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Volumn 21, Issue 4, 2010, Pages 381-390

A unifying mechanism accounts for sensing of membrane curvature by BAR domains, amphipathic helices and membrane-anchored proteins

Author keywords

Amphipathic helix; BAR domains; Lipid packing defects; Membrane curvature sensing; Protein sorting

Indexed keywords

AMPHIPHYSIN; BIN AMPHIPHYSIN RVS167; LIPOSOME; UNCLASSIFIED DRUG;

EID: 77950596030     PISSN: 10849521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.semcdb.2009.12.004     Document Type: Review
Times cited : (87)

References (77)
  • 1
    • 33847199803 scopus 로고    scopus 로고
    • Sheets, ribbons and tubules-how organelles get their shape
    • Voeltz G.K., and Prinz W.A. Sheets, ribbons and tubules-how organelles get their shape. Nature Reviews Molecular Cell Biology 8 (2007) 258-264
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , pp. 258-264
    • Voeltz, G.K.1    Prinz, W.A.2
  • 4
    • 45849152550 scopus 로고    scopus 로고
    • Mechanisms of membrane fusion: disparate players and common principles
    • Martens S., and McMahon H.T. Mechanisms of membrane fusion: disparate players and common principles. Nature Reviews Molecular Cell Biology 9 (2008) 543-556
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , pp. 543-556
    • Martens, S.1    McMahon, H.T.2
  • 6
    • 28444476999 scopus 로고    scopus 로고
    • Membrane curvature and mechanisms of dynamic cell membrane remodelling
    • McMahon H.T., and Gallop J.L. Membrane curvature and mechanisms of dynamic cell membrane remodelling. Nature 438 (2005) 590-596
    • (2005) Nature , vol.438 , pp. 590-596
    • McMahon, H.T.1    Gallop, J.L.2
  • 8
    • 33745737926 scopus 로고    scopus 로고
    • Membrane deformation by protein coats
    • Antonny B. Membrane deformation by protein coats. Current Opinion in Cell Biology 18 (2006) 386-394
    • (2006) Current Opinion in Cell Biology , vol.18 , pp. 386-394
    • Antonny, B.1
  • 9
    • 46449135255 scopus 로고    scopus 로고
    • The hydrophobic insertion mechanism of membrane curvature generation by proteins
    • Campelo F., McMahon H.T., and Kozlov M.M. The hydrophobic insertion mechanism of membrane curvature generation by proteins. Biophysical Journal 95 (2008) 2325-2339
    • (2008) Biophysical Journal , vol.95 , pp. 2325-2339
    • Campelo, F.1    McMahon, H.T.2    Kozlov, M.M.3
  • 10
    • 0038290760 scopus 로고    scopus 로고
    • Protein-lipid interplay in fusion and fission of biological membranes
    • Chernomordik L.V., and Kozlov M.M. Protein-lipid interplay in fusion and fission of biological membranes. Annual Review of Biochemistry 72 (2003) 175-207
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 175-207
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 12
    • 40049086567 scopus 로고    scopus 로고
    • Structural basis of membrane invagination by F-BAR domains
    • Frost A., Perera R., Roux A., Spasov K., Destaing O., Egelman E., et al. Structural basis of membrane invagination by F-BAR domains. Cell 132 (2008) 807
    • (2008) Cell , vol.132 , pp. 807
    • Frost, A.1    Perera, R.2    Roux, A.3    Spasov, K.4    Destaing, O.5    Egelman, E.6
  • 14
    • 34249933061 scopus 로고    scopus 로고
    • How synaptotagmin promotes membrane fusion
    • Martens S., Kozlov M.M., and McMahon H.T. How synaptotagmin promotes membrane fusion. Science 316 (2007) 1205-1208
    • (2007) Science , vol.316 , pp. 1205-1208
    • Martens, S.1    Kozlov, M.M.2    McMahon, H.T.3
  • 15
    • 69949183624 scopus 로고    scopus 로고
    • Conserved functions of membrane active GTPases in coated vesicle formation
    • Pucadyil T.J., and Schmid S.L. Conserved functions of membrane active GTPases in coated vesicle formation. Science 325 (2009) 1217-1220
    • (2009) Science , vol.325 , pp. 1217-1220
    • Pucadyil, T.J.1    Schmid, S.L.2
  • 17
    • 34249316521 scopus 로고    scopus 로고
    • Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis
    • Shimada A., Niwa H., Tsujita K., Suetsugu S., Nitta K., Hanawa-Suetsugu K., et al. Curved EFC/F-BAR-domain dimers are joined end to end into a filament for membrane invagination in endocytosis. Cell 129 (2007) 761-772
    • (2007) Cell , vol.129 , pp. 761-772
    • Shimada, A.1    Niwa, H.2    Tsujita, K.3    Suetsugu, S.4    Nitta, K.5    Hanawa-Suetsugu, K.6
  • 18
    • 0033130119 scopus 로고    scopus 로고
    • Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis
    • Takei K., Slepnev V.I., Haucke V., and De Camilli P. Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis. Nature Cell Biology 1 (1999) 33-39
    • (1999) Nature Cell Biology , vol.1 , pp. 33-39
    • Takei, K.1    Slepnev, V.I.2    Haucke, V.3    De Camilli, P.4
  • 19
    • 33845350971 scopus 로고    scopus 로고
    • Amphipathic helices as mediators of the membrane interaction of amphitropic proteins, and as modulators of bilayer physical properties
    • Cornell R.B., and Taneva S.G. Amphipathic helices as mediators of the membrane interaction of amphitropic proteins, and as modulators of bilayer physical properties. Current Protein & Peptide Science 7 (2006) 539-552
    • (2006) Current Protein & Peptide Science , vol.7 , pp. 539-552
    • Cornell, R.B.1    Taneva, S.G.2
  • 20
    • 77951896130 scopus 로고    scopus 로고
    • Amphipathic helices and membrane curvature
    • doi:10.1016/j.febslet.2009.10.022
    • Drin G., and Antonny B. Amphipathic helices and membrane curvature. FEBS Letters (2009) doi:10.1016/j.febslet.2009.10.022
    • (2009) FEBS Letters
    • Drin, G.1    Antonny, B.2
  • 21
    • 33748288113 scopus 로고    scopus 로고
    • BAR, F-BAR (EFC) and ENTH/ANTH domains in the regulation of membrane-cytosol interfaces and membrane curvature
    • Itoh T., and De Camilli P. BAR, F-BAR (EFC) and ENTH/ANTH domains in the regulation of membrane-cytosol interfaces and membrane curvature. Biochimica et Biophysica Acta-Molecular and Cell Biology of Lipids 1761 (2006) 897-912
    • (2006) Biochimica et Biophysica Acta-Molecular and Cell Biology of Lipids , vol.1761 , pp. 897-912
    • Itoh, T.1    De Camilli, P.2
  • 22
    • 1442317538 scopus 로고    scopus 로고
    • BAR domains as sensors of membrane curvature: the amphiphysin BAR structure
    • Peter B.J., Kent H.M., Mills I.G., Vallis Y., Butler P.J.G., Evans P.R., et al. BAR domains as sensors of membrane curvature: the amphiphysin BAR structure. Science 303 (2004) 495-499
    • (2004) Science , vol.303 , pp. 495-499
    • Peter, B.J.1    Kent, H.M.2    Mills, I.G.3    Vallis, Y.4    Butler, P.J.G.5    Evans, P.R.6
  • 23
    • 38549092474 scopus 로고    scopus 로고
    • Membrane recognition by phospholipid-binding domains
    • Lemmon M.A. Membrane recognition by phospholipid-binding domains. Nature Reviews Molecular Cell Biology 9 (2008) 99-111
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , pp. 99-111
    • Lemmon, M.A.1
  • 24
    • 33750266831 scopus 로고    scopus 로고
    • Trafficking and signaling by fatty-acylated and prenylated proteins
    • Resh M.D. Trafficking and signaling by fatty-acylated and prenylated proteins. Nature Chemical Biology 2 (2006) 584-590
    • (2006) Nature Chemical Biology , vol.2 , pp. 584-590
    • Resh, M.D.1
  • 25
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes
    • Davidson W.S., Jonas A., Clayton D.F., and George J.M. Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes. Journal of Biological Chemistry 273 (1998) 9443-9449
    • (1998) Journal of Biological Chemistry , vol.273 , pp. 9443-9449
    • Davidson, W.S.1    Jonas, A.2    Clayton, D.F.3    George, J.M.4
  • 27
    • 0346756190 scopus 로고    scopus 로고
    • Lipid packing sensed by ArfGAP1 couples COPI coat disassembly to membrane bilayer curvature
    • Bigay J., Gounon P., Robineau S., and Antonny B. Lipid packing sensed by ArfGAP1 couples COPI coat disassembly to membrane bilayer curvature. Nature 426 (2003) 563-566
    • (2003) Nature , vol.426 , pp. 563-566
    • Bigay, J.1    Gounon, P.2    Robineau, S.3    Antonny, B.4
  • 28
    • 6944255481 scopus 로고    scopus 로고
    • Sorting nexin-1 mediates tubular endosome-to-TGN transport through coincidence sensing of high-curvature membranes and 3-phosphoinositides
    • Carlton J., Bujny M., Peter B.J., Oorschot V.M.J., Rutherford A., Mellor H., et al. Sorting nexin-1 mediates tubular endosome-to-TGN transport through coincidence sensing of high-curvature membranes and 3-phosphoinositides. Current Biology 14 (2004) 1791-1800
    • (2004) Current Biology , vol.14 , pp. 1791-1800
    • Carlton, J.1    Bujny, M.2    Peter, B.J.3    Oorschot, V.M.J.4    Rutherford, A.5    Mellor, H.6
  • 31
    • 62149141206 scopus 로고    scopus 로고
    • Geometric cue for protein localization in a bacterium
    • Ramamurthi K.S., Lecuyer S., Stone H.A., and Losick R. Geometric cue for protein localization in a bacterium. Science 323 (2009) 1354-1357
    • (2009) Science , vol.323 , pp. 1354-1357
    • Ramamurthi, K.S.1    Lecuyer, S.2    Stone, H.A.3    Losick, R.4
  • 34
    • 0034681120 scopus 로고    scopus 로고
    • Interfacial control of lid opening in Thermomyces lanuginosa lipase
    • Cajal Y., Svendsen A., Girona V., Patkar S.A., and Alsina M.A. Interfacial control of lid opening in Thermomyces lanuginosa lipase. Biochemistry 39 (2000) 413-423
    • (2000) Biochemistry , vol.39 , pp. 413-423
    • Cajal, Y.1    Svendsen, A.2    Girona, V.3    Patkar, S.A.4    Alsina, M.A.5
  • 36
    • 0037340961 scopus 로고    scopus 로고
    • Nanotubules formed by highly hydrophobic amphiphilic alpha-helical peptides and natural phospholipids
    • Furuya T., Kiyota T., Lee S., Inoue T., Sugihara G., Logvinova A., et al. Nanotubules formed by highly hydrophobic amphiphilic alpha-helical peptides and natural phospholipids. Biophysical Journal 84 (2003) 1950-1959
    • (2003) Biophysical Journal , vol.84 , pp. 1950-1959
    • Furuya, T.1    Kiyota, T.2    Lee, S.3    Inoue, T.4    Sugihara, G.5    Logvinova, A.6
  • 37
    • 0242331729 scopus 로고    scopus 로고
    • Imaging coexisting fluid domains in biomembrane models coupling curvature and line tension
    • Baumgart T., Hess S.T., and Webb W.W. Imaging coexisting fluid domains in biomembrane models coupling curvature and line tension. Nature 425 (2003) 821-824
    • (2003) Nature , vol.425 , pp. 821-824
    • Baumgart, T.1    Hess, S.T.2    Webb, W.W.3
  • 38
    • 18444366155 scopus 로고    scopus 로고
    • Role of curvature and phase transition in lipid sorting and fission of membrane tubules
    • Roux A., Cuvelier D., Nassoy P., Prost J., Bassereau P., and Goud B. Role of curvature and phase transition in lipid sorting and fission of membrane tubules. EMBO Journal 24 (2005) 1537-1545
    • (2005) EMBO Journal , vol.24 , pp. 1537-1545
    • Roux, A.1    Cuvelier, D.2    Nassoy, P.3    Prost, J.4    Bassereau, P.5    Goud, B.6
  • 39
    • 0028930164 scopus 로고
    • Effect of cholesterol, fatty acyl-chain composition, and bilayer curvature on the interaction of cytochrome B(5) with liposomes of phosphatidylcholines
    • Taylor K.M.P., and Roseman M.A. Effect of cholesterol, fatty acyl-chain composition, and bilayer curvature on the interaction of cytochrome B(5) with liposomes of phosphatidylcholines. Biochemistry 34 (1995) 3841-3850
    • (1995) Biochemistry , vol.34 , pp. 3841-3850
    • Taylor, K.M.P.1    Roseman, M.A.2
  • 40
    • 0037007486 scopus 로고    scopus 로고
    • Thermodynamics of the coil-alpha-helix transition of amphipathic peptides in a membrane environment: the role of vesicle curvature
    • Wieprecht T., Beyermann M., and Seelig J. Thermodynamics of the coil-alpha-helix transition of amphipathic peptides in a membrane environment: the role of vesicle curvature. Biophysical Chemistry 96 (2002) 191-201
    • (2002) Biophysical Chemistry , vol.96 , pp. 191-201
    • Wieprecht, T.1    Beyermann, M.2    Seelig, J.3
  • 41
    • 0026808783 scopus 로고
    • Peptide binding to lipid bilayers-nonclassical hydrophobic effect and membrane-induced Pk shifts
    • Beschiaschvili G., and Seelig J. Peptide binding to lipid bilayers-nonclassical hydrophobic effect and membrane-induced Pk shifts. Biochemistry 31 (1992) 10044-10053
    • (1992) Biochemistry , vol.31 , pp. 10044-10053
    • Beschiaschvili, G.1    Seelig, J.2
  • 43
    • 22744442219 scopus 로고    scopus 로고
    • ArfGAP1 responds to membrane curvature through the folding of a lipid packing sensor motif
    • Bigay J., Casella J.F., Drin G., Mesmin B., and Antonny B. ArfGAP1 responds to membrane curvature through the folding of a lipid packing sensor motif. EMBO Journal 24 (2005) 2244-2253
    • (2005) EMBO Journal , vol.24 , pp. 2244-2253
    • Bigay, J.1    Casella, J.F.2    Drin, G.3    Mesmin, B.4    Antonny, B.5
  • 44
    • 33847075871 scopus 로고    scopus 로고
    • Two lipid-packing sensor motifs contribute to the sensitivity of ArfGAP1 to membrane curvature
    • Mesmin B., Drin G., Levi S., Rawet M., Cassel D., Bigay J., et al. Two lipid-packing sensor motifs contribute to the sensitivity of ArfGAP1 to membrane curvature. Biochemistry 46 (2007) 1779-1790
    • (2007) Biochemistry , vol.46 , pp. 1779-1790
    • Mesmin, B.1    Drin, G.2    Levi, S.3    Rawet, M.4    Cassel, D.5    Bigay, J.6
  • 45
    • 50949166660 scopus 로고    scopus 로고
    • A fluorescence-based technique to construct size distributions from single-object measurements: application to the extrusion of lipid vesicles
    • Kunding A.H., Mortensen M.W., Christensen S.M., and Stamou D. A fluorescence-based technique to construct size distributions from single-object measurements: application to the extrusion of lipid vesicles. Biophysical Journal 95 (2008) 1176-1188
    • (2008) Biophysical Journal , vol.95 , pp. 1176-1188
    • Kunding, A.H.1    Mortensen, M.W.2    Christensen, S.M.3    Stamou, D.4
  • 47
    • 66249127141 scopus 로고    scopus 로고
    • Sorting of lipids and proteins in membrane curvature gradients
    • Tian A., and Baumgart T. Sorting of lipids and proteins in membrane curvature gradients. Biophysical Journal 96 (2009) 2676-2688
    • (2009) Biophysical Journal , vol.96 , pp. 2676-2688
    • Tian, A.1    Baumgart, T.2
  • 48
    • 70350336902 scopus 로고    scopus 로고
    • Physiological membrane tension causes an increase in lipid diffusion: a single molecule fluorescence study
    • Muddana H.S., Gullapalli R.R., Tabouillot T., and Butler P. Physiological membrane tension causes an increase in lipid diffusion: a single molecule fluorescence study. Biophysical Journal 96 (2009) 197a-198a
    • (2009) Biophysical Journal , vol.96
    • Muddana, H.S.1    Gullapalli, R.R.2    Tabouillot, T.3    Butler, P.4
  • 49
    • 33745752076 scopus 로고    scopus 로고
    • Curvature-modulated phase separation in lipid bilayer membranes
    • Parthasarathy R., Yu C.H., and Groves J.T. Curvature-modulated phase separation in lipid bilayer membranes. Langmuir 22 (2006) 5095-5099
    • (2006) Langmuir , vol.22 , pp. 5095-5099
    • Parthasarathy, R.1    Yu, C.H.2    Groves, J.T.3
  • 50
    • 43149119500 scopus 로고    scopus 로고
    • Bending membranes on demand: fluid phospholipid bilayers on topographically deformable substrates
    • Sanii B., Smith A.M., Butti R., Brozell A.M., and Parikh A.N. Bending membranes on demand: fluid phospholipid bilayers on topographically deformable substrates. Nano Letters 8 (2008) 866-871
    • (2008) Nano Letters , vol.8 , pp. 866-871
    • Sanii, B.1    Smith, A.M.2    Butti, R.3    Brozell, A.M.4    Parikh, A.N.5
  • 53
    • 68149120533 scopus 로고    scopus 로고
    • Quantification of nano-scale intermembrane contact areas using fluorescence resonance energy transfer
    • Bendix P.M., Pedersen M.S., and Stamou D. Quantification of nano-scale intermembrane contact areas using fluorescence resonance energy transfer. PNAS 106 (2009) 12341-12346
    • (2009) PNAS , vol.106 , pp. 12341-12346
    • Bendix, P.M.1    Pedersen, M.S.2    Stamou, D.3
  • 54
    • 34447256592 scopus 로고    scopus 로고
    • Structure and analysis of FCHo2F-BAR domain: a dimerizing and membrane recruitment module that effects membrane curvature
    • Henne W.M., Kent H.M., Ford M.G.J., Hegde B.G., Daumke O., Butler P.J.G., et al. Structure and analysis of FCHo2F-BAR domain: a dimerizing and membrane recruitment module that effects membrane curvature. Structure 15 (2007) 839-852
    • (2007) Structure , vol.15 , pp. 839-852
    • Henne, W.M.1    Kent, H.M.2    Ford, M.G.J.3    Hegde, B.G.4    Daumke, O.5    Butler, P.J.G.6
  • 55
    • 30944435279 scopus 로고    scopus 로고
    • Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis
    • Tsujita K., Suetsugu S., Sasaki N., Furutani M., Oikawa T., and Takenawa T. Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis. Journal of Cell Biology 172 (2006) 269-279
    • (2006) Journal of Cell Biology , vol.172 , pp. 269-279
    • Tsujita, K.1    Suetsugu, S.2    Sasaki, N.3    Furutani, M.4    Oikawa, T.5    Takenawa, T.6
  • 56
    • 0035807063 scopus 로고    scopus 로고
    • Regulation of CTP: phosphocholine cytidylyltransferase activity by the physical properties of lipid membranes: an important role for stored curvature strain energy
    • Davies S.M.A., Epand R.M., Kraayenhof R., and Cornell R.B. Regulation of CTP: phosphocholine cytidylyltransferase activity by the physical properties of lipid membranes: an important role for stored curvature strain energy. Biochemistry 40 (2001) 10522-10531
    • (2001) Biochemistry , vol.40 , pp. 10522-10531
    • Davies, S.M.A.1    Epand, R.M.2    Kraayenhof, R.3    Cornell, R.B.4
  • 57
    • 0030692015 scopus 로고    scopus 로고
    • Activation of ADP-ribosylation factor 1 GTPase-activating protein by phosphatidylcholine-derived diacylglycerols
    • Antonny B., Huber I., Paris S., Chabre M., and Cassel D. Activation of ADP-ribosylation factor 1 GTPase-activating protein by phosphatidylcholine-derived diacylglycerols. Journal of Biological Chemistry 272 (1997) 30848-30851
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 30848-30851
    • Antonny, B.1    Huber, I.2    Paris, S.3    Chabre, M.4    Cassel, D.5
  • 58
    • 1842483252 scopus 로고    scopus 로고
    • Membrane curvature: how BAR domains bend bilayers
    • Zimmerberg J., and McLaughlin S. Membrane curvature: how BAR domains bend bilayers. Current Biology 14 (2004) R250-R252
    • (2004) Current Biology , vol.14
    • Zimmerberg, J.1    McLaughlin, S.2
  • 60
    • 13444291116 scopus 로고    scopus 로고
    • Structural basis of filopodia formation induced by the IRSp53/MIM homology domain of human IRSp53
    • Millard T.H., Bompard G., Heung M.Y., Dafforn T.R., Scott D.J., Machesky L.M., et al. Structural basis of filopodia formation induced by the IRSp53/MIM homology domain of human IRSp53. EMBO Journal 24 (2005) 240-250
    • (2005) EMBO Journal , vol.24 , pp. 240-250
    • Millard, T.H.1    Bompard, G.2    Heung, M.Y.3    Dafforn, T.R.4    Scott, D.J.5    Machesky, L.M.6
  • 61
    • 33745559393 scopus 로고    scopus 로고
    • Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms
    • Masuda M., Takeda S., Sone M., Ohki T., Mori H., Kamioka Y., et al. Endophilin BAR domain drives membrane curvature by two newly identified structure-based mechanisms. EMBO Journal 25 (2006) 2889-2897
    • (2006) EMBO Journal , vol.25 , pp. 2889-2897
    • Masuda, M.1    Takeda, S.2    Sone, M.3    Ohki, T.4    Mori, H.5    Kamioka, Y.6
  • 63
    • 0033935281 scopus 로고    scopus 로고
    • Binding of the antibacterial peptide magainin 2 amide to small and large unilamellar vesicles
    • Wieprecht T., Apostolov O., and Seelig J. Binding of the antibacterial peptide magainin 2 amide to small and large unilamellar vesicles. Biophysical Chemistry 85 (2000) 187-198
    • (2000) Biophysical Chemistry , vol.85 , pp. 187-198
    • Wieprecht, T.1    Apostolov, O.2    Seelig, J.3
  • 64
    • 2542461043 scopus 로고    scopus 로고
    • Alpha-synuclein has a high affinity for packing defects in a bilayer membrane-a thermodynamics study
    • Nuscher B., Kamp F., Mehnert T., Odoy S., Haass C., Kahle P.J., et al. Alpha-synuclein has a high affinity for packing defects in a bilayer membrane-a thermodynamics study. Journal of Biological Chemistry 279 (2004) 21966-21975
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 21966-21975
    • Nuscher, B.1    Kamp, F.2    Mehnert, T.3    Odoy, S.4    Haass, C.5    Kahle, P.J.6
  • 66
    • 38049052532 scopus 로고    scopus 로고
    • Real-time detection reveals that effectors couple dynamin's GTP-dependent conformational changes to the membrane
    • Ramachandran R., and Schmid S.L. Real-time detection reveals that effectors couple dynamin's GTP-dependent conformational changes to the membrane. EMBO Journal 27 (2008) 27-37
    • (2008) EMBO Journal , vol.27 , pp. 27-37
    • Ramachandran, R.1    Schmid, S.L.2
  • 68
    • 20144375061 scopus 로고    scopus 로고
    • An acylation cycle regulates localization and activity of palmitoylated Ras isoforms
    • Rocks O., Peyker A., Kahms M., Verveer P.J., Koerner C., Lumbierres M., et al. An acylation cycle regulates localization and activity of palmitoylated Ras isoforms. Science 307 (2005) 1746-1752
    • (2005) Science , vol.307 , pp. 1746-1752
    • Rocks, O.1    Peyker, A.2    Kahms, M.3    Verveer, P.J.4    Koerner, C.5    Lumbierres, M.6
  • 73
    • 69249135065 scopus 로고    scopus 로고
    • Tickets to ride: selecting cargo for clathrin-regulated internalization
    • Traub L.M. Tickets to ride: selecting cargo for clathrin-regulated internalization. Nature Reviews Molecular Cell Biology 10 (2009) 583-596
    • (2009) Nature Reviews Molecular Cell Biology , vol.10 , pp. 583-596
    • Traub, L.M.1
  • 74
    • 28444477387 scopus 로고    scopus 로고
    • Plasma membrane phosphoinositide organization by protein electrostatics
    • McLaughlin S., and Murray D. Plasma membrane phosphoinositide organization by protein electrostatics. Nature 438 (2005) 605-611
    • (2005) Nature , vol.438 , pp. 605-611
    • McLaughlin, S.1    Murray, D.2
  • 75
    • 38149094836 scopus 로고    scopus 로고
    • Membrane phosphatidylserine regulates surface charge and protein localization
    • Yeung T., Gilbert G.E., Shi J., Silvius J., Kapus A., and Grinstein S. Membrane phosphatidylserine regulates surface charge and protein localization. Science 319 (2008) 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.