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Volumn 14, Issue 11, 2003, Pages 4427-4436

Visualization of Protein Compartmentation within the Plasma Membrane of Living Yeast Cells

Author keywords

[No Author keywords available]

Indexed keywords

COTRANSPORTER; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; PROTEIN; PROTEIN CAN1P; PROTEIN PMA1P; UNCLASSIFIED DRUG;

EID: 0345255797     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E03-04-0221     Document Type: Article
Times cited : (243)

References (54)
  • 1
    • 0035661570 scopus 로고    scopus 로고
    • Plasma membrane proton ATPase Pma1p requires raft association for surface delivery in yeast
    • Bagnat, M., Chang, A., and Simons, K. (2001). Plasma membrane proton ATPase Pma1p requires raft association for surface delivery in yeast. Mol. Biol. Cell 12, 4129-4138.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 4129-4138
    • Bagnat, M.1    Chang, A.2    Simons, K.3
  • 2
    • 0034724182 scopus 로고    scopus 로고
    • Lipid rafts function in biosynthetic delivery of proteins to the cell surface in yeast
    • Bagnat, M., Keranen, S., Shevchenko, A., and Simons, K. (2000). Lipid rafts function in biosynthetic delivery of proteins to the cell surface in yeast. Proc. Natl. Acad. Sci. USA 97, 3254-3259.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3254-3259
    • Bagnat, M.1    Keranen, S.2    Shevchenko, A.3    Simons, K.4
  • 3
    • 0037195112 scopus 로고    scopus 로고
    • Cell surface polarization during yeast mating
    • Bagnat, M., and Simons, K. (2002). Cell surface polarization during yeast mating. Proc. Natl. Acad. Sci. USA 99, 14183-14188.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14183-14188
    • Bagnat, M.1    Simons, K.2
  • 4
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: A useful set of strains and plasmids for PCR-mediated gene disruption and other applications
    • Brachmann, C.B., Davies, A., Cost, G.J., Caputo, E., Li, J., Hieter, P., and Boeke, J.D. (1998). Designer deletion strains derived from Saccharomyces cerevisiae S288C: a useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast 14, 115-132.
    • (1998) Yeast , vol.14 , pp. 115-132
    • Brachmann, C.B.1    Davies, A.2    Cost, G.J.3    Caputo, E.4    Li, J.5    Hieter, P.6    Boeke, J.D.7
  • 6
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown, D.A., and London, E. (1998). Functions of lipid rafts in biological membranes. Annu. Rev. Cell Dev. Biol. 14, 111-136.
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 7
    • 0026512314 scopus 로고
    • Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the cell surface
    • Brown, D.A., and Rose, J.K. (1992). Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the cell surface. Cell 68, 533-544.
    • (1992) Cell , vol.68 , pp. 533-544
    • Brown, D.A.1    Rose, J.K.2
  • 9
    • 0034051803 scopus 로고    scopus 로고
    • Cysteine-string protein: The chaperone at the synapse
    • Chamberlain, L.H., and Burgoyne, R.D. (2000). Cysteine-string protein: the chaperone at the synapse. J. Neurochem. 74, 1781-1789.
    • (2000) J. Neurochem. , vol.74 , pp. 1781-1789
    • Chamberlain, L.H.1    Burgoyne, R.D.2
  • 10
    • 0035826727 scopus 로고    scopus 로고
    • SNARE proteins are highly enriched in lipid rafts in PC12 cells: Implications for the spatial control of exocytosis
    • Chamberlain, L.H., Burgoyne, R.D., and Gould, G.W. (2001). SNARE proteins are highly enriched in lipid rafts in PC12 cells: implications for the spatial control of exocytosis. Proc. Natl. Acad. Sci. USA 98, 5619-5624.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5619-5624
    • Chamberlain, L.H.1    Burgoyne, R.D.2    Gould, G.W.3
  • 11
    • 0035213174 scopus 로고    scopus 로고
    • Rafts and synapses in the spatial organization of immune cell signaling receptors
    • Dykstra, M., Cherukuri, A., and Pierce, S.K. (2001). Rafts and synapses in the spatial organization of immune cell signaling receptors. J. Leukoc. Biol. 70, 699-707.
    • (2001) J. Leukoc. Biol. , vol.70 , pp. 699-707
    • Dykstra, M.1    Cherukuri, A.2    Pierce, S.K.3
  • 12
    • 0031041581 scopus 로고    scopus 로고
    • Compartmentalized activation of the high affinity immunoglobulin E receptor within membrane domains
    • Field, K.A., Holowka, D., and Baird, B. (1997). Compartmentalized activation of the high affinity immunoglobulin E receptor within membrane domains. J. Biol. Chem. 272, 4276-4280.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4276-4280
    • Field, K.A.1    Holowka, D.2    Baird, B.3
  • 13
    • 0035943423 scopus 로고    scopus 로고
    • Emerging themes in lipid rafts and caveolae
    • Galbiati, F., Razani, B., and Lisanti, M.P. (2001). Emerging themes in lipid rafts and caveolae. Cell 106, 403-411.
    • (2001) Cell , vol.106 , pp. 403-411
    • Galbiati, F.1    Razani, B.2    Lisanti, M.P.3
  • 14
    • 0031750335 scopus 로고    scopus 로고
    • Lipid domain structure of the plasma membrane revealed by patching of membrane components
    • Harder, T., Scheiffele, P., Verkade, P., and Simons, K. (1998). Lipid domain structure of the plasma membrane revealed by patching of membrane components. J. Cell Biol. 141, 929-942.
    • (1998) J. Cell Biol. , vol.141 , pp. 929-942
    • Harder, T.1    Scheiffele, P.2    Verkade, P.3    Simons, K.4
  • 15
    • 0029687367 scopus 로고    scopus 로고
    • Fluorescence microscopy methods
    • Hasek, J., and Streiblova, E. (1996). Fluorescence microscopy methods. Methods Mol. Biol. 53, 391-405.
    • (1996) Methods Mol. Biol. , vol.53 , pp. 391-405
    • Hasek, J.1    Streiblova, E.2
  • 16
    • 0037423225 scopus 로고    scopus 로고
    • The uracil transporter Fur4p associates with lipid rafts
    • Hearn, J.D., Lester, R.L., and Dickson, R.C. (2003). The uracil transporter Fur4p associates with lipid rafts. J. Biol. Chem. 278, 3679-3686.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3679-3686
    • Hearn, J.D.1    Lester, R.L.2    Dickson, R.C.3
  • 17
    • 0028102402 scopus 로고
    • Proton migration along the membrane surface and retarded surface to bulk transfer
    • Heberle, J., Riesle, J., Thiedemann, G., Oesterhelt, D., and Dencher, N.A. (1994). Proton migration along the membrane surface and retarded surface to bulk transfer. Nature 370, 379-382.
    • (1994) Nature , vol.370 , pp. 379-382
    • Heberle, J.1    Riesle, J.2    Thiedemann, G.3    Oesterhelt, D.4    Dencher, N.A.5
  • 18
    • 0028921834 scopus 로고
    • Improved green fluorescence
    • Heim, R., Cubitt, A.B., and Tsien, R.Y. (1995). Improved green fluorescence. Nature 373, 663-664.
    • (1995) Nature , vol.373 , pp. 663-664
    • Heim, R.1    Cubitt, A.B.2    Tsien, R.Y.3
  • 19
    • 0022212597 scopus 로고
    • Molecular characterization of the CAN1 locus in Saccharomyces cerevisiae. A transmembrane protein without N-terminal hydrophobic signal sequence
    • Hoffmann, W. (1985). Molecular characterization of the CAN1 locus in Saccharomyces cerevisiae. A transmembrane protein without N-terminal hydrophobic signal sequence. J. Biol. Chem. 260, 11831-11837.
    • (1985) J. Biol. Chem. , vol.260 , pp. 11831-11837
    • Hoffmann, W.1
  • 20
    • 0035423556 scopus 로고    scopus 로고
    • Roles of lipid rafts in membrane transport
    • Ikonen, E. (2001). Roles of lipid rafts in membrane transport. Curr. Opin. Cell Biol. 13, 470-477.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 470-477
    • Ikonen, E.1
  • 23
    • 0030474342 scopus 로고    scopus 로고
    • Identification of Triton X-100 insoluble membrane domains in the yeast Saccharomyces cerevisiae. Lipid requirements for targeting of heterotrimeric G-protein subunits
    • Kübler, E., Dohlman, H.G., and Lisanti, M.P. (1996). Identification of Triton X-100 insoluble membrane domains in the yeast Saccharomyces cerevisiae. Lipid requirements for targeting of heterotrimeric G-protein subunits. J. Biol. Chem. 271, 32975-32980.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32975-32980
    • Kübler, E.1    Dohlman, H.G.2    Lisanti, M.P.3
  • 24
    • 0030222116 scopus 로고    scopus 로고
    • Cell surface organization by the membrane skeleton
    • Kusumi, A., and Sako, Y. (1996). Cell surface organization by the membrane skeleton. Curr. Opin. Cell Biol. 8, 566-574.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 566-574
    • Kusumi, A.1    Sako, Y.2
  • 25
    • 0037151098 scopus 로고    scopus 로고
    • Ceramide biosynthesis is required for the formation of the oligomeric H+-ATPase Pma1p in the yeast endoplasmic reticulum
    • Lee, M.C., Hamamoto, S., and Schekman, R. (2002). Ceramide biosynthesis is required for the formation of the oligomeric H+-ATPase Pma1p in the yeast endoplasmic reticulum. J. Biol. Chem. 277, 22395-22401.
    • (2002) J. Biol. Chem. , vol.277 , pp. 22395-22401
    • Lee, M.C.1    Hamamoto, S.2    Schekman, R.3
  • 27
    • 0029044628 scopus 로고
    • Insolubility and redistribution of GPI-anchored proteins at the cell surface after detergent treatment
    • Mayor, S., and Maxfield, F.R. (1995). Insolubility and redistribution of GPI-anchored proteins at the cell surface after detergent treatment. Mol. Biol. Cell 6, 929-944.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 929-944
    • Mayor, S.1    Maxfield, F.R.2
  • 29
    • 0031952731 scopus 로고    scopus 로고
    • Post-translational fate of CAN1 permease of Saccharomyces cerevisiae
    • Opekarova, M., Caspari, T., Pinson, B., Brethes, D., and Tanner, W. (1998). Post-translational fate of CAN1 permease of Saccharomyces cerevisiae. Yeast 14, 215-224.
    • (1998) Yeast , vol.14 , pp. 215-224
    • Opekarova, M.1    Caspari, T.2    Pinson, B.3    Brethes, D.4    Tanner, W.5
  • 30
    • 0037136036 scopus 로고    scopus 로고
    • Phosphatidyl ethanolamine is essential for targeting the arginine transporter Canlp to the plasma membrane of yeast
    • Opekarova, M., Robl, I., and Tanner, W. (2002). Phosphatidyl ethanolamine is essential for targeting the arginine transporter Canlp to the plasma membrane of yeast. Biochim. Biophys. Acta 1564, 9-13.
    • (2002) Biochim. Biophys. Acta , vol.1564 , pp. 9-13
    • Opekarova, M.1    Robl, I.2    Tanner, W.3
  • 31
    • 0034611005 scopus 로고    scopus 로고
    • Sphin-golipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells
    • Pralle, A., Keller, P., Florin, E.L., Simons, K., and Horber, J.K. (2000). Sphin-golipid-cholesterol rafts diffuse as small entities in the plasma membrane of mammalian cells. J. Cell Biol. 148, 997-1008.
    • (2000) J. Cell Biol. , vol.148 , pp. 997-1008
    • Pralle, A.1    Keller, P.2    Florin, E.L.3    Simons, K.4    Horber, J.K.5
  • 32
    • 0028949280 scopus 로고
    • Identification of novel HXT genes in Saccharomyces cerevisiae reveals the impact of individual hexose transporters on glycolytic flux
    • Reifenberger, E., Freidel, K., and Ciriacy, M. (1995). Identification of novel HXT genes in Saccharomyces cerevisiae reveals the impact of individual hexose transporters on glycolytic flux. Mol. Microbiol. 16, 157-167.
    • (1995) Mol. Microbiol. , vol.16 , pp. 157-167
    • Reifenberger, E.1    Freidel, K.2    Ciriacy, M.3
  • 33
    • 0031740079 scopus 로고    scopus 로고
    • The differential miscibility of lipids as the basis for the formation of functional membrane rafts
    • Rietveld, A., and Simons, K. (1998). The differential miscibility of lipids as the basis for the formation of functional membrane rafts. Biochim. Biophys. Acta 1376, 467-479.
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 467-479
    • Rietveld, A.1    Simons, K.2
  • 34
    • 0033577803 scopus 로고    scopus 로고
    • LST1 is a SEC24 homologue used for selective export of the plasma membrane ATPase from the endoplasmic reticulum
    • Roberg, K.J., Crotwell, M., Espenshade, P., Gimeno, R., and Kaiser, C.A. (1999). LST1 is a SEC24 homologue used for selective export of the plasma membrane ATPase from the endoplasmic reticulum. J. Cell Biol. 145, 659-672.
    • (1999) J. Cell Biol. , vol.145 , pp. 659-672
    • Roberg, K.J.1    Crotwell, M.2    Espenshade, P.3    Gimeno, R.4    Kaiser, C.A.5
  • 35
    • 0023739386 scopus 로고
    • Protein sorting in Saccharomyces cerevisiae: Isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases
    • Robinson, J.S., Klionsky, D.J., Banta, L.M., and Emr, S.D. (1988). Protein sorting in Saccharomyces cerevisiae: isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases. Mol. Cell. Biol. 8, 4936-4948.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4936-4948
    • Robinson, J.S.1    Klionsky, D.J.2    Banta, L.M.3    Emr, S.D.4
  • 36
    • 0035114940 scopus 로고    scopus 로고
    • Construction of phosphatidylethanolamine-less strain of Saccharomyces cerevisiae. Effect on amino acid transport
    • Robl, I., Grassl, R., Tanner, W., and Opekarova, M. (2001). Construction of phosphatidylethanolamine-less strain of Saccharomyces cerevisiae. Effect on amino acid transport. Yeast 18, 251-260.
    • (2001) Yeast , vol.18 , pp. 251-260
    • Robl, I.1    Grassl, R.2    Tanner, W.3    Opekarova, M.4
  • 37
    • 0035879095 scopus 로고    scopus 로고
    • Glycolipid-enriched membrane domains are assembled into membrane patches by associating with the actin cytoskeleton
    • Rodgers, W., and Zavzavadjian, J. (2001). Glycolipid-enriched membrane domains are assembled into membrane patches by associating with the actin cytoskeleton. Exp. Cell Res. 267, 173-183.
    • (2001) Exp. Cell Res. , vol.267 , pp. 173-183
    • Rodgers, W.1    Zavzavadjian, J.2
  • 38
    • 0034282003 scopus 로고    scopus 로고
    • Retention of prominin in microvilli reveals distinct cholesterol-based lipid micro-domains in the apical plasma membrane
    • Roper, K., Corbeil, D., and Huttner, W.B. (2000). Retention of prominin in microvilli reveals distinct cholesterol-based lipid micro-domains in the apical plasma membrane. Nat. Cell Biol. 2, 582-592.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 582-592
    • Roper, K.1    Corbeil, D.2    Huttner, W.B.3
  • 40
    • 0037164716 scopus 로고    scopus 로고
    • Differential localization of glucose transporter isoforms in non-polarized mammalian cells: Distribution of GLUT1 but not GLUT3 to detergent-resistant membrane domains
    • Sakyo, T., and Kitagawa, T. (2002). Differential localization of glucose transporter isoforms in non-polarized mammalian cells: distribution of GLUT1 but not GLUT3 to detergent-resistant membrane domains. Biochim. Biophys. Acta 1567, 165-175.
    • (2002) Biochim. Biophys. Acta , vol.1567 , pp. 165-175
    • Sakyo, T.1    Kitagawa, T.2
  • 41
    • 0022607425 scopus 로고
    • Yeast plasma membrane ATPase is essential for growth and has homology with (Na+ + K+), K+- and Ca2+-ATPases
    • Serrano, R., Kielland-Brandt, M.C., and Fink, G.R. (1986). Yeast plasma membrane ATPase is essential for growth and has homology with (Na+ + K+), K+- and Ca2+-ATPases. Nature 319, 689-693.
    • (1986) Nature , vol.319 , pp. 689-693
    • Serrano, R.1    Kielland-Brandt, M.C.2    Fink, G.R.3
  • 42
    • 0000871808 scopus 로고
    • Genome Dynamics, Protein Synthesis and Energetics
    • ed. J.R. Broach, E.W. Jones, and J.R. Pringle, Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Serrano, R. (1991). Genome Dynamics, Protein Synthesis and Energetics. In: The Molecular and Cellular Biology of the Yeast Saccharomyces, ed. J.R. Broach, E.W. Jones, and J.R. Pringle, Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press, 523-585.
    • (1991) The Molecular and Cellular Biology of the Yeast Saccharomyces , pp. 523-585
    • Serrano, R.1
  • 43
    • 0019304034 scopus 로고
    • Lateral mobility of integral membrane proteins is increased in spherocytic erythrocytes
    • Sheetz, M.P., Schindler, M., and Koppel, D.E. (1980). Lateral mobility of integral membrane proteins is increased in spherocytic erythrocytes. Nature 285, 510-511.
    • (1980) Nature , vol.285 , pp. 510-511
    • Sheetz, M.P.1    Schindler, M.2    Koppel, D.E.3
  • 44
    • 0034722347 scopus 로고    scopus 로고
    • Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae
    • Shimoni, Y., Kurihara, T., Ravazzola, M., Amherdt, M., Orci, L., and Schekman, R. (2000). Lst1p and Sec24p cooperate in sorting of the plasma membrane ATPase into COPII vesicles in Saccharomyces cerevisiae. J. Cell Biol. 151, 973-984.
    • (2000) J. Cell Biol. , vol.151 , pp. 973-984
    • Shimoni, Y.1    Kurihara, T.2    Ravazzola, M.3    Amherdt, M.4    Orci, L.5    Schekman, R.6
  • 45
    • 0023788823 scopus 로고
    • Lipid sorting in epithelial cells
    • Simons, K., and van Meer, G. (1988). Lipid sorting in epithelial cells. Biochemistry 27, 6197-6202.
    • (1988) Biochemistry , vol.27 , pp. 6197-6202
    • Simons, K.1    Van Meer, G.2
  • 46
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons, K., and Ikonen, E. (1997). Functional rafts in cell membranes. Nature 387, 569-572.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 47
    • 0034529050 scopus 로고    scopus 로고
    • How cells handle cholesterol
    • Simons, K., and Ikonen, E. (2000). How cells handle cholesterol. Science 290, 1721-1726.
    • (2000) Science , vol.290 , pp. 1721-1726
    • Simons, K.1    Ikonen, E.2
  • 49
    • 0031452944 scopus 로고    scopus 로고
    • Compartmentalized IgE receptor-mediated signal transduction in living cells
    • Stauffer, T.P., and Meyer, T. (1997). Compartmentalized IgE receptor-mediated signal transduction in living cells. J. Cell Biol. 139, 1447-1454.
    • (1997) J. Cell Biol. , vol.139 , pp. 1447-1454
    • Stauffer, T.P.1    Meyer, T.2
  • 50
    • 0032563615 scopus 로고    scopus 로고
    • Regulation mechanism of the lateral diffusion of band 3 in erythrocyte membranes by the membrane skeleton
    • Tomishige, M., Sako, Y., and Kusumi, A. (1998). Regulation mechanism of the lateral diffusion of band 3 in erythrocyte membranes by the membrane skeleton. J. Cell Biol. 142, 989-1000.
    • (1998) J. Cell Biol. , vol.142 , pp. 989-1000
    • Tomishige, M.1    Sako, Y.2    Kusumi, A.3
  • 51
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma, R., and Mayor, S. (1998). GPI-anchored proteins are organized in submicron domains at the cell surface. Nature 394, 798-801.
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 52
    • 0036727004 scopus 로고    scopus 로고
    • Evidence for segregation of heterologous GPI-anchored proteins into separate lipid rafts within the plasma membrane
    • Wang, J., Gunning, W., Kelley, K.M., and Ratnam, M. (2002). Evidence for segregation of heterologous GPI-anchored proteins into separate lipid rafts within the plasma membrane. J. Membr. Biol. 189, 35-43.
    • (2002) J. Membr. Biol. , vol.189 , pp. 35-43
    • Wang, J.1    Gunning, W.2    Kelley, K.M.3    Ratnam, M.4
  • 53
    • 0001881653 scopus 로고    scopus 로고
    • Biochemical and physical properties of green fluorescent protein
    • ed. M. Chalfie and S. Kain, New York: John Wiley & Sons
    • Ward, W.W. (1998). Biochemical and physical properties of green fluorescent protein. In: Green Fluorescent Protein: Properties, Applications and Protocols, ed. M. Chalfie and S. Kain, New York: John Wiley & Sons, 45-76.
    • (1998) Green Fluorescent Protein: Properties, Applications and Protocols , pp. 45-76
    • Ward, W.W.1
  • 54
    • 0034659799 scopus 로고    scopus 로고
    • Sphingoid base synthesis requirement for endocytosis in Saccharomyces cerevisiae
    • Zanolari, B., Friant, S., Funato, K., Sutterlin, C., Stevenson, B.J., and Riezman, H. (2000). Sphingoid base synthesis requirement for endocytosis in Saccharomyces cerevisiae. EMBO J. 19, 2824-33.
    • (2000) EMBO J. , vol.19 , pp. 2824-2833
    • Zanolari, B.1    Friant, S.2    Funato, K.3    Sutterlin, C.4    Stevenson, B.J.5    Riezman, H.6


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