메뉴 건너뛰기




Volumn 2, Issue 1, 2010, Pages

Understanding lipid rafts and other related membrane domains

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CHOLESTEROL; LIPID; MEMBRANE PROTEIN;

EID: 77955081952     PISSN: 17404118     EISSN: 1757594X     Source Type: Journal    
DOI: 10.3410/B2-31     Document Type: Review
Times cited : (29)

References (44)
  • 1
    • 0016287588 scopus 로고
    • Lipid components of two different regions of an intestinal epithelial cell membrane of a mouse
    • Kawai K, Fujita M, Nakao M: Lipid components of two different regions of an intestinal epithelial cell membrane of a mouse. Biochim Biophys Acta 1974, 369:222-33.
    • (1974) Biochim Biophys Acta , vol.369 , pp. 222-233
    • Kawai, K.1    Fujita, M.2    Nakao, M.3
  • 2
    • 0020339953 scopus 로고
    • Viruses budding from either the apical or the basolateral plasma membrane domain of MDCK cells have unique phospholipid compositions
    • van Meer G, Simons K: Viruses budding from either the apical or the basolateral plasma membrane domain of MDCK cells have unique phospholipid compositions. EMBO J 1982, 1:847-52.
    • (1982) EMBO J , vol.1 , pp. 847-852
    • Van Meer, G.1    Simons, K.2
  • 3
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • Lingwood D, Simons K: Lipid rafts as a membrane-organizing principle. Science 2010, 327:46-50.
    • Science , vol.2010 , Issue.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 7
    • 38149122245 scopus 로고    scopus 로고
    • Structural determinants for partitioning of lipids and proteins between coexisting fluid phases in giant plasma membrane vesicles
    • Sengupta P, Hammond A, Holowka D, Baird B: Structural determinants for partitioning of lipids and proteins between coexisting fluid phases in giant plasma membrane vesicles. Biochim Biophys Acta 2008, 1778:20-32.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 20-32
    • Sengupta, P.1    Hammond, A.2    Holowka, D.3    Baird, B.4
  • 8
    • 48249097851 scopus 로고    scopus 로고
    • Plasma membranes are poised for activation of raft phase coalesence at physiological temperature
    • Lingwood D, Ries J, Schwille P, Simons K: Plasma membranes are poised for activation of raft phase coalesence at physiological temperature. Proc Natl Acad Sci U S A 2008, 105:10005-10.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 10005-10010
    • Lingwood, D.1    Ries, J.2    Schwille, P.3    Simons, K.4
  • 10
    • 1542399850 scopus 로고    scopus 로고
    • Lipid raft proteins have a random distribution during localized activation of the T-cell receptor
    • Glebov OO, Nichols BJ: Lipid raft proteins have a random distribution during localized activation of the T-cell receptor. Nat Cell Biol 2004, 6:238-43.
    • (2004) Nat Cell Biol , vol.6 , pp. 238-243
    • Glebov, O.O.1    Nichols, B.J.2
  • 12
    • 33845901815 scopus 로고    scopus 로고
    • Lipid rafts: At a crossroad between cell biology and physics
    • DOI 10.1038/ncb0107-7, PII NCB0107-7
    • Jacobson K, Mouritsen OG, Anderson RG: Lipid rafts: at a crossroad between cell biology and physics. Nat Cell Biol 2007, 9:7-14. (Pubitemid 46024188)
    • (2007) Nature Cell Biology , vol.9 , Issue.1 , pp. 7-14
    • Jacobson, K.1    Mouritsen, O.G.2    Anderson, R.G.W.3
  • 16
    • 46749128544 scopus 로고    scopus 로고
    • Both MHC class II and its GPI-anchored form undergo hop diffusion as observed by single-molecule tracking
    • Umemura YM, Vrjic M, Nishimura SY, Fujiwara TK, Suzuki KG, Kusumi A: Both MHC class II and its GPI-anchored form undergo hop diffusion as observed by single-molecule tracking. Biophys J 2008, 95:435-50.
    • (2008) Biophys J , vol.95 , pp. 435-450
    • Umemura, Y.M.1    Vrjic, M.2    Nishimura, S.Y.3    Fujiwara, T.K.4    Suzuki, K.G.5    Kusumi, A.6
  • 17
    • 33749544508 scopus 로고    scopus 로고
    • Transient anchorage of cross-linked glycosyl-phosphatidylinositol- anchored proteins depends on cholesterol, Src family kinases, caveolin, and phosphoinositides
    • Chen Y, Thelin WR, Yang B, Milgram SL, Jacobson K: Transient anchorage of cross-linked glycosyl-phosphatidylinositol-anchored proteins depends on cholesterol, Src family kinases, caveolin, and phosphoinositides. J Cell Biol 2006, 175:169-78.
    • (2006) J Cell Biol , vol.175 , pp. 169-178
    • Chen, Y.1    Thelin, W.R.2    Yang, B.3    Milgram, S.L.4    Jacobson, K.5
  • 18
    • 34249066421 scopus 로고    scopus 로고
    • GPI-anchored receptor clusters transiently recruit Lyn and G alpha for temporary cluster immobilization and Lyn activation: Single-molecule tracking study 1
    • Suzuki KG, Fugiwara TK, Sanematsu F, lino R, Edidin M, Kusumi A: GPI-anchored receptor clusters transiently recruit Lyn and G alpha for temporary cluster immobilization and Lyn activation: single-molecule tracking study 1. J Cell Biol 2007, 177:717-30.
    • (2007) J Cell Biol , vol.177 , pp. 717-730
    • Suzuki, K.G.1    Fugiwara, T.K.2    Sanematsu, F.3    Lino, R.4    Edidin, M.5    Kusumi, A.6
  • 19
    • 34249074042 scopus 로고    scopus 로고
    • Dynamic recruitment of phospholipase C gamma at transiently immobilized GPI-anchored receptor clusters induces IP3-Ca2+ signalling: Single-molecule tracking study 2
    • Suzuki KG, Fujiwara TK, Edidin M, Kusumi A: Dynamic recruitment of phospholipase C gamma at transiently immobilized GPI-anchored receptor clusters induces IP3-Ca2+ signalling: single-molecule tracking study 2. J Cell Biol 2007, 177:731-42.
    • (2007) J Cell Biol , vol.177 , pp. 731-742
    • Suzuki, K.G.1    Fujiwara, T.K.2    Edidin, M.3    Kusumi, A.4
  • 20
    • 70450236974 scopus 로고    scopus 로고
    • The transmembrane protein CBP plays a role in transiently anchoring small clusters of Thy-1, a GPI-anchored protein, to the cytoskeleton
    • Chen Y, Veracini L, Benistant C, Jacobson K: The transmembrane protein CBP plays a role in transiently anchoring small clusters of Thy-1, a GPI-anchored protein, to the cytoskeleton. J Cell Sci 2009, 122:3966-72.
    • (2009) J Cell Sci , vol.122 , pp. 3966-3972
    • Chen, Y.1    Veracini, L.2    Benistant, C.3    Jacobson, K.4
  • 21
    • 0034015604 scopus 로고    scopus 로고
    • Evidence for budding of human immunodeficiency virus type 1 selectively from glycolipid-enriched membrane lipid rafts
    • Nguyen DH, Hildreth JE: Evidence for budding of human immunodeficiency virus type 1 selectively from glycolipid-enriched membrane lipid rafts. J Virol 2000, 74:3264-72.
    • (2000) J Virol , vol.74 , pp. 3264-3272
    • Nguyen, D.H.1    Hildreth, J.E.2
  • 23
    • 0033593321 scopus 로고    scopus 로고
    • Influenza Viruses Select Ordered Lipid Domains during Budding from the Plasma Membrane
    • Scheiffele P, Rietveld A, Wilk T, Simons K: Influenza viruses select ordered lipid domains during budding from the plasma membrane. J Biol Chem 1999, 274:2038-44. (Pubitemid 129621737)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.4 , pp. 2038-2044
    • Scheiffele, P.1    Rietveld, A.2    Wilk, T.3    Simons, K.4
  • 25
    • 67749139973 scopus 로고    scopus 로고
    • The lipidomes of vesicular stomatitis virus, semliki forest virus, and the host plasma membrane analyzed by quantitative shotgun mass spectrometry
    • Kalvodova L, Sampaio JL, Cordo S, Ejsing CS, Shevchenko A, Simons K: The lipidomes of vesicular stomatitis virus, semliki forest virus, and the host plasma membrane analyzed by quantitative shotgun mass spectrometry. J Virol 2009, 83:7996-8003.
    • (2009) J Virol , vol.83 , pp. 7996-8003
    • Kalvodova, L.1    Sampaio, J.L.2    Cordo, S.3    Ejsing, C.S.4    Shevchenko, A.5    Simons, K.6
  • 26
    • 36849053761 scopus 로고    scopus 로고
    • Dynamic clustered distribution of hemagglutinin resolved at 40 nm in living cell membranes discriminates between raft theories
    • Hess ST, Gould TJ, Gudheti MV, Maas SA, Mills KD, Zimmerberg J: Dynamic clustered distribution of hemagglutinin resolved at 40 nm in living cell membranes discriminates between raft theories. Proc Natl Acad Sci U S A 2007, 104:17370-5.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 17370-17375
    • Hess, S.T.1    Gould, T.J.2    Gudheti, M.V.3    Maas, S.A.4    Mills, K.D.5    Zimmerberg, J.6
  • 27
    • 0347482478 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion
    • Takeda M, Leser GP, Russell CJ, Lamb RA: Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion. Proc Natl Acad Sci U S A 2003, 100:14610-7.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 14610-14617
    • Takeda, M.1    Leser, G.P.2    Russell, C.J.3    Lamb, R.A.4
  • 28
    • 74349083523 scopus 로고    scopus 로고
    • FLIM-FRET and FRAP reveal association of influenza virus haemagglutinin with membrane rafts
    • Engel S, Scolari S, Thaa B, Krebs N, Korte T, Herrmann A, Veit M: FLIM-FRET and FRAP reveal association of influenza virus haemagglutinin with membrane rafts. Biochem J 2010, 425:567-73.
    • Biochem J , vol.2010 , Issue.425 , pp. 567-573
    • Engel, S.1    Scolari, S.2    Thaa, B.3    Krebs, N.4    Korte, T.5    Herrmann, A.6    Veit, M.7
  • 29
    • 67650103574 scopus 로고    scopus 로고
    • Lateral distribution of the transmembrane domain of influenza virus hemagglutinin revealed by time-resolved fluorescence imaging
    • Scolari S, Engel S, Krebs N, Plazzo AP, De Almeida RF, Prieto M, Veit M, Herrmann A: Lateral distribution of the transmembrane domain of influenza virus hemagglutinin revealed by time-resolved fluorescence imaging. J Biol Chem 2009, 284:15708-16.
    • (2009) J Biol Chem , vol.284 , pp. 15708-15716
    • Scolari, S.1    Engel, S.2    Krebs, N.3    Plazzo, A.P.4    De Almeida, R.F.5    Prieto, M.6    Veit, M.7    Herrmann, A.8
  • 30
    • 40949088194 scopus 로고    scopus 로고
    • Progressive ordering with decreasing temperature of the phospholipids of influenza virus
    • DOI 10.1038/nchembio.77, PII NCHEMBIO77
    • Polozov IV, Bezrukov L, Grawrisch K, Zimmerberg J: Progressive ordering with decreasing temperature of the phospholipids of influenza virus. Nat Chem Biol 2008, 4:248-55. (Pubitemid 351414833)
    • (2008) Nature Chemical Biology , vol.4 , Issue.4 , pp. 248-255
    • Polozov, I.V.1    Bezrukov, L.2    Gawrisch, K.3    Zimmerberg, J.4
  • 31
    • 47049130164 scopus 로고    scopus 로고
    • Imaging the biogenesis of individual HIV-1 virions in live cells
    • Jouvenet N, Bieniasz PD, Simon SM: Imaging the biogenesis of individual HIV-1 virions in live cells. Nature 2008, 454:236-40.
    • (2008) Nature , vol.454 , pp. 236-240
    • Jouvenet, N.1    Bieniasz, P.D.2    Simon, S.M.3
  • 33
    • 33746625935 scopus 로고    scopus 로고
    • Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly
    • Saad JS, Miller J, Tai J, Kim A, Ghanam RH, Summers MF: Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly. Proc Natl Acad Sci U S A 2006, 103:11364-9.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 11364-11369
    • Saad, J.S.1    Miller, J.2    Tai, J.3    Kim, A.4    Ghanam, R.H.5    Summers, M.F.6
  • 34
    • 28444441957 scopus 로고    scopus 로고
    • Tetraspanin functions and associated microdomains
    • Hemler ME: Tetraspanin functions and associated microdomains. Nat Rev Mol Cell Biol 2005, 6:801-11.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 801-811
    • Hemler, M.E.1
  • 35
    • 33747394451 scopus 로고    scopus 로고
    • Mapping of tetraspanin-enriched microdomains that can function as gateways for HIV-1
    • Nydegger S, Khurana S, Krementsov DN, Foti M, Thali M: Mapping of tetraspanin-enriched microdomains that can function as gateways for HIV-1. J Cell Biol 2006, 173:795-807.
    • (2006) J Cell Biol , vol.173 , pp. 795-807
    • Nydegger, S.1    Khurana, S.2    Krementsov, D.N.3    Foti, M.4    Thali, M.5
  • 36
    • 34547105037 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 assembly, budding, and cell-cell spread in T cells take place in tetraspanin-enriched plasma membrane domains
    • Jolly C, Sattentau QJ: Human immunodeficiency virus type 1 assembly, budding, and cell-cell spread in T cells take place in tetraspanin-enriched plasma membrane domains. J Virol 2007, 81:7873-84.
    • (2007) J Virol , vol.81 , pp. 7873-7884
    • Jolly, C.1    Sattentau, Q.J.2
  • 37
    • 0035896648 scopus 로고    scopus 로고
    • Evaluation of prototype transmembrane 4 superfamily protein complexes and their relation to lipid rafts
    • Claas C, Stipp CS, Hemler ME: Evaluation of prototype transmembrane 4 superfamily protein complexes and their relation to lipid rafts. J Biol Chem 2001, 276:7974-84.
    • (2001) J Biol Chem , vol.276 , pp. 7974-7984
    • Claas, C.1    Stipp, C.S.2    Hemler, M.E.3
  • 38
    • 33845975257 scopus 로고    scopus 로고
    • Membrane microdomains and proteomics: Lessons from tetraspanin microdomains and comparison with lipid rafts
    • DOI 10.1002/pmic.200600282
    • Le Naour F, Andre M, Boucheix C, Rubinstein E: Membrane microdomains and proteomics: lessons from tetraspanin microdomains and comparison with lipid rafts. Proteomics 2006, 6:6447-54. (Pubitemid 46048385)
    • (2006) Proteomics , vol.6 , Issue.24 , pp. 6447-6454
    • Le Naour, F.1    Andre, M.2    Boucheix, C.3    Rubinstein, E.4
  • 42
    • 42149114525 scopus 로고    scopus 로고
    • Distribution and lateral mobility of DC-SIGN on immature dendritic cells-implications for pathogen uptake
    • Neumann AK, Thompson NL, Jacobson K: Distribution and lateral mobility of DC-SIGN on immature dendritic cells-implications for pathogen uptake. J Cell Sci 2008, 121:634-43.
    • (2008) J Cell Sci , vol.121 , pp. 634-643
    • Neumann, A.K.1    Thompson, N.L.2    Jacobson, K.3
  • 43
    • 67649781736 scopus 로고    scopus 로고
    • T-cell growth, cell surface organization, and the galectin-glycoprotein lattice
    • Grigorian A, Torossian S, Demetriou M: T-cell growth, cell surface organization, and the galectin-glycoprotein lattice. Immunol Rev 2009, 230:232-46.
    • (2009) Immunol Rev , vol.230 , pp. 232-246
    • Grigorian, A.1    Torossian, S.2    Demetriou, M.3
  • 44
    • 77649250020 scopus 로고    scopus 로고
    • A novel pseudopodial component of the dendritic cell anti-fungal response: The fungipod
    • Neumann AK, Jacobson K: A novel pseudopodial component of the dendritic cell anti-fungal response: the fungipod. PLoS Pathog 2010, 6:e1000760.
    • PLoS Pathog , vol.2010 , Issue.6
    • Neumann, A.K.1    Jacobson, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.