메뉴 건너뛰기




Volumn 581, Issue 11, 2007, Pages 2098-2104

Lipid rafts and membrane traffic

Author keywords

Cholesterol facilitated; Liquid ordered; Membrane microstructure; Rafts

Indexed keywords

MEMBRANE LIPID;

EID: 34248195469     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.03.019     Document Type: Short Survey
Times cited : (267)

References (50)
  • 2
    • 0038557037 scopus 로고    scopus 로고
    • Lipids on the frontier: a century of cell-membrane bilayers
    • Edidin M. Lipids on the frontier: a century of cell-membrane bilayers. Nat. Rev. Mol. Cell. Biol. 4 (2003) 414-418
    • (2003) Nat. Rev. Mol. Cell. Biol. , vol.4 , pp. 414-418
    • Edidin, M.1
  • 4
    • 29144510046 scopus 로고    scopus 로고
    • How principles of domain formation in model membranes may explain ambiguities concerning lipid raft formation in cells
    • London E. How principles of domain formation in model membranes may explain ambiguities concerning lipid raft formation in cells. Biochim. Biophys. Acta 1746 (2005) 203-220
    • (2005) Biochim. Biophys. Acta , vol.1746 , pp. 203-220
    • London, E.1
  • 5
    • 33748577712 scopus 로고    scopus 로고
    • Lipid microdomains in model and biological membranes: how strong are the connections?
    • Silvius J.R. Lipid microdomains in model and biological membranes: how strong are the connections?. Q. Rev. Biophys. 38 (2006) 1-11
    • (2006) Q. Rev. Biophys. , vol.38 , pp. 1-11
    • Silvius, J.R.1
  • 7
    • 33745041479 scopus 로고    scopus 로고
    • Roles of bilayer material properties in function and distribution of membrane proteins
    • McIntosh T.J., and Simon S.A. Roles of bilayer material properties in function and distribution of membrane proteins. Annu. Rev. Biophys. Biomol. Struct. 35 (2006) 177-198
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 177-198
    • McIntosh, T.J.1    Simon, S.A.2
  • 8
    • 0344585437 scopus 로고    scopus 로고
    • Lipid rafts: elusive or illusive?
    • Munro S. Lipid rafts: elusive or illusive?. Cell 115 (2003) 377-388
    • (2003) Cell , vol.115 , pp. 377-388
    • Munro, S.1
  • 9
    • 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. 7 (2006) 456-462
    • (2006) Nat. Rev. Mol. Cell. Biol. , vol.7 , pp. 456-462
    • Hancock, J.F.1
  • 10
    • 33750130964 scopus 로고    scopus 로고
    • Lipid rafts: now you see them, now you don't
    • Shaw A.S. Lipid rafts: now you see them, now you don't. Nat. Immunol. 7 (2006) 1139-1142
    • (2006) Nat. Immunol. , vol.7 , pp. 1139-1142
    • Shaw, A.S.1
  • 11
    • 33845901815 scopus 로고    scopus 로고
    • Lipid rafts: at a crossroad between cell biology and physics
    • Jacobson K., Mouritsen O.G., and Anderson R.G.W. Lipid rafts: at a crossroad between cell biology and physics. Nat. Cell Biol. 9 (2007) 7-14
    • (2007) Nat. Cell Biol. , vol.9 , pp. 7-14
    • Jacobson, K.1    Mouritsen, O.G.2    Anderson, R.G.W.3
  • 12
    • 33645241165 scopus 로고    scopus 로고
    • Identifying optimal lipid raft characteristics required to promote nanoscale protein-protein interactions on the plasma membrane
    • Nicolau D.V., Burrage K., Parton R.G., and Hancock J.F. Identifying optimal lipid raft characteristics required to promote nanoscale protein-protein interactions on the plasma membrane. Mol. Cell. Biol. 26 (2006) 313-323
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 313-323
    • Nicolau, D.V.1    Burrage, K.2    Parton, R.G.3    Hancock, J.F.4
  • 13
    • 28844467280 scopus 로고    scopus 로고
    • Nonequilibrium raftlike membrane domains under continuous recycling
    • Turner M.S., Sens P., and Socci N.D. Nonequilibrium raftlike membrane domains under continuous recycling. Phys. Rev. Lett. 95 (2005) 168301
    • (2005) Phys. Rev. Lett. , vol.95 , pp. 168301
    • Turner, M.S.1    Sens, P.2    Socci, N.D.3
  • 14
    • 29144483525 scopus 로고    scopus 로고
    • Towards understanding the dynamics of membrane-raft-based molecular interactions
    • Kusumi A., and Suzuki K. Towards understanding the dynamics of membrane-raft-based molecular interactions. Biochim. Biophys. Acta 1746 (2005) 234-251
    • (2005) Biochim. Biophys. Acta , vol.1746 , pp. 234-251
    • Kusumi, A.1    Suzuki, K.2
  • 15
    • 22744437388 scopus 로고    scopus 로고
    • Detergent-resistant membranes should not be identified with membrane rafts
    • Lichtenberg D., Goni F.M., and Heerklotz H. Detergent-resistant membranes should not be identified with membrane rafts. Trends Biochem. Sci. 30 (2005) 430-436
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 430-436
    • Lichtenberg, D.1    Goni, F.M.2    Heerklotz, H.3
  • 16
    • 33746928724 scopus 로고    scopus 로고
    • Biochemical characterization of detergent-resistant membranes: a systematic approach
    • Babiychuk E.B., and Draeger A. Biochemical characterization of detergent-resistant membranes: a systematic approach. Biochem. J. 397 (2006) 407-416
    • (2006) Biochem. J. , vol.397 , pp. 407-416
    • Babiychuk, E.B.1    Draeger, A.2
  • 17
    • 1642354334 scopus 로고    scopus 로고
    • Lipid rafts: heterogeneity on the high seas
    • Pike L. Lipid rafts: heterogeneity on the high seas. Biochem. J. 378 (2004) 281-292
    • (2004) Biochem. J. , vol.378 , pp. 281-292
    • Pike, L.1
  • 20
    • 9444267662 scopus 로고    scopus 로고
    • Protein oligomerization modulates raft partitioning and apical sorting of GPI-anchored proteins
    • Paladino S., Sarnataro D., Pillich R., Tivodar S., Nitsch L., and Zurzolo C. Protein oligomerization modulates raft partitioning and apical sorting of GPI-anchored proteins. J. Cell Biol. 167 (2004) 699-709
    • (2004) J. Cell Biol. , vol.167 , pp. 699-709
    • Paladino, S.1    Sarnataro, D.2    Pillich, R.3    Tivodar, S.4    Nitsch, L.5    Zurzolo, C.6
  • 21
    • 0027892019 scopus 로고
    • Cholesterol and the Golgi apparatus
    • Bretscher M.S., and Munro S. Cholesterol and the Golgi apparatus. Science 261 (1993) 1280-1281
    • (1993) Science , vol.261 , pp. 1280-1281
    • Bretscher, M.S.1    Munro, S.2
  • 22
    • 7244244196 scopus 로고    scopus 로고
    • Lipids do influence protein function - the hydrophobic matching hypothesis revisited
    • Jensen M.O., and Mouritsen O.G. Lipids do influence protein function - the hydrophobic matching hypothesis revisited. Biochim. Biophys. Acta 1666 (2004) 205-226
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 205-226
    • Jensen, M.O.1    Mouritsen, O.G.2
  • 23
    • 33644838018 scopus 로고    scopus 로고
    • Clathrin-independent endocytosis: new insights into caveolae and non-caveolar lipid raft carriers
    • Kirkham M., and Parton R.G. Clathrin-independent endocytosis: new insights into caveolae and non-caveolar lipid raft carriers. Biochim. Biophys. Acta 1746 (2005) 350-363
    • (2005) Biochim. Biophys. Acta , vol.1746 , pp. 350-363
    • Kirkham, M.1    Parton, R.G.2
  • 24
    • 33645216741 scopus 로고    scopus 로고
    • Biogenesis of caveolae: a structural model for caveolin-induced domain formation
    • Parton R.G., Hanzal-Bayer M., and Hancock J.F. Biogenesis of caveolae: a structural model for caveolin-induced domain formation. J. Cell Sci. 119 (2006) 787-796
    • (2006) J. Cell Sci. , vol.119 , pp. 787-796
    • Parton, R.G.1    Hanzal-Bayer, M.2    Hancock, J.F.3
  • 25
    • 0035265834 scopus 로고    scopus 로고
    • Interleukin 2 receptors and detergent-resistant membrane domains define a clathring-independent endocytic pathway
    • Lamaze C., Dujeancourt A., Baba T., Lo C.G., Benmerah A., and Dautry-Varsat A. Interleukin 2 receptors and detergent-resistant membrane domains define a clathring-independent endocytic pathway. Mol. Cell 7 (2001) 661-671
    • (2001) Mol. Cell , vol.7 , pp. 661-671
    • Lamaze, C.1    Dujeancourt, A.2    Baba, T.3    Lo, C.G.4    Benmerah, A.5    Dautry-Varsat, A.6
  • 26
    • 0036232040 scopus 로고    scopus 로고
    • GPI-anchored proteins are delivered to recycling endosomes via a distinct cdc42-regulated, clathrin-independent pinocytic pathway
    • Sabharanjak S., Sharma P., Parton R.G., and Mayor S. GPI-anchored proteins are delivered to recycling endosomes via a distinct cdc42-regulated, clathrin-independent pinocytic pathway. Dev. Cell 2 (2002) 411-423
    • (2002) Dev. Cell , vol.2 , pp. 411-423
    • Sabharanjak, S.1    Sharma, P.2    Parton, R.G.3    Mayor, S.4
  • 27
    • 17244380947 scopus 로고    scopus 로고
    • Lipid raft and membrane dynamics
    • Rajendran L., and Simons K. Lipid raft and membrane dynamics. J. Cell Sci 118 (2005) 1099-1102
    • (2005) J. Cell Sci , vol.118 , pp. 1099-1102
    • Rajendran, L.1    Simons, K.2
  • 28
    • 28444476999 scopus 로고    scopus 로고
    • Membrane curvature and mechanisms of dynamic cell membrane remodelling
    • McMahon H., 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.1    Gallop, J.L.2
  • 29
    • 0001335174 scopus 로고
    • Budding of membranes induced by intramembrane domains
    • Lipowsky R. Budding of membranes induced by intramembrane domains. J. Phys. II France 2 (1992) 1825-1840
    • (1992) J. Phys. II France , vol.2 , pp. 1825-1840
    • Lipowsky, R.1
  • 30
  • 31
    • 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
  • 32
    • 14744278787 scopus 로고    scopus 로고
    • Sterol structure determines the separation of phases and the curvature of the liquid-ordered phase in model membranes
    • Bacia K., Schwille P., and Kurzchalia T. Sterol structure determines the separation of phases and the curvature of the liquid-ordered phase in model membranes. Proc. Natl. Acad. Sci. USA 102 (2005) 3272-3277
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 3272-3277
    • Bacia, K.1    Schwille, P.2    Kurzchalia, T.3
  • 33
    • 20644454019 scopus 로고    scopus 로고
    • Line tension and interaction energies of membrane rafts calculated from lipid splay and tilt
    • Kuzmin P.I., Akimov S.A., Chizmadzhev Y.A., Zimmerberg J., and Cohen F.S. Line tension and interaction energies of membrane rafts calculated from lipid splay and tilt. Biophys. J. 88 (2005) 1120-1133
    • (2005) Biophys. J. , vol.88 , pp. 1120-1133
    • Kuzmin, P.I.1    Akimov, S.A.2    Chizmadzhev, Y.A.3    Zimmerberg, J.4    Cohen, F.S.5
  • 34
    • 18444366155 scopus 로고    scopus 로고
    • Role of curvature and phase separation 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 separation in lipid sorting and fission of membrane tubules. EMBO J. 24 (2005) 1537-1545
    • (2005) EMBO J. , vol.24 , pp. 1537-1545
    • Roux, A.1    Cuvelier, D.2    Nassoy, P.3    Prost, J.4    Bassereau, P.5    Goud, B.6
  • 36
    • 2442560225 scopus 로고    scopus 로고
    • A role for myosin 1a in the localization of a brush border disaccharidase
    • Tyska M.J., and Mooseker M.S. A role for myosin 1a in the localization of a brush border disaccharidase. J. Cell Biol. 165 (2004) 395-405
    • (2004) J. Cell Biol. , vol.165 , pp. 395-405
    • Tyska, M.J.1    Mooseker, M.S.2
  • 37
    • 22744458753 scopus 로고    scopus 로고
    • Role of fission yeast myosin I in organization of sterol-rich membrane domains
    • Takeda T., and Chang F. Role of fission yeast myosin I in organization of sterol-rich membrane domains. Curr. Biol. 15 (2005) 1331-1336
    • (2005) Curr. Biol. , vol.15 , pp. 1331-1336
    • Takeda, T.1    Chang, F.2
  • 39
    • 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
  • 40
    • 33845368663 scopus 로고    scopus 로고
    • Actin polymerization serves as a membrane domain switch in model lipid bilayers
    • Liu A.P., and Fletcher D.A. Actin polymerization serves as a membrane domain switch in model lipid bilayers. Biophys. J. 91 (2006) 4064-4070
    • (2006) Biophys. J. , vol.91 , pp. 4064-4070
    • Liu, A.P.1    Fletcher, D.A.2
  • 42
    • 21244500528 scopus 로고    scopus 로고
    • Lipid raft association of SNARE proteins regulates exocytosis in PC12 cells
    • Salaün C., Gould G.W., and Chamberlain L.H. Lipid raft association of SNARE proteins regulates exocytosis in PC12 cells. J. Biol. Chem. 280 (2005) 19449-19453
    • (2005) J. Biol. Chem. , vol.280 , pp. 19449-19453
    • Salaün, C.1    Gould, G.W.2    Chamberlain, L.H.3
  • 43
    • 33645839858 scopus 로고    scopus 로고
    • STED microscopy reveals that synaptotagmin remains clustered after synaptic vesicle exocytosis
    • Willig K.I., Rizzoli S.O., Westphal V., Jahn R., and Hell S.W. STED microscopy reveals that synaptotagmin remains clustered after synaptic vesicle exocytosis. Nature 440 (2006) 935-939
    • (2006) Nature , vol.440 , pp. 935-939
    • Willig, K.I.1    Rizzoli, S.O.2    Westphal, V.3    Jahn, R.4    Hell, S.W.5
  • 44
    • 2942738956 scopus 로고    scopus 로고
    • Cholesterol domains regulate the actin cytoskeleton at the leading edge of moving cells
    • Manes S., and Martinez-A C. Cholesterol domains regulate the actin cytoskeleton at the leading edge of moving cells. Trends Cell. Biol. 14 (2004) 275-278
    • (2004) Trends Cell. Biol. , vol.14 , pp. 275-278
    • Manes, S.1    Martinez-A, C.2
  • 45
    • 0347764491 scopus 로고    scopus 로고
    • Polarization of plasma membrane microviscosity during endothelial cell migration
    • Vasanji A., et al. Polarization of plasma membrane microviscosity during endothelial cell migration. Dev. Cell 6 (2004) 29-41
    • (2004) Dev. Cell , vol.6 , pp. 29-41
    • Vasanji, A.1
  • 46
    • 33746478573 scopus 로고    scopus 로고
    • The region-specific activities of lipid rafts during axongrowth and guidance
    • Kamiguchi H. The region-specific activities of lipid rafts during axongrowth and guidance. J. Neurochem. 98 (2006) 330-335
    • (2006) J. Neurochem. , vol.98 , pp. 330-335
    • Kamiguchi, H.1
  • 47
    • 1842557804 scopus 로고    scopus 로고
    • Lipid rafts mediate chemotropic guidance of nerve growth cones
    • Guirland C., Suzuki S., Kojima M., Lu B., and Zheng J.Q. Lipid rafts mediate chemotropic guidance of nerve growth cones. Neuron 42 (2004) 51-62
    • (2004) Neuron , vol.42 , pp. 51-62
    • Guirland, C.1    Suzuki, S.2    Kojima, M.3    Lu, B.4    Zheng, J.Q.5
  • 48
    • 33751213401 scopus 로고    scopus 로고
    • Transbilayer effects of Raft-like lipid domains in asymmetric planar bilayers measured by single molecule tracking
    • Kiessling V., Crane J.M., and Tamm L.K. Transbilayer effects of Raft-like lipid domains in asymmetric planar bilayers measured by single molecule tracking. Biophys. J. 91 (2006) 3313-3326
    • (2006) Biophys. J. , vol.91 , pp. 3313-3326
    • Kiessling, V.1    Crane, J.M.2    Tamm, L.K.3
  • 50
    • 17844381899 scopus 로고    scopus 로고
    • Bacterial invasion via lipid rafts
    • Lafont F., and van der Goot F.G. Bacterial invasion via lipid rafts. Cell. Microbiol. 7 (2005) 613-620
    • (2005) Cell. Microbiol. , vol.7 , pp. 613-620
    • Lafont, F.1    van der Goot, F.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.