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Volumn 37, Issue 2, 2012, Pages 295-300

Insights into eisosome assembly and organization

Author keywords

Eisosome; Membrane organization; Pil1

Indexed keywords

EIOSOSOME; MEMBRANE PROTEIN; PROTEIN LSP1; PROTEIN PIL1; UNCLASSIFIED DRUG;

EID: 84864375399     PISSN: 02505991     EISSN: 09737138     Source Type: Journal    
DOI: 10.1007/s12038-012-9206-6     Document Type: Review
Times cited : (8)

References (46)
  • 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
    • 79957449178 scopus 로고    scopus 로고
    • Identification, in vitro activity and mode of action of phosphoinositide-dependent-1 kinase inhibitors as antifungal molecules
    • Baxter BK, Didone L, Oga D, Schor S and Krysan DJ 2011 Identification, in vitro activity and mode of action of phosphoinositide-dependent-1 kinase inhibitors as antifungal molecules. ACS Chem. Biol. 20 502-510
    • (2011) ACS Chem. Biol. , vol.20 , pp. 502-510
    • Baxter, B.K.1    Didone, L.2    Oga, D.3    Schor, S.4    Krysan, D.J.5
  • 4
    • 63749117393 scopus 로고    scopus 로고
    • TORC2 plasma membrane localization is essential for cell viability and restricted to a distinct domain
    • Berchtold D and Walther TC 2009 TORC2 plasma membrane localization is essential for cell viability and restricted to a distinct domain. Mol. Biol. Cell 20 1565-1575
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1565-1575
    • Berchtold, D.1    Walther, T.C.2
  • 5
    • 79551574273 scopus 로고    scopus 로고
    • Reassessment of the role of plasma membrane domains in the regulation of vesicular traffic in yeast
    • Brach T, Specht T and Kaksonen M 2011 Reassessment of the role of plasma membrane domains in the regulation of vesicular traffic in yeast. J. Cell Sci. 124 328-337
    • (2011) J. Cell Sci. , vol.124 , pp. 328-337
    • Brach, T.1    Specht, T.2    Kaksonen, M.3
  • 6
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid- and cholesterol-rich membrane rafts
    • Brown DA and London E 2000 Structure and function of sphingolipid- and cholesterol-rich membrane rafts. J. Biol. Chem. 275 17221-17224
    • (2000) J. Biol. Chem. , vol.275 , pp. 17221-17224
    • Brown, D.A.1    London, E.2
  • 7
    • 33745049690 scopus 로고    scopus 로고
    • Slm1 and slm2 are novel substrates of the calcineurin phosphatase required for heat stress-induced endocytosis of the yeast uracil permease
    • Bultynck G, Heath VL, Majeed AP, Galan JM, Haguenauer-Tsapis R and Cyert MS 2006 Slm1 and slm2 are novel substrates of the calcineurin phosphatase required for heat stress-induced endocytosis of the yeast uracil permease. Mol. Cell Biol. 26 4729-4745
    • (2006) Mol. Cell Biol. , vol.26 , pp. 4729-4745
    • Bultynck, G.1    Heath, V.L.2    Majeed, A.P.3    Galan, J.M.4    Haguenauer-Tsapis, R.5    Cyert, M.S.6
  • 8
    • 0033602281 scopus 로고    scopus 로고
    • Functional counterparts of mammalian protein kinases PDK1 and SGK in budding yeast
    • Casamayor A, Torrance PD, Kobayashi T, Thorner J and Alessi DR 1999 Functional counterparts of mammalian protein kinases PDK1 and SGK in budding yeast. Curr. Biol. 9 186-197
    • (1999) Curr. Biol. , vol.9 , pp. 186-197
    • Casamayor, A.1    Torrance, P.D.2    Kobayashi, T.3    Thorner, J.4    Alessi, D.R.5
  • 9
    • 33846147991 scopus 로고    scopus 로고
    • The yeast PH domain proteins Slm1 and Slm2 are targets of sphingolipid signaling during the response to heat stress
    • Daquinag A, Fadri M, Jung SY, Qin J and Kunz J 2007 The yeast PH domain proteins Slm1 and Slm2 are targets of sphingolipid signaling during the response to heat stress. Mol. Cell Biol. 27 633-650
    • (2007) Mol. Cell Biol. , vol.27 , pp. 633-650
    • Daquinag, A.1    Fadri, M.2    Jung, S.Y.3    Qin, J.4    Kunz, J.5
  • 10
    • 67649613489 scopus 로고    scopus 로고
    • Unifying fluorescence microscopy and mass spectrometry for studying protein complexes in cells
    • Deng C, Xiong X and Krutchinsky AN 2009 Unifying fluorescence microscopy and mass spectrometry for studying protein complexes in cells. Mol. Cell. Proteom. 8 1413-1423
    • (2009) Mol. Cell. Proteom. , vol.8 , pp. 1413-1423
    • Deng, C.1    Xiong, X.2    Krutchinsky, A.N.3
  • 11
    • 0032546798 scopus 로고    scopus 로고
    • MSS4, a phosphatidylinositol-4-phosphate 5-kinase required for organization of the actin cytoskeleton in Saccharomyces cerevisiae
    • Desrivieres S, Cooke FT, Parker PJ and Hall MN 1998 MSS4, a phosphatidylinositol-4-phosphate 5-kinase required for organization of the actin cytoskeleton in Saccharomyces cerevisiae. J. Biol. Chem. 273 15787-15793
    • (1998) J. Biol. Chem. , vol.273 , pp. 15787-15793
    • Desrivieres, S.1    Cooke, F.T.2    Parker, P.J.3    Hall, M.N.4
  • 12
    • 16344385976 scopus 로고    scopus 로고
    • The pleckstrin homology domain proteins Slm1 and Slm2 are required for actin cytoskeleton organization in yeast and bind phosphatidylinositol-4,5- bisphosphate and TORC2
    • Fadri M, Daquinag A, Wang S, Xue T and Kunz J 2005 The pleckstrin homology domain proteins Slm1 and Slm2 are required for actin cytoskeleton organization in yeast and bind phosphatidylinositol-4,5-bisphosphate and TORC2. Mol. Biol. Cell 16 1883-1900
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1883-1900
    • Fadri, M.1    Daquinag, A.2    Wang, S.3    Xue, T.4    Kunz, J.5
  • 13
  • 14
    • 64249110493 scopus 로고    scopus 로고
    • The BAR domain superfamily: Membrane-molding macromolecules
    • Frost A, Unger VM and De Camilli P 2009 The BAR domain superfamily: membrane-molding macromolecules. Cell 137 191-196
    • (2009) Cell , vol.137 , pp. 191-196
    • Frost, A.1    Unger, V.M.2    De Camilli, P.3
  • 15
    • 15544366139 scopus 로고    scopus 로고
    • BAR domains and membrane curvature: Bringing your curves to the BAR
    • Gallop JL and McMahon HT 2005 BAR domains and membrane curvature: bringing your curves to the BAR. Biochem. Soc. Symp. 223-231
    • (2005) Biochem. Soc. Symp. , pp. 223-231
    • Gallop, J.L.1    McMahon, H.T.2
  • 17
    • 33846240490 scopus 로고    scopus 로고
    • Membrane potential governs lateral segregation of plasma membrane proteins and lipids in yeast
    • Grossmann G, Opekarova M, Malinsky J, Weig-Meckl I and Tanner W. 2007 Membrane potential governs lateral segregation of plasma membrane proteins and lipids in yeast. EMBO J. 26 1-8
    • (2007) EMBO J. , vol.26 , pp. 1-8
    • Grossmann, G.1    Opekarova, M.2    Malinsky, J.3    Weig-Meckl, I.4    Tanner, W.5
  • 18
    • 0033532062 scopus 로고    scopus 로고
    • SAC1-like domains of yeast SAC1, INP52 and INP53 and of human synaptojanin encode polyphosphoinositide phosphatases
    • Guo S, Stolz LE, Lemrow SM and York JD 1999 SAC1-like domains of yeast SAC1, INP52 and INP53 and of human synaptojanin encode polyphosphoinositide phosphatases. J. Biol. Chem. 274 12990-12995
    • (1999) J. Biol. Chem. , vol.274 , pp. 12990-12995
    • Guo, S.1    Stolz, L.E.2    Lemrow, S.M.3    York, J.D.4
  • 19
    • 0037144543 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae YBR159w gene encodes the 3-ketoreductase of the microsomal fatty acid elongase
    • Han G, Gable K, Kohlwein SD, Beaudoin F, Napier JA and Dunn TM 2002 The Saccharomyces cerevisiae YBR159w gene encodes the 3-ketoreductase of the microsomal fatty acid elongase. J. Biol. Chem. 277 35440-35449
    • (2002) J. Biol. Chem. , vol.277 , pp. 35440-35449
    • Han, G.1    Gable, K.2    Kohlwein, S.D.3    Beaudoin, F.4    Napier, J.A.5    Dunn, T.M.6
  • 20
    • 0037423225 scopus 로고    scopus 로고
    • The uracil transporter Fur4p associates with lipid rafts
    • Hearn JD, Lester RL and Dickson RC 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
  • 21
    • 80655125002 scopus 로고    scopus 로고
    • The filament-forming protein Pil1 assembles linear eisosomes in fission yeast
    • Kabeche R, Baldissard S, Hammond J, Howard L and Moseley JB 2011 The filament-forming protein Pil1 assembles linear eisosomes in fission yeast. Mol. Biol. Cell 22 4059-4067
    • (2011) Mol. Biol. Cell , vol.22 , pp. 4059-4067
    • Kabeche, R.1    Baldissard, S.2    Hammond, J.3    Howard, L.4    Moseley, J.B.5
  • 22
    • 79957630131 scopus 로고    scopus 로고
    • Requirements of Slm proteins for proper eisosome organization, endocytic trafficking and recycling in the yeast Saccharomyces cerevisiae
    • Kamble C, Jain S, Murphy E and Kim K 2011 Requirements of Slm proteins for proper eisosome organization, endocytic trafficking and recycling in the yeast Saccharomyces cerevisiae. J. Biosci. 36 79-96
    • (2011) J. Biosci. , vol.36 , pp. 79-96
    • Kamble, C.1    Jain, S.2    Murphy, E.3    Kim, K.4
  • 24
    • 84858703061 scopus 로고    scopus 로고
    • Lipid rafts: A signalling platform linking lipoprotein metabolism to atherogenesis
    • Lemaire-Ewing S, Lagrost L and Neel D 2011 Lipid rafts: A signalling platform linking lipoprotein metabolism to atherogenesis. Atherosclerosis 221 303-310
    • (2011) Atherosclerosis , vol.221 , pp. 303-310
    • Lemaire-Ewing, S.1    Lagrost, L.2    Neel, D.3
  • 25
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membraneorganizing principle
    • Lingwood D and Simons K. 2010 Lipid rafts as a membraneorganizing principle. Science 327 46-50
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 26
    • 44849101230 scopus 로고    scopus 로고
    • The sphingolipid long-chain base-Pkh1/2-Ypk1/2 signaling pathway regulates eisosome assembly and turnover
    • Luo G, Gruhler A, Liu Y, Jensen ON and Dickson RC 2008 The sphingolipid long-chain base-Pkh1/2-Ypk1/2 signaling pathway regulates eisosome assembly and turnover. J. Biol. Chem. 283 10433-10444
    • (2008) J. Biol. Chem. , vol.283 , pp. 10433-10444
    • Luo, G.1    Gruhler, A.2    Liu, Y.3    Jensen, O.N.4    Dickson, R.C.5
  • 27
    • 0345255797 scopus 로고    scopus 로고
    • Visualization of protein compartmentation within the plasma membrane of living yeast cells
    • Malinska K, Malinsky J, Opekarova M and Tanner W 2003 Visualization of protein compartmentation within the plasma membrane of living yeast cells. Mol. Biol. Cell 14 4427-4436
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4427-4436
    • Malinska, K.1    Malinsky, J.2    Opekarova, M.3    Tanner, W.4
  • 28
    • 12344298783 scopus 로고    scopus 로고
    • Distribution of Can1p into stable domains reflects lateral protein segregation within the plasma membrane of living S. cerevisiae cells
    • Malinska K, Malinsky J, Opekarova M and Tanner W 2004 Distribution of Can1p into stable domains reflects lateral protein segregation within the plasma membrane of living S. cerevisiae cells. J. Cell Sci. 117 6031-6041
    • (2004) J. Cell Sci. , vol.117 , pp. 6031-6041
    • Malinska, K.1    Malinsky, J.2    Opekarova, M.3    Tanner, W.4
  • 29
    • 80052408748 scopus 로고    scopus 로고
    • Pil1, an eisosome organizer, plays an important role in the recruitment of synaptojanins and amphiphysins to facilitate receptor-mediated endocytosis in yeast
    • Murphy ER, Boxberger J, Colvin R, Lee SJ, Zahn G, Loor F and Kim K 2011 Pil1, an eisosome organizer, plays an important role in the recruitment of synaptojanins and amphiphysins to facilitate receptor-mediated endocytosis in yeast. Eur. J. Cell Biol. 90 825-833
    • (2011) Eur. J. Cell Biol. , vol.90 , pp. 825-833
    • Murphy, E.R.1    Boxberger, J.2    Colvin, R.3    Lee, S.J.4    Zahn, G.5    Loor, F.6    Kim, K.7
  • 31
    • 33646937804 scopus 로고    scopus 로고
    • Members of the Arabidopsis FAE1-like 3-ketoacyl-CoA synthase gene family substitute for the Elop proteins of Saccharomyces cerevisiae
    • Paul S, Gable K, Beaudoin F, Cahoon E, Jaworski J, Napier JA and Dunn TM 2006 Members of the Arabidopsis FAE1-like 3-ketoacyl-CoA synthase gene family substitute for the Elop proteins of Saccharomyces cerevisiae. J. Biol. Chem. 281 9018-9029
    • (2006) J. Biol. Chem. , vol.281 , pp. 9018-9029
    • Paul, S.1    Gable, K.2    Beaudoin, F.3    Cahoon, E.4    Jaworski, J.5    Napier, J.A.6    Dunn, T.M.7
  • 32
    • 79953285898 scopus 로고    scopus 로고
    • Dual-colour fluorescence microscopy using yEmCherry-/GFP-tagging of eisosome components Pil1 and Lsp1 in Candida albicans
    • Reijnst P, Walther A and Wendland J 2011 Dual-colour fluorescence microscopy using yEmCherry-/GFP-tagging of eisosome components Pil1 and Lsp1 in Candida albicans. Yeast 28 331-338
    • (2011) Yeast , vol.28 , pp. 331-338
    • Reijnst, P.1    Walther, A.2    Wendland, J.3
  • 33
    • 79956089059 scopus 로고    scopus 로고
    • Formation and stability of eisosomes in the filamentous fungus Ashbya gossypii
    • Seger S, Rischatsch R and Philippsen P 2011 Formation and stability of eisosomes in the filamentous fungus Ashbya gossypii. J. Cell Sci. 124 1629-1634
    • (2011) J. Cell Sci. , vol.124 , pp. 1629-1634
    • Seger, S.1    Rischatsch, R.2    Philippsen, P.3
  • 34
    • 79955073961 scopus 로고    scopus 로고
    • Lipid rafts: Signaling and sorting platforms of cells and their roles in cancer
    • Staubach S and Hanisch FG 2011 Lipid rafts: signaling and sorting platforms of cells and their roles in cancer. Expert Rev. Proteom. 8 263-277
    • (2011) Expert Rev. Proteom. , vol.8 , pp. 263-277
    • Staubach, S.1    Hanisch, F.G.2
  • 36
    • 33947199781 scopus 로고    scopus 로고
    • Synthesis and function of membrane phosphoinositides in budding yeast Saccharomyces cerevisiae
    • Strahl T and Thorner J 2007 Synthesis and function of membrane phosphoinositides in budding yeast Saccharomyces cerevisiae. Biochim. Biophys. Acta 1771 353-404
    • (2007) Biochim. Biophys. Acta , vol.1771 , pp. 353-404
    • Strahl, T.1    Thorner, J.2
  • 37
    • 77950594242 scopus 로고    scopus 로고
    • Subcellular membrane curvature mediated by the BAR domain superfamily proteins
    • Suetsugu S, Toyooka K and Senju Y. 2010 Subcellular membrane curvature mediated by the BAR domain superfamily proteins. Semin. Cell Dev. Biol. 21 340-349
    • (2010) Semin. Cell Dev. Biol. , vol.21 , pp. 340-349
    • Suetsugu, S.1    Toyooka, K.2    Senju, Y.3
  • 38
    • 34247526437 scopus 로고    scopus 로고
    • PtdIns (4,5)P2 turnover is required for multiple stages during clathrin- and actin-dependent endocytic internalization
    • Sun Y, Carroll S, Kaksonen M, Toshima JY and Drubin DG 2007 PtdIns(4,5)P2 turnover is required for multiple stages during clathrin- and actin-dependent endocytic internalization. J. Cell Biol. 177 355-367
    • (2007) J. Cell Biol. , vol.177 , pp. 355-367
    • Sun, Y.1    Carroll, S.2    Kaksonen, M.3    Toshima, J.Y.4    Drubin, D.G.5
  • 39
    • 41849145402 scopus 로고    scopus 로고
    • Multiple pathways regulate endocytic coat disassembly in Saccharomyces cerevisiae for optimal downstream trafficking
    • Toret CP, Lee L, Sekiya-Kawasaki M and Drubin DG 2008 Multiple pathways regulate endocytic coat disassembly in Saccharomyces cerevisiae for optimal downstream trafficking. Traffic 9 848-859
    • (2008) Traffic , vol.9 , pp. 848-859
    • Toret, C.P.1    Lee, L.2    Sekiya-Kawasaki, M.3    Drubin, D.G.4
  • 43
  • 44
  • 45
    • 2542499556 scopus 로고    scopus 로고
    • Pil1p and Lsp1p negatively regulate the 3-phosphoinositide-dependent protein kinase-like kinase Pkh1p and downstream signaling pathways Pkc1p and Ypk1p
    • Zhang X, Lester RL and Dickson RC 2004 Pil1p and Lsp1p negatively regulate the 3-phosphoinositide-dependent protein kinase-like kinase Pkh1p and downstream signaling pathways Pkc1p and Ypk1p. J. Biol. Chem. 279 22030-22038
    • (2004) J. Biol. Chem. , vol.279 , pp. 22030-22038
    • Zhang, X.1    Lester, R.L.2    Dickson, R.C.3


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