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Volumn 9, Issue 8, 2010, Pages 1184-1192

C terminus of Nce 102 determines the structure and function of microdomains in the Saccharomyces cerevisiae plasma membrane

Author keywords

[No Author keywords available]

Indexed keywords

ASCOMYCOTA; SACCHAROMYCES CEREVISIAE; SCHIZOSACCHAROMYCES POMBE;

EID: 77956800487     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.00006-10     Document Type: Article
Times cited : (35)

References (39)
  • 1
    • 0025082921 scopus 로고
    • Helix-coil stability constants for the naturally occurring amino acids in water. XXIII. Proline parameters from random poly (hydroxybutylglutamine-co-L-proline)
    • Altmann, K.-H., J. Wojcik, M. Vasquez, and H. A. Scheraga. 1990. Helix-coil stability constants for the naturally occurring amino acids in water. XXIII. Proline parameters from random poly (hydroxybutylglutamine-co-L-proline). Biopolymers 30:107-120.
    • (1990) Biopolymers , vol.30 , pp. 107-120
    • Altmann, K.-H.1    Wojcik, J.2    Vasquez, M.3    Scheraga, H.A.4
  • 3
    • 33749078313 scopus 로고    scopus 로고
    • A new paradigm for membrane-organizing and -shaping scaffolds
    • Bauer, M., and L. Pelkmans. 2006. A new paradigm for membrane-organizing and -shaping scaffolds. FEBS Lett. 580:5559-5564.
    • (2006) FEBS Lett. , vol.580 , pp. 5559-5564
    • Bauer, M.1    Pelkmans, L.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., A. Davies, G. J. Cost, E. Caputo, J. Li, P. Hieter, and J. D. Boeke. 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
  • 5
    • 46449135255 scopus 로고    scopus 로고
    • The hydrophobic insertion mechanism of membrane curvature generation by proteins
    • Campelo, F., H. T. McMahon, and M. M. Kozlov. 2008. The hydrophobic insertion mechanism of membrane curvature generation by proteins. Biophys. J. 95:2325-2339.
    • (2008) Biophys. J. , vol.95 , pp. 2325-2339
    • Campelo, F.1    McMahon, H.T.2    Kozlov, M.M.3
  • 6
    • 0030000860 scopus 로고    scopus 로고
    • A new pathway for protein export in Saccharomyces cerevisiae
    • Cleves, A. E., D. N. Cooper, S. H. Barondes, and R. B. Kelly. 1996. A new pathway for protein export in Saccharomyces cerevisiae. J. Cell Biol. 133: 1017-1026.
    • (1996) J. Cell Biol. , vol.133 , pp. 1017-1026
    • Cleves, A.E.1    Cooper, D.N.2    Barondes, S.H.3    Kelly, R.B.4
  • 7
    • 0035815754 scopus 로고    scopus 로고
    • Membrane topology and function of Der3/Hrd1p as a ubiquitin-protein ligase (E3) involved in endoplasmic reticulum degradation
    • Deak, P. M., and D. H. Wolf. 2001. Membrane topology and function of Der3/Hrd1p as a ubiquitin-protein ligase (E3) involved in endoplasmic reticulum degradation. J. Biol. Chem. 276:10663-10669.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10663-10669
    • Deak, P.M.1    Wolf, D.H.2
  • 8
    • 0030669030 scopus 로고    scopus 로고
    • Exploring the metabolic and genetic control of gene expression on a genomic scale
    • DeRisi, J. L., V. R. Iyer, and P.O. Brown. 1997. Exploring the metabolic and genetic control of gene expression on a genomic scale. Science. 278:680-686.
    • (1997) Science , vol.278 , pp. 680-686
    • Derisi, J.L.1    Iyer, V.R.2    Brown, P.O.3
  • 9
    • 0023567026 scopus 로고
    • A yeast mutant defective at an early stage in import of secretory protein precursors into the endoplasmic reticulum
    • Deshaies, R. J., and R. Schekman. 1987. A yeast mutant defective at an early stage in import of secretory protein precursors into the endoplasmic reticulum. J. Cell Biol. 105:633-645.
    • (1987) J. Cell Biol. , vol.105 , pp. 633-645
    • Deshaies, R.J.1    Schekman, R.2
  • 10
    • 67649625166 scopus 로고    scopus 로고
    • A genome-wide screen for genes affecting eisosomes reveals Nce102 function in sphingolipid signaling
    • K. Moreira, P. S. Aguilar, N. C. Hubner, M. Mann, P. Walter, and T. C. Walther. 2009. A genome-wide screen for genes affecting eisosomes reveals Nce102 function in sphingolipid signaling. J. Cell Biol. 185: 1227-1242.
    • (2009) J. Cell Biol. , vol.185 , pp. 1227-1242
    • Moreira, K.1    Aguilar, P.S.2    Hubner, N.C.3    Mann, M.4    Walter, P.5    Walther, T.C.6
  • 12
    • 0035162698 scopus 로고    scopus 로고
    • Genomic expression responses to DNA-damaging agents and the regulatory role of the yeast ATR homolog Mec1p
    • Gasch, A. P., M. Huang, S. Metzner, D. Botstein, S. J. Elledge, and P. O. Brown. 2001. Genomic expression responses to DNA-damaging agents and the regulatory role of the yeast ATR homolog Mec1p. Mol. Biol. Cell 12:2987-3003.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2987-3003
    • Gasch, A.P.1    Huang, M.2    Metzner, S.3    Botstein, D.4    Elledge, S.J.5    Brown, P.O.6
  • 13
    • 0024266139 scopus 로고
    • New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites
    • Gietz, R. D., and A. Sugino. 1988. New yeast-Escherichia coli shuttle vectors constructed with in vitro mutagenized yeast genes lacking six-base pair restriction sites. Gene 74:527-534.
    • (1988) Gene , vol.74 , pp. 527-534
    • Gietz, R.D.1    Sugino, A.2
  • 14
    • 0036270543 scopus 로고    scopus 로고
    • Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method
    • Gietz, R. D. and R. A. Woods. 2002. Transformation of yeast by lithium acetate/single-stranded carrier DNA/polyethylene glycol method. Methods Enzymol. 350:87-96.
    • (2002) Methods Enzymol. , vol.350 , pp. 87-96
    • Gietz, R.D.1    Woods, R.A.2
  • 15
    • 33846240490 scopus 로고    scopus 로고
    • Membrane potential governs lateral segregation of plasma membrane proteins and lipids in yeast
    • Grossmann, G., M. Opekarová, J. Malinsky, I. Weig-Meckl, and W. Tanner. 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    Opekarová, M.2    Malinsky, J.3    Weig-Meckl, I.4    Tanner, W.5
  • 17
    • 76049120802 scopus 로고    scopus 로고
    • Coupling between membrane curvature and lipid shape: Measurement of the curvature preference of fluorescently labeled phospholipids
    • Kamal, M. M., D. Mills, M. Grzybek, and J. Howard. 2009. Coupling between membrane curvature and lipid shape: measurement of the curvature preference of fluorescently labeled phospholipids. Proc. Natl. Acad. Sci. U. S. A. 106:22245-22250.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 22245-22250
    • Kamal, M.M.1    Mills, D.2    Grzybek, M.3    Howard, J.4
  • 18
    • 0038701655 scopus 로고    scopus 로고
    • Topology models for 37 Saccharomyces cerevisiae membrane proteins based on C-terminal reporter fusions and predictions
    • Kim, H., K. Melén, and G. von Heijne. 2003. Topology models for 37 Saccharomyces cerevisiae membrane proteins based on C-terminal reporter fusions and predictions. J. Biol. Chem. 278:10208-10213.
    • (2003) J. Biol. Chem. , vol.278 , pp. 10208-10213
    • Kim, H.1    Melén, K.2    von Heijne, G.3
  • 19
    • 0038236204 scopus 로고    scopus 로고
    • Determination of the membrane topology of Ost4p and its subunit interactions in the oligosaccharyltransferase complex in Saccharomyces cerevisiae
    • Kim, H., Q. Yan, G. von Heijne, G. A. Caputo, and W. J. Lennarz. 2003. Determination of the membrane topology of Ost4p and its subunit interactions in the oligosaccharyltransferase complex in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U. S. A. 100:7460-7464.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 7460-7464
    • Kim, H.1    Yan, Q.2    von Heijne, G.3    Caputo, G.A.4    Lennarz, W.J.5
  • 20
  • 21
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • Krogh, A., B. Larsson, G. von Heijne, and E. L. Sonnhammer. 2001. Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 305:567-580.
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    von Heijne, G.3    Sonnhammer, E.L.4
  • 23
    • 44849101230 scopus 로고    scopus 로고
    • The sphingolipid long-chain base-Pkh1/2-Ypk1/2 signaling pathway regulates eisosome assembly and turnover
    • Luo, G., A. Gruhler, Y. Liu, O. N. Jensen, and R. C. Dickson. 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
  • 24
    • 0025890946 scopus 로고
    • Influence of proline residues on protein conformation
    • MacArthur, M. W., and J. M. Thornton. 1991. Influence of proline residues on protein conformation. J. Mol. Biol. 218:397-412.
    • (1991) J. Mol. Biol. , vol.218 , pp. 397-412
    • MacArthur, M.W.1    Thornton, J.M.2
  • 25
    • 0345255797 scopus 로고    scopus 로고
    • Visualization of protein compartmentation within the plasma membrane of living yeast cells
    • Malínská, K., J. Malinsky, M. Opekarová, and W. Tanner. 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
    • Malínská, K.1    Malinsky, J.2    Opekarová, M.3    Tanner, W.4
  • 26
    • 12344298783 scopus 로고    scopus 로고
    • Distribution of Can1p into stable domains reflects lateral protein segregation within the plasma membrane of living S. cerevisiae cells
    • Malínská, K., J. Malinsky, M. Opekarová, and W. Tanner. 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
    • Malínská, K.1    Malinsky, J.2    Opekarová, M.3    Tanner, W.4
  • 27
    • 77956825202 scopus 로고    scopus 로고
    • The lateral compartmentation of the yeast plasma membrane
    • 14 April doi:10.1002/ yea
    • Malinsky, J., M. Opekarová, and W. Tanner. 14 April 2010. The lateral compartmentation of the yeast plasma membrane. Yeast doi:10.1002/ yea.1772.
    • (2010) Yeast , pp. 1772
    • Malinsky, J.1    Opekarová, M.2    Tanner, W.3
  • 28
    • 85010225704 scopus 로고
    • Fine structure in frozen-etched yeast cells
    • Moor, H., and K. Mühlethaler. 1963. Fine structure in frozen-etched yeast cells. J. Cell Biol. 17:609-628.
    • (1963) J. Cell Biol. , vol.17 , pp. 609-628
    • Moor, H.1    Mühlethaler, K.2
  • 30
    • 0012998399 scopus 로고    scopus 로고
    • The ultrastructure of Ignicoccus: Evidence for a novel outer membrane and for intracellular vesicle budding in an archaeon
    • Rachel, R., I. Wyschkony, S. Riehl, and H. Huber. 2002. The ultrastructure of Ignicoccus: evidence for a novel outer membrane and for intracellular vesicle budding in an archaeon. Archaea 1:9-18.
    • (2002) Archaea , vol.1 , pp. 9-18
    • Rachel, R.1    Wyschkony, I.2    Riehl, S.3    Huber, H.4
  • 31
    • 0030945486 scopus 로고    scopus 로고
    • Transmembrane domain-dependent sorting of proteins to the ER and plasma membrane in yeast
    • Rayner, J. C. and H. R. B. Pelham. 1997. Transmembrane domain-dependent sorting of proteins to the ER and plasma membrane in yeast. EMBO J. 16:1832-1841.
    • (1997) EMBO J. , vol.16 , pp. 1832-1841
    • Rayner, J.C.1    Pelham, H.R.B.2
  • 33
    • 0033605720 scopus 로고    scopus 로고
    • Transmembrane topology of Pmt1p, a member of an evolutionary conserved family of protein O-mannosyltransferases
    • Strahl-Bolsinger, S., and A. Scheinost. 1999. Transmembrane topology of Pmt1p, a member of an evolutionary conserved family of protein O-mannosyltransferases. J. Biol. Chem. 274:9068-9075.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9068-9075
    • Strahl-Bolsinger, S.1    Scheinost, A.2
  • 34
    • 0037447510 scopus 로고    scopus 로고
    • Screening and characterization of transposon-insertion mutants in a pseudohyphal strain of Saccharomyces cerevisiae
    • Suzuki, C., Y. Hori, and Y. Kashiwagi. 2003. Screening and characterization of transposon-insertion mutants in a pseudohyphal strain of Saccharomyces cerevisiae. Yeast 20:407-415.
    • (2003) Yeast , vol.20 , pp. 407-415
    • Suzuki, C.1    Hori, Y.2    Kashiwagi, Y.3
  • 35
    • 0023275830 scopus 로고
    • A family of yeast expression vectors containing the phage f1 intergenic region
    • Vernet, T., D. Dignard, and D.Y. Thomas. 1987. A family of yeast expression vectors containing the phage f1 intergenic region. Gene 52:225-233.
    • (1987) Gene , vol.52 , pp. 225-233
    • Vernet, T.1    Dignard, D.2    Thomas, D.Y.3
  • 37
    • 0034805876 scopus 로고    scopus 로고
    • Transmembrane domain length determines intracellular membrane compartment localization of syntaxins 3, 4, and 5
    • Watson, R. T., and J. E. Pessin. 2001. Transmembrane domain length determines intracellular membrane compartment localization of syntaxins 3, 4, and 5. Am. J. Physiol. Cell Physiol. 281:C215-C223.
    • (2001) Am. J. Physiol. Cell Physiol. , vol.281
    • Watson, R.T.1    Pessin, J.E.2
  • 38
    • 0025602520 scopus 로고
    • The influence of proline residues on alpha-helical structure
    • Woolfson, D. N., and D. H. Williams. 1990. The influence of proline residues on alpha-helical structure. FEBS Lett. 277:185-188.
    • (1990) FEBS Lett. , vol.277 , pp. 185-188
    • Woolfson, D.N.1    Williams, D.H.2
  • 39
    • 0025996871 scopus 로고
    • Proline in alpha-helix: Stability and conformation studied by dynamics simulation
    • Yun, R. H., A. Anderson, and J. Hermans. 1991. Proline in alpha-helix: stability and conformation studied by dynamics simulation. Proteins 10:219-228.
    • (1991) Proteins , vol.10 , pp. 219-228
    • Yun, R.H.1    Anderson, A.2    Hermans, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.