메뉴 건너뛰기




Volumn 3, Issue 10, 2002, Pages 730-739

An ER membrane protein, Sop4, facilitates ER export of the yeast plasma membrane [H+]ATPase, Pma1

Author keywords

ER export; Plasma membrane; Pma1; Protein targeting; Yeast

Indexed keywords

CARBOXYPEPTIDASE C; CELL PROTEIN; HYDROGEN POTASSIUM ADENOSINE TRIPHOSPHATASE; MEMBRANE PROTEIN; MUTANT PROTEIN; PHEROMONE; PROTEIN SOP4; UNCLASSIFIED DRUG;

EID: 0036787215     PISSN: 13989219     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1600-0854.2002.31005.x     Document Type: Article
Times cited : (25)

References (46)
  • 1
    • 0033521072 scopus 로고    scopus 로고
    • Setting the standards: Quality control in the secretory pathway
    • Ellgard L, Molinari M, Helenius A. Setting the standards: quality control in the secretory pathway. Science 1999;286:1882-1888.
    • (1999) Science , vol.286 , pp. 1882-1888
    • Ellgard, L.1    Molinari, M.2    Helenius, A.3
  • 2
    • 0031128320 scopus 로고    scopus 로고
    • ER-associated and proteasome-mediated protein degradation: How two topologically restricted events came together
    • Brodsky JL, McCracken AA. ER-associated and proteasome-mediated protein degradation: how two topologically restricted events came together. Trends Cell Biol 1997;7:151-156.
    • (1997) Trends Cell Biol , vol.7 , pp. 151-156
    • Brodsky, J.L.1    McCracken, A.A.2
  • 3
    • 0030700576 scopus 로고    scopus 로고
    • Endoplasmic reticulum degradation. reverse protein flow of no return
    • Sommer T, Wolf DH. Endoplasmic reticulum degradation. reverse protein flow of no return. FASEB J 1997;11:1227-1233.
    • (1997) FASEB J , vol.11 , pp. 1227-1233
    • Sommer, T.1    Wolf, D.H.2
  • 4
    • 0030949874 scopus 로고    scopus 로고
    • ER quality control: The cytoplasmic connection
    • Kopito R. ER quality control: the cytoplasmic connection. Cell 1997; 88:427-430,
    • (1997) Cell , vol.88 , pp. 427-430
    • Kopito, R.1
  • 5
    • 0033574678 scopus 로고    scopus 로고
    • A primer on vesicle budding
    • Springer S, Spang A, Schekman R. A primer on vesicle budding. Cell 1999;97:145-148.
    • (1999) Cell , vol.97 , pp. 145-148
    • Springer, S.1    Spang, A.2    Schekman, R.3
  • 6
    • 0034611009 scopus 로고    scopus 로고
    • The Emp24 complex recruits a specific cargo molecule into endoplasmic reticulum-derived vesicles
    • Muniz M, Nuoffer C, Hauri H-P, Riezman H. The Emp24 complex recruits a specific cargo molecule into endoplasmic reticulum-derived vesicles. J Cell Biol 2000;148:925-930.
    • (2000) J. Cell Biol , vol.148 , pp. 925-930
    • Muniz, M.1    Nuoffer, C.2    Hauri, H.-P.3    Riezman, H.4
  • 8
    • 0029831539 scopus 로고    scopus 로고
    • Amino acid permeases require COPII components and the ER resident membrane protein Shr3p for packaging into transport vesicles in vitro
    • Kuehn MJ, Schekman R, Ljungdahl P. Amino acid permeases require COPII components and the ER resident membrane protein Shr3p for packaging into transport vesicles in vitro. J Cell Biol 1996;135:585-595.
    • (1996) J. Cell Biol , vol.135 , pp. 585-595
    • Kuehn, M.J.1    Schekman, R.2    Ljungdahl, P.3
  • 9
    • 0033967340 scopus 로고    scopus 로고
    • Pho86p, an endoplasmic reticulum (ER) resident protein in Saccharomyces cerevisiae, is required for ER exit of the high-affinity phosphate transporter Pho84p
    • Lau W-TW, Howson RW, Malkus P, Schekman R, O'Shea E. Pho86p, an endoplasmic reticulum (ER) resident protein in Saccharomyces cerevisiae, is required for ER exit of the high-affinity phosphate transporter Pho84p. Proc Natl Acad Sci USA 2000;97:1107-1112.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1107-1112
    • Lau, W.-T.W.1    Howson, R.W.2    Malkus, P.3    Schekman, R.4    O'Shea, E.5
  • 10
    • 0033594914 scopus 로고    scopus 로고
    • Efficient export of the glucose transporter Hxtl p from the endoplasmic reticulum requires Gsf2p
    • Sherwood PW, Carlson M. Efficient export of the glucose transporter Hxtl p from the endoplasmic reticulum requires Gsf2p. Proc Natl Acad Sci USA 1999;96:7415-7420.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 7415-7420
    • Sherwood, P.W.1    Carlson, M.2
  • 11
    • 0029094253 scopus 로고
    • Quality control in the secretory pathway
    • Hammond C, Helenius A. Quality control in the secretory pathway. Curr Opin Cell Biol 1995;7:523-529.
    • (1995) Curr. Opin. Cell Biol , vol.7 , pp. 523-529
    • Hammond, C.1    Helenius, A.2
  • 12
    • 0029829005 scopus 로고    scopus 로고
    • A pathway for targeting soluble misfolded proteins to the yeast vacuole
    • Hong E, Davidson AR, Kaiser CA. A pathway for targeting soluble misfolded proteins to the yeast vacuole. J Cell Biol 1996;135:623-633.
    • (1996) J. Cell Biol , vol.135 , pp. 623-633
    • Hong, E.1    Davidson, A.R.2    Kaiser, C.A.3
  • 13
    • 0032941754 scopus 로고    scopus 로고
    • Yeast mutants affecting possible quality control of plasma membrane proteins
    • Li Y, Kane T, Tipper C, Spatrick P, Jenness DD. Yeast mutants affecting possible quality control of plasma membrane proteins. Mol Cell Biol 1999;19:3588-3599.
    • (1999) Mol. Cell Biol , vol.19 , pp. 3588-3599
    • Li, Y.1    Kane, T.2    Tipper, C.3    Spatrick, P.4    Jenness, D.D.5
  • 15
    • 0024024076 scopus 로고
    • Coincident localization of secretory and plasma membrane proteins in organelles of the yeast secretory pathway
    • Brada D, Schekman R. Coincident localization of secretory and plasma membrane proteins in organelles of the yeast secretory pathway. J Bacteriol 1988,170:2775-2783.
    • (1988) J. Bacteriol , vol.170 , pp. 2775-2783
    • Brada, D.1    Schekman, R.2
  • 16
    • 0026039784 scopus 로고
    • +]ATPase involves phosphorylation during intracellular transport
    • +]ATPase involves phosphorylation during intracellular transport. J Cell Biol 1991;115:289-295.
    • (1991) J. Cell Biol , vol.115 , pp. 289-295
    • Chang, A.1    Slayman, C.W.2
  • 18
    • 0031719958 scopus 로고    scopus 로고
    • Characterization of an allele-nonspecific intragenic suppressor in the yeast plasma membrane H+-ATPase gene (PMA1)
    • Maldonado AM, de la Fuente N, Portillo F. Characterization of an allele-nonspecific intragenic suppressor in the yeast plasma membrane H+-ATPase gene (PMA1). Genetics 1998;150:11-19.
    • (1998) Genetics , vol.150 , pp. 11-19
    • Maldonado, A.M.1    de la Fuente, N.2    Portillo, F.3
  • 20
    • 0033230434 scopus 로고    scopus 로고
    • Eps1, a novel PDI-related protein involved in ER quality control in yeast
    • Wang Q, Chang A. Eps1, a novel PDI-related protein involved in ER quality control in yeast. EMBO J 1999;18:5972-5982.
    • (1999) EMBO J , vol.18 , pp. 5972-5982
    • Wang, Q.1    Chang, A.2
  • 21
    • 0028795584 scopus 로고
    • +]ATPase: A novel gene AST1 prevents mislocalization of mutant ATPase to the vacuole
    • +]ATPase: a novel gene AST1 prevents mislocalization of mutant ATPase to the vacuole. J Cell Biol 1995;128:39-49.
    • (1995) J. Cell Biol , vol.128 , pp. 39-49
    • Chang, A.1    Fink, G.R.2
  • 22
    • 0030809534 scopus 로고    scopus 로고
    • Novel genes involved in endosomal traffic in yeast revealed by suppression of a targeting-defective plasma membrane ATPase mutant
    • Luo W-j, Chang A. Novel genes involved in endosomal traffic in yeast revealed by suppression of a targeting-defective plasma membrane ATPase mutant. J Cell Biol 1997;138:731-746.
    • (1997) J. Cell Biol , vol.138 , pp. 731-746
    • Luo, W.-J.1    Chang, A.2
  • 24
    • 0036270269 scopus 로고    scopus 로고
    • Plasma membrane biogenesis
    • Chang A. Plasma membrane biogenesis. Meth Enzymol 2002;351: 339-350.
    • (2002) Meth. Enzymol , vol.351 , pp. 339-350
    • Chang, A.1
  • 25
    • 0028586017 scopus 로고
    • Regulatable promoters of Saccharomyces cerevisiae: Comparison of transcriptional activity and their use for heterologous expression
    • Mumberg D, Muller R, Funk M. Regulatable promoters of Saccharomyces cerevisiae: comparison of transcriptional activity and their use for heterologous expression. Nucl Acids Res 1994;22:5767-5768.
    • (1994) Nucl. Acids Res , vol.22 , pp. 5767-5768
    • Mumberg, D.1    Muller, R.2    Funk, M.3
  • 26
    • 0033999819 scopus 로고    scopus 로고
    • An endosome-to-plasma membrane pathway involved in trafficking of a mutant plasma membrane ATPase in yeast
    • Luo W-j, Chang A. An endosome-to-plasma membrane pathway involved in trafficking of a mutant plasma membrane ATPase in yeast. Mol Biol Cell 2000;11:579-592.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 579-592
    • Luo, W.-J.1    Chang, A.2
  • 27
    • 0030069907 scopus 로고    scopus 로고
    • GPI anchor attachment is required for Gas1p transport from the endoplasmic reticulum in COPII vesicles
    • Doering TL, Schekman R. GPI anchor attachment is required for Gas1p transport from the endoplasmic reticulum in COPII vesicles. EMBO J 1996;15:182-191.
    • (1996) EMBO J , vol.15 , pp. 182-191
    • Doering, T.L.1    Schekman, R.2
  • 28
    • 0030665269 scopus 로고    scopus 로고
    • Specific requirements for the ER to Golgi transport of GPI-anchored proteins in yeast
    • Sutterlin C, Doering TL, Schimmoller F, Schroder S, Riezman H. Specific requirements for the ER to Golgi transport of GPI-anchored proteins in yeast. J Cell Sci 1997;110:2703-2714.
    • (1997) J. Cell Sci , vol.110 , pp. 2703-2714
    • Sutterlin, C.1    Doering, T.L.2    Schimmoller, F.3    Schroder, S.4    Riezman, H.5
  • 29
    • 0030808571 scopus 로고    scopus 로고
    • Elimination of defective α-factor pheromone receptors
    • Jenness DD, Li Y, Tipper C, Spatrick P. Elimination of defective α-factor pheromone receptors. Mol Cell Biol 1997;17:6236-6245.
    • (1997) Mol. Cell Biol , vol.17 , pp. 6236-6245
    • Jenness, D.D.1    Li, Y.2    Tipper, C.3    Spatrick, P.4
  • 30
    • 0030814254 scopus 로고    scopus 로고
    • COPII and secretory cargo capture into transport vesicles
    • Kuehn MJ, Schekman R. COPII and secretory cargo capture into transport vesicles. Curr Opin Cell Biol 1997,9:477-483.
    • (1997) Curr. Opin. Cell Biol , vol.9 , pp. 477-483
    • Kuehn, M.J.1    Schekman, R.2
  • 31
    • 0025094319 scopus 로고
    • An essential role for a phospholipid transfer protein in yeast Golgi function
    • Bankaitis V, Aitken J, Cleves A, Dowhan W. An essential role for a phospholipid transfer protein in yeast Golgi function. Nature 1990; 347:561-562.
    • (1990) Nature , vol.347 , pp. 561-562
    • Bankaitis, V.1    Aitken, J.2    Cleves, A.3    Dowhan, W.4
  • 32
    • 0029803610 scopus 로고    scopus 로고
    • Kes1p shares homology with human oxysterol binding protein and participates in a novel regulatory pathway for yeast Golgi-derived transport vesicle biogenesis
    • Fang M, Kearns BG, Gedvilaite A, Kagiwada S, Keorns M, Fung MKY, Bankatis VA. Kes1p shares homology with human oxysterol binding protein and participates in a novel regulatory pathway for yeast Golgi-derived transport vesicle biogenesis. EMBO J 1996;15:6447-6459.
    • (1996) EMBO J , vol.15 , pp. 6447-6459
    • Fang, M.1    Kearns, B.G.2    Gedvilaite, A.3    Kagiwada, S.4    Keorns, M.5    Fung, M.K.Y.6    Bankatis, V.A.7
  • 33
    • 0031127906 scopus 로고    scopus 로고
    • Synthetic leaders with potential BiP binding mediate high-yield secretion of correctly folded insulin precursors from Saccharomyces cerevisiae
    • Kjeldsen T, Pettersson AF, Hach M, Diers I, Havelund S, Hansen PH, Andersen AS. Synthetic leaders with potential BiP binding mediate high-yield secretion of correctly folded insulin precursors from Saccharomyces cerevisiae. Protein Expr Purif 1997;9:331-336.
    • (1997) Protein Expr. Purif , vol.9 , pp. 331-336
    • Kjeldsen, T.1    Pettersson, A.F.2    Hach, M.3    Diers, I.4    Havelund, S.5    Hansen, P.H.6    Andersen, A.S.7
  • 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 KJ, Crotwell M, Espenshade P, Gimeno R, Kaiser CA. LST1 is a SEC24 homologue used for selective export of the plasma membrane ATPase from the endoplasmic reticulum. J Cell Biol 1999;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
    • 0034646666 scopus 로고    scopus 로고
    • Evidence for overlapping and distinct functions in protein transport of coat protein Sec24p family members
    • Peng R, De Antoni A, Gallwitz D. Evidence for overlapping and distinct functions in protein transport of coat protein Sec24p family members. J Biol Chem 2000;275:11521-11528.
    • (2000) J. Biol. Chem , vol.275 , pp. 11521-11528
    • Peng, R.1    De Antoni, A.2    Gallwitz, D.3
  • 36
    • 0001352978 scopus 로고    scopus 로고
    • Post-translation control of Nramp metal transport in yeast
    • Liu XF, Culotta VC. Post-translation control of Nramp metal transport in yeast. J Biol Chem 1999;274:4863-4868.
    • (1999) J. Biol. Chem , vol.274 , pp. 4863-4868
    • Liu, X.F.1    Culotta, V.C.2
  • 37
    • 0035423555 scopus 로고    scopus 로고
    • ER export: Public transportation by the COPII coach
    • Antonny B, Schekman R. ER export: public transportation by the COPII coach. Curr Opin Cell Biol 2001;13:438-443.
    • (2001) Curr. Opin. Cell Biol , vol.13 , pp. 438-443
    • Antonny, B.1    Schekman, R.2
  • 39
    • 0036789925 scopus 로고    scopus 로고
    • Sphingoid base synthesis is required for oligomerization and cell surface stability of yeast plasma membrane ATPase, Pma1
    • in press
    • Wang Q, Chang A. Sphingoid base synthesis is required for oligomerization and cell surface stability of yeast plasma membrane ATPase, Pma1. Proc Natl Acad Sci 2002:in press.
    • (2002) Proc. Natl. Acad. Sci
    • Wang, Q.1    Chang, A.2
  • 40
    • 0025362445 scopus 로고
    • ERD2, a yeast gene required for the receptor-mediated retrieval of lumenal ER proteins from the secretory pathway
    • Semenza JC, Hardwick KG, Dean N, Pelham HR. ERD2, a yeast gene required for the receptor-mediated retrieval of lumenal ER proteins from the secretory pathway. Cell 1990;61:1349-1357.
    • (1990) Cell , vol.61 , pp. 1349-1357
    • Semenza, J.C.1    Hardwick, K.G.2    Dean, N.3    Pelham, H.R.4
  • 42
    • 0035979185 scopus 로고    scopus 로고
    • A mutant plasma membrane ATPase, Pma1-10, is defective in stability at the yeast cell surface
    • Gong X, Chang A. A mutant plasma membrane ATPase, Pma1-10, is defective in stability at the yeast cell surface. Proc Natl Acad Sci USA 2001;98:9104-9109.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 9104-9109
    • Gong, X.1    Chang, A.2
  • 44
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz D, St. Jean A, Woods RA, Schiestl RH. Improved method for high efficiency transformation of intact yeast cells. Nucl Acids Res 1992;20:1425.
    • (1992) Nucl. Acids Res , vol.20 , pp. 1425
    • Gietz, D.1    St. Jean, A.2    Woods, R.A.3    Schiestl, R.H.4
  • 45
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel TAJD, Roberts JD, Zakour RA. Rapid and efficient site-specific mutagenesis without phenotypic selection. Meth Enzymol 1987;154: 508-519.
    • (1987) Meth. Enzymol , vol.154 , pp. 508-519
    • Kunkel, T.A.J.D.1    Roberts, J.D.2    Zakour, R.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.