.6
  • 41
  • 42
    • 0028272507 scopus 로고
    • Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane
    • Leevers S.J., Paterson H.F., Marshall C.J. Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane. Nature 1994, 369:411-414.
    • (1994) Nature , vol.369 , pp. 411-414
    • Leevers, S.J.1    Paterson, H.F.2    Marshall, C.J.3
  • 43
    • 12244270658 scopus 로고    scopus 로고
    • Organization in lipid membranes containing cholesterol
    • Veatch S.L., Keller S.L. Organization in lipid membranes containing cholesterol. Phys. Rev. Lett. 2002, 89:268101.
    • (2002) Phys. Rev. Lett. , vol.89 , pp. 268101
    • Veatch, S.L.1    Keller, S.L.2
  • 44
    • 0242385346 scopus 로고    scopus 로고
    • Separation of liquid phases in giant vesicles of ternary mixtures of phospholipids and cholesterol
    • Veatch S.L., Keller S.L. Separation of liquid phases in giant vesicles of ternary mixtures of phospholipids and cholesterol. Biophys. J. 2003, 85:3074-3083.
    • (2003) Biophys. J. , vol.85 , pp. 3074-3083
    • Veatch, S.L.1    Keller, S.L.2
  • 46
    • 77957167810 scopus 로고    scopus 로고
    • Revitalizing membrane rafts: new tools and insights
    • Simons K., Gerl M.J. Revitalizing membrane rafts: new tools and insights. Nat. Rev. Mol. Cell Biol. 2010, 11:688-699.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 688-699
    • Simons, K.1    Gerl, M.J.2
  • 47
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K., Ikonen E. Functional rafts in cell membranes. Nature 1997, 387:569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 50
    • 84860857782 scopus 로고    scopus 로고
    • Nonsteroidal anti-inflammatory drugs alter the spatiotemporal organization of Ras proteins on the plasma membrane
    • Zhou Y., Cho K.J., Plowman S.J., Hancock J.F. Nonsteroidal anti-inflammatory drugs alter the spatiotemporal organization of Ras proteins on the plasma membrane. J. Biol. Chem. 2012, 287:16586-16595.
    • (2012) J. Biol. Chem. , vol.287 , pp. 16586-16595
    • Zhou, Y.1    Cho, K.J.2    Plowman, S.J.3    Hancock, J.F.4
  • 52
    • 78751545856 scopus 로고    scopus 로고
    • The MARCKS protein plays a critical role in phosphatidylinositol 4,5-bisphosphate metabolism and directed cell movement in vascular endothelial cells
    • Kalwa H., Michel T. The MARCKS protein plays a critical role in phosphatidylinositol 4,5-bisphosphate metabolism and directed cell movement in vascular endothelial cells. J. Biol. Chem. 2011, 286:2320-2330.
    • (2011) J. Biol. Chem. , vol.286 , pp. 2320-2330
    • Kalwa, H.1    Michel, T.2
  • 53
    • 84861325378 scopus 로고    scopus 로고
    • The lipid raft-associated protein CD98 is required for vaccinia virus endocytosis
    • Schroeder N., Chung C.S., Chen C.H., Liao C.L., Chang W. The lipid raft-associated protein CD98 is required for vaccinia virus endocytosis. J. Virol. 2012, 86:4868-4882.
    • (2012) J. Virol. , vol.86 , pp. 4868-4882
    • Schroeder, N.1    Chung, C.S.2    Chen, C.H.3    Liao, C.L.4    Chang, W.5
  • 55
    • 0029935339 scopus 로고    scopus 로고
    • Raf-1 kinase possesses distinct binding domains for phosphatidylserine and phosphatidic acid. Phosphatidic acid regulates the translocation of Raf-1 in 12-O-tetradecanoylphorbol-13-acetate-stimulated Madin-Darby canine kidney cells
    • Ghosh S., Strum J.C., Sciorra V.A., Daniel L., Bell R.M. Raf-1 kinase possesses distinct binding domains for phosphatidylserine and phosphatidic acid. Phosphatidic acid regulates the translocation of Raf-1 in 12-O-tetradecanoylphorbol-13-acetate-stimulated Madin-Darby canine kidney cells. J. Biol. Chem. 1996, 271:8472-8480.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8472-8480
    • Ghosh, S.1    Strum, J.C.2    Sciorra, V.A.3    Daniel, L.4    Bell, R.M.5
  • 56
    • 38149094836 scopus 로고    scopus 로고
    • Membrane phosphatidylserine regulates surface charge and protein localization
    • Yeung T., Gilbert G.E., Shi J., Silvius J., Kapus A., Grinstein S. Membrane phosphatidylserine regulates surface charge and protein localization. Science 2008, 319:210-213.
    • (2008) Science , vol.319 , pp. 210-213
    • Yeung, T.1    Gilbert, G.E.2    Shi, J.3    Silvius, J.4    Kapus, A.5    Grinstein, S.6
  • 61
    • 84872959202 scopus 로고    scopus 로고
    • Caveolae as plasma membrane sensors, protectors and organizers
    • Parton R.G., del Pozo M.A. Caveolae as plasma membrane sensors, protectors and organizers. Nat. Rev. Mol. Cell Biol. 2013, 14:98-112.
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 98-112
    • Parton, R.G.1    del Pozo, M.A.2
  • 62
    • 0037435608 scopus 로고    scopus 로고
    • Caveolin scaffolding region and the membrane binding region of SRC form lateral membrane domains
    • Wanaski S.P., Ng B.K., Glaser M. Caveolin scaffolding region and the membrane binding region of SRC form lateral membrane domains. Biochemistry 2003, 42:42-56.
    • (2003) Biochemistry , vol.42 , pp. 42-56
    • Wanaski, S.P.1    Ng, B.K.2    Glaser, M.3
  • 66
    • 67650072744 scopus 로고    scopus 로고
    • SDPR induces membrane curvature and functions in the formation of caveolae
    • Hansen C.G., Bright N.A., Howard G., Nichols B.J. SDPR induces membrane curvature and functions in the formation of caveolae. Nat. Cell Biol. 2009, 11:807-814.
    • (2009) Nat. Cell Biol. , vol.11 , pp. 807-814
    • Hansen, C.G.1    Bright, N.A.2    Howard, G.3    Nichols, B.J.4
  • 67
    • 37649017003 scopus 로고    scopus 로고
    • PTRF triggers a cave in
    • Chadda R., Mayor S. PTRF triggers a cave in. Cell 2008, 132:23-24.
    • (2008) Cell , vol.132 , pp. 23-24
    • Chadda, R.1    Mayor, S.2
  • 69
    • 84864025624 scopus 로고    scopus 로고
    • Structure-based reassessment of the caveolin signaling model: do caveolae regulate signaling through caveolin-protein interactions?
    • Collins B.M., Davis M.J., Hancock J.F., Parton R.G. Structure-based reassessment of the caveolin signaling model: do caveolae regulate signaling through caveolin-protein interactions?. Dev. Cell 2012, 23:11-20.
    • (2012) Dev. Cell , vol.23 , pp. 11-20
    • Collins, B.M.1    Davis, M.J.2    Hancock, J.F.3    Parton, R.G.4
  • 70
    • 8444221934 scopus 로고    scopus 로고
    • Localized Ras signaling at the leading edge regulates PI3K, cell polarity, and directional cell movement
    • Sasaki A.T., Chun C., Takeda K., Firtel R.A. Localized Ras signaling at the leading edge regulates PI3K, cell polarity, and directional cell movement. J. Cell Biol. 2004, 167:505-518.
    • (2004) J. Cell Biol. , vol.167 , pp. 505-518
    • Sasaki, A.T.1    Chun, C.2    Takeda, K.3    Firtel, R.A.4
  • 71
    • 33745607882 scopus 로고    scopus 로고
    • Feedback signaling controls leading-edge formation during chemotaxis
    • Charest P.G., Firtel R.A. Feedback signaling controls leading-edge formation during chemotaxis. Curr. Opin. Genet. Dev. 2006, 16:339-347.
    • (2006) Curr. Opin. Genet. Dev. , vol.16 , pp. 339-347
    • Charest, P.G.1    Firtel, R.A.2
  • 72
    • 77952920346 scopus 로고    scopus 로고
    • A Ras signaling complex controls the RasC-TORC2 pathway and directed cell migration
    • Charest P.G., Shen Z., Lakoduk A., Sasaki A.T., Briggs S.P., Firtel R.A. A Ras signaling complex controls the RasC-TORC2 pathway and directed cell migration. Dev. Cell 2010, 18:737-749.
    • (2010) Dev. Cell , vol.18 , pp. 737-749
    • Charest, P.G.1    Shen, Z.2    Lakoduk, A.3    Sasaki, A.T.4    Briggs, S.P.5    Firtel, R.A.6
  • 73
    • 78049410557 scopus 로고    scopus 로고
    • The anti-inflammatory drug indomethacin alters nanoclustering in synthetic and cell plasma membranes
    • Zhou Y., Plowman S.J., Lichtenberger L.M., Hancock J.F. The anti-inflammatory drug indomethacin alters nanoclustering in synthetic and cell plasma membranes. J. Biol. Chem. 2010, 285:35188-35195.
    • (2010) J. Biol. Chem. , vol.285 , pp. 35188-35195
    • Zhou, Y.1    Plowman, S.J.2    Lichtenberger, L.M.3    Hancock, J.F.4
  • 74
    • 77952472956 scopus 로고    scopus 로고
    • The nonsteroidal anti-inflammatory drug indomethacin induces heterogeneity in lipid membranes: potential implication for its diverse biological action
    • Zhou Y., Hancock J.F., Lichtenberger L.M. The nonsteroidal anti-inflammatory drug indomethacin induces heterogeneity in lipid membranes: potential implication for its diverse biological action. PLoS One 2010, 5:e8811.
    • (2010) PLoS One , vol.5 , pp. e8811
    • Zhou, Y.1    Hancock, J.F.2    Lichtenberger, L.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.