메뉴 건너뛰기




Volumn 135, Issue 6, 2008, Pages 1085-1097

Nanoclusters of GPI-Anchored Proteins Are Formed by Cortical Actin-Driven Activity

Author keywords

CELLBIO

Indexed keywords

ACTIN; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED PROTEIN; MYOSIN;

EID: 57149125825     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2008.11.032     Document Type: Article
Times cited : (400)

References (36)
  • 2
    • 0031471375 scopus 로고    scopus 로고
    • Ezrin: a protein requiring conformational activation to link microfilaments to the plasma membrane in the assembly of cell surface structures
    • Bretscher A., Reczek D., and Berryman M. Ezrin: a protein requiring conformational activation to link microfilaments to the plasma membrane in the assembly of cell surface structures. J. Cell Sci. 110 (1997) 3011-3018
    • (1997) J. Cell Sci. , vol.110 , pp. 3011-3018
    • Bretscher, A.1    Reczek, D.2    Berryman, M.3
  • 3
    • 34249090252 scopus 로고    scopus 로고
    • Cholesterol-sensitive Cdc42 activation regulates actin polymerization for endocytosis via the GEEC pathway
    • Chadda R., Howes M.T., Plowman S.J., Hancock J.F., Parton R.G., and Mayor S. Cholesterol-sensitive Cdc42 activation regulates actin polymerization for endocytosis via the GEEC pathway. Traffic 8 (2007) 702-717
    • (2007) Traffic , vol.8 , pp. 702-717
    • Chadda, R.1    Howes, M.T.2    Plowman, S.J.3    Hancock, J.F.4    Parton, R.G.5    Mayor, S.6
  • 8
    • 0035794533 scopus 로고    scopus 로고
    • GPI anchoring leads to sphingolipid-dependent retention of endocytosed proteins in the recycling endosomal compartment
    • Chatterjee S., Smith E.R., Hanada K., Stevens V.L., and Mayor S. GPI anchoring leads to sphingolipid-dependent retention of endocytosed proteins in the recycling endosomal compartment. EMBO J. 20 (2001) 1583-1592
    • (2001) EMBO J. , vol.20 , pp. 1583-1592
    • Chatterjee, S.1    Smith, E.R.2    Hanada, K.3    Stevens, V.L.4    Mayor, S.5
  • 9
    • 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 W.R., Yang B., Milgram S.L., and Jacobson K. Transient anchorage of cross-linked glycosyl-phosphatidylinositol-anchored proteins depends on cholesterol, Src family kinases, caveolin, and phosphoinositides. J. Cell Biol. 175 (2006) 169-178
    • (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
  • 10
    • 34848927902 scopus 로고    scopus 로고
    • The many faces of actin: matching assembly factors with cellular structures
    • Chhabra E.S., and Higgs H.N. The many faces of actin: matching assembly factors with cellular structures. Nat. Cell Biol. 9 (2007) 1110-1121
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1110-1121
    • Chhabra, E.S.1    Higgs, H.N.2
  • 11
    • 0037959071 scopus 로고    scopus 로고
    • The state of lipids rafts: From model membranes to cells
    • Edidin M. The state of lipids rafts: From model membranes to cells. Annu. Rev. Biophys. Biomol. Struct. 32 (2003) 257-283
    • (2003) Annu. Rev. Biophys. Biomol. Struct. , vol.32 , pp. 257-283
    • Edidin, M.1
  • 12
    • 34250368055 scopus 로고    scopus 로고
    • Gangliosides GM1 and GM3 in the living cell membrane form clusters susceptible to cholesterol depletion and chilling
    • Fujita A., Cheng J., Hirakawa M., Furukawa K., Kusunoki S., and Fujimoto T. Gangliosides GM1 and GM3 in the living cell membrane form clusters susceptible to cholesterol depletion and chilling. Mol. Biol. Cell 18 (2007) 2112-2122
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2112-2122
    • Fujita, A.1    Cheng, J.2    Hirakawa, M.3    Furukawa, K.4    Kusunoki, S.5    Fujimoto, T.6
  • 13
    • 33645299024 scopus 로고    scopus 로고
    • Visualizing membrane microdomains by Laurdan 2-photon microscopy
    • Gaus K., Zech T., and Harder T. Visualizing membrane microdomains by Laurdan 2-photon microscopy. Mol. Membr. Biol. 23 (2006) 41-48
    • (2006) Mol. Membr. Biol. , vol.23 , pp. 41-48
    • Gaus, K.1    Zech, T.2    Harder, T.3
  • 14
    • 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
  • 16
    • 0034683671 scopus 로고    scopus 로고
    • Activation by Cdc42 and PIP(2) of Wiskott-Aldrich syndrome protein (WASp) stimulates actin nucleation by Arp2/3 complex
    • Higgs H.N., and Pollard T.D. Activation by Cdc42 and PIP(2) of Wiskott-Aldrich syndrome protein (WASp) stimulates actin nucleation by Arp2/3 complex. J. Cell Biol. 150 (2000) 1311-1320
    • (2000) J. Cell Biol. , vol.150 , pp. 1311-1320
    • Higgs, H.N.1    Pollard, T.D.2
  • 18
    • 33845901815 scopus 로고    scopus 로고
    • Lipid rafts: at a crossroad between cell biology and physics
    • Jacobson K., Mouritsen O.G., and Anderson R.G. 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.3
  • 19
    • 0036318103 scopus 로고    scopus 로고
    • Differences in cortical actin structure and dynamics document that different types of blebs are formed by distinct mechanisms
    • Keller H., Rentsch P., and Hagmann J. Differences in cortical actin structure and dynamics document that different types of blebs are formed by distinct mechanisms. Exp. Cell Res. 277 (2002) 161-172
    • (2002) Exp. Cell Res. , vol.277 , pp. 161-172
    • Keller, H.1    Rentsch, P.2    Hagmann, J.3
  • 20
    • 1642632601 scopus 로고    scopus 로고
    • Asters, vortices and rotating spirals in active gels of polar filaments
    • Kruse K., Joanny J.F., Jülicher F., Prost J., and Sekimoto K. Asters, vortices and rotating spirals in active gels of polar filaments. Phys. Rev. Lett. 92 (2004) 078101
    • (2004) Phys. Rev. Lett. , vol.92 , pp. 078101
    • Kruse, K.1    Joanny, J.F.2    Jülicher, F.3    Prost, J.4    Sekimoto, K.5
  • 21
    • 0345564815 scopus 로고    scopus 로고
    • Membrane cholesterol, lateral mobility, and the phosphatidylinositol 4,5-bisphosphate-dependent organization of cell actin
    • Kwik J., Boyle S., Fooksman D., Margolis L., Sheetz M.P., and Edidin M. Membrane cholesterol, lateral mobility, and the phosphatidylinositol 4,5-bisphosphate-dependent organization of cell actin. Proc. Natl. Acad. Sci. USA 100 (2003) 13964-13969
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13964-13969
    • Kwik, J.1    Boyle, S.2    Fooksman, D.3    Margolis, L.4    Sheetz, M.P.5    Edidin, M.6
  • 22
    • 1842536499 scopus 로고    scopus 로고
    • Rafts: scale-dependent, active lipid organization at the cell surface
    • Mayor S., and Rao M. Rafts: scale-dependent, active lipid organization at the cell surface. Traffic 5 (2004) 231-240
    • (2004) Traffic , vol.5 , pp. 231-240
    • Mayor, S.1    Rao, M.2
  • 24
    • 28444482087 scopus 로고    scopus 로고
    • Regulation of protein activities by phosphoinositide phosphates
    • Niggli V. Regulation of protein activities by phosphoinositide phosphates. Annu. Rev. Cell Dev. Biol. 21 (2005) 57-79
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 57-79
    • Niggli, V.1
  • 25
    • 0345203007 scopus 로고
    • Continuous fluorescence microphotolysis: A sensitive method for study of diffusion processes in single cells
    • Peters R., Brunger A., and Schulten K. Continuous fluorescence microphotolysis: A sensitive method for study of diffusion processes in single cells. Proc. Natl. Acad. Sci. USA 78 (1981) 962-966
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 962-966
    • Peters, R.1    Brunger, A.2    Schulten, K.3
  • 26
    • 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., and 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. USA 102 (2005) 15500-15505
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 15500-15505
    • Plowman, S.J.1    Muncke, C.2    Parton, R.G.3    Hancock, J.F.4
  • 27
    • 0038140101 scopus 로고    scopus 로고
    • The physics of active membranes
    • Ramaswamy S., and Rao M. The physics of active membranes. C R Acad. Sci. IV 2 (2001) 817-839
    • (2001) C R Acad. Sci. IV , vol.2 , pp. 817-839
    • Ramaswamy, S.1    Rao, M.2
  • 28
    • 36949017931 scopus 로고    scopus 로고
    • Active-filament hydrodynamics: instabilities, boundary conditions and rheology
    • Ramaswamy S., and Rao M. Active-filament hydrodynamics: instabilities, boundary conditions and rheology. N. J. Phys. 9 (2007) 423
    • (2007) N. J. Phys. , vol.9 , pp. 423
    • Ramaswamy, S.1    Rao, M.2
  • 29
    • 29144533892 scopus 로고    scopus 로고
    • Use of Forster's resonance energy transfer microscopy to study lipid rafts
    • Rao M., and Mayor S. Use of Forster's resonance energy transfer microscopy to study lipid rafts. Biochim. Biophys. Acta 1746 (2005) 221-233
    • (2005) Biochim. Biophys. Acta , vol.1746 , pp. 221-233
    • Rao, M.1    Mayor, S.2
  • 31
    • 0021719038 scopus 로고
    • ATP-dependent movement of myosin in vitro: characterization of a quantitative assay
    • Sheetz M.P., Chasan R., and Spudich J.A. ATP-dependent movement of myosin in vitro: characterization of a quantitative assay. J. Cell Biol. 99 (1984) 1867-1871
    • (1984) J. Cell Biol. , vol.99 , pp. 1867-1871
    • Sheetz, M.P.1    Chasan, R.2    Spudich, J.A.3
  • 32
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K., and Ikonen E. Functional rafts in cell membranes. Nature 387 (1997) 569-572
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 35
    • 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 K.G., Fujiwara T.K., Sanematsu F., Iino R., Edidin M., and 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. 177 (2007) 717-730
    • (2007) J. Cell Biol. , vol.177 , pp. 717-730
    • Suzuki, K.G.1    Fujiwara, T.K.2    Sanematsu, F.3    Iino, R.4    Edidin, M.5    Kusumi, A.6
  • 36
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma R., and Mayor S. GPI-anchored proteins are organized in submicron domains at the cell surface. Nature 394 (1998) 798-801
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.