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Volumn 10, Issue 1, 2011, Pages 63-71

Hph1 and Hph2 are novel components of the Sec63/Sec62 posttranslational translocation complex that aid in vacuolar proton ATPase biogenesis

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; HEAT SHOCK PROTEIN; HPH1 PROTEIN, S CEREVISIAE; HPH2 PROTEIN, S CEREVISIAE; MULTIPROTEIN COMPLEX; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; SACCHAROMYCES CEREVISIAE PROTEIN; SEC62 PROTEIN, S CEREVISIAE; SEC63 PROTEIN, S CEREVISIAE; SIGNAL PEPTIDE;

EID: 78651477794     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.00241-10     Document Type: Article
Times cited : (14)

References (50)
  • 1
    • 0004270170 scopus 로고
    • Current protocols in molecular biology
    • John Wiley & Sons Inc: New York, NY
    • Ausubel, F. M. 1991. Current protocols in molecular biology. John Wiley & Sons Inc: New York, NY.
    • (1991)
    • Ausubel, F.M.1
  • 2
    • 0029954823 scopus 로고    scopus 로고
    • Functional interaction of cytosolic hsp70 and DnaJ-related protein, Ydj1, in protein translocation in vivo
    • Becker, J., W. Walter, W. Yan, and E. A. Craig. 1996. Functional interaction of cytosolic hsp70 and DnaJ-related protein, Ydj1, in protein translocation in vivo. Mol. Biol. Cell 16:4378-4386.
    • (1996) Mol. Biol. Cell , vol.16 , pp. 4378-4386
    • Becker, J.1    Walter, W.2    Yan, W.3    Craig, E.A.4
  • 3
    • 0037424360 scopus 로고    scopus 로고
    • Bipartite signals mediate subcellular targeting of tail-anchored membrane proteins in Saccharomyces cerevisiae
    • Beilharz, T., B. Egan, P. A. Silver, K. Hofmann, and T. Lithgow. 2003. Bipartite signals mediate subcellular targeting of tail-anchored membrane proteins in Saccharomyces cerevisiae. J. Biol. Chem. 278:8219-8223.
    • (2003) J. Biol. Chem , vol.278 , pp. 8219-8223
    • Beilharz, T.1    Egan, B.2    Silver, P.A.3    Hofmann, K.4    Lithgow, T.5
  • 4
    • 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., et al. 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
  • 5
    • 0742272120 scopus 로고    scopus 로고
    • A complete set of SNAREs in yeast
    • Burri, L., and T. Lithgow. 2004. A complete set of SNAREs in yeast. Traffic 5:45-52.
    • (2004) Traffic , vol.5 , pp. 45-52
    • Burri, L.1    Lithgow, T.2
  • 6
    • 0027102871 scopus 로고
    • YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism
    • Caplan, A. J., D. M. Cyr, and M. G. Douglas. 1992. YDJ1p facilitates polypeptide translocation across different intracellular membranes by a conserved mechanism. Cell 71:1143-1155.
    • (1992) Cell , vol.71 , pp. 1143-1155
    • Caplan, A.J.1    Cyr, D.M.2    Douglas, M.G.3
  • 7
    • 70349318145 scopus 로고    scopus 로고
    • Genomewide analysis reveals novel pathway affecting endoplasmic reticulum homeostasis, protein modification and quality control
    • Copic, A., et al. 2009. Genomewide analysis reveals novel pathway affecting endoplasmic reticulum homeostasis, protein modification and quality control. Genetics 182:757-769.
    • (2009) Genetics , vol.182 , pp. 757-769
    • Copic, A.1
  • 9
    • 0027324844 scopus 로고
    • Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase
    • Cox, J. S., C. E. Shamu, and P. Walter. 1993. Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell 73:1197-1206.
    • (1993) Cell , vol.73 , pp. 1197-1206
    • Cox, J.S.1    Shamu, C.E.2    Walter, P.3
  • 10
    • 0242355632 scopus 로고    scopus 로고
    • Calcineurin signaling in Saccharomyces cerevisiae: How yeast go crazy in response to stress
    • Cyert, M. S. 2003. Calcineurin signaling in Saccharomyces cerevisiae: how yeast go crazy in response to stress. Biochem. Biophys. Res. Commun. 311:1143-1150.
    • (2003) Biochem. Biophys. Res. Commun , vol.311 , pp. 1143-1150
    • Cyert, M.S.1
  • 11
    • 33846002764 scopus 로고    scopus 로고
    • PKR1 encodes an assembly factor for the yeast V-type ATPase
    • Davis-Kaplan, S. R., et al. 2006. PKR1 encodes an assembly factor for the yeast V-type ATPase. J. Biol. Chem. 281:32025-32035.
    • (2006) J. Biol. Chem , vol.281 , pp. 32025-32035
    • Davis-Kaplan, S.R.1
  • 12
    • 0024298711 scopus 로고
    • A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides
    • Deshaies, R. J., B. D. Koch, M. Werner-Washburne, E. A. Craig, and R. Schekman. 1988. A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides. Nature 332:800-805.
    • (1988) Nature , vol.332 , pp. 800-805
    • Deshaies, R.J.1    Koch, B.D.2    Werner-Washburne, M.3    Craig, E.A.4    Schekman, R.5
  • 13
    • 0025970051 scopus 로고
    • Assembly of the yeast Sec proteins involved in the translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex
    • Deshaies, R. J., S. L. Sanders, D. Feldheim, and R. Schekman. 1991. Assembly of the yeast Sec proteins involved in the translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex. Nature 349:806-808.
    • (1991) Nature , vol.349 , pp. 806-808
    • Deshaies, R.J.1    Sanders, S.L.2    Feldheim, D.3    Schekman, R.4
  • 14
    • 0023567026 scopus 로고
    • A yeast mutant defective at an early stage in import of secretory protein precursors into the edoplasmic reticulum
    • Deshaies, R. J., and R. Schekman. 1987. A yeast mutant defective at an early stage in import of secretory protein precursors into the edoplasmic reticulum. J. Cell Biol. 105:633-645.
    • (1987) J. Cell Biol , vol.105 , pp. 633-645
    • Deshaies, R.J.1    Schekman, R.2
  • 15
    • 57349114323 scopus 로고    scopus 로고
    • Nonapoptotic death of Saccharomyces cerevisiae cells that is stimulated by Hsp90 and inhibited by calcineurin and Cmk2 in response to endoplasmic reticulum stresses
    • Dudgeon, D. D., N. Zhang, O. O. Ositelu, H. Kim, and K. W. Cunningham. 2008. Nonapoptotic death of Saccharomyces cerevisiae cells that is stimulated by Hsp90 and inhibited by calcineurin and Cmk2 in response to endoplasmic reticulum stresses. Eukaryot. Cell 7:2037-2051.
    • (2008) Eukaryot. Cell , vol.7 , pp. 2037-2051
    • Dudgeon, D.D.1    Zhang, N.2    Ositelu, O.O.3    Kim, H.4    Cunningham, K.W.5
  • 16
    • 0027520458 scopus 로고
    • The yeast SSS1 gene is essential for secretory protein translocation and encodes a conserved protein of the endoplasmic reticulum
    • Esnault, Y., M. O. Blondel, R. J. Deshaies, R. Schekman, and F. Kepes. 1993. The yeast SSS1 gene is essential for secretory protein translocation and encodes a conserved protein of the endoplasmic reticulum. EMBO J. 12: 4083-4093.
    • (1993) EMBO J , vol.12 , pp. 4083-4093
    • Esnault, Y.1    Blondel, M.O.2    Deshaies, R.J.3    Schekman, R.4    Kepes, F.5
  • 17
    • 0028151096 scopus 로고
    • SSS1 encodes a stabilizing component of the Sec61 subcomplex of the yeast protein translocation apparatus
    • Esnault, Y., D. Feldheim, M. O. Blondel, R. Schekman, and F. Kepes. 1994. SSS1 encodes a stabilizing component of the Sec61 subcomplex of the yeast protein translocation apparatus. J. Cell Biol. 269:27478-27485.
    • (1994) J. Cell Biol , vol.269 , pp. 27478-27485
    • Esnault, Y.1    Feldheim, D.2    Blondel, M.O.3    Schekman, R.4    Kepes, F.5
  • 18
    • 0028088419 scopus 로고
    • Nonlethal sec71-1 and sec72-1 mutations eliminate proteins associated with the Sec63p-BiP complex from S. cerevisiae
    • Fang, H., and N. Green. 1994. Nonlethal sec71-1 and sec72-1 mutations eliminate proteins associated with the Sec63p-BiP complex from S. cerevisiae. Mol. Biol. Cell 5:933-942.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 933-942
    • Fang, H.1    Green, N.2
  • 19
    • 0028022701 scopus 로고
    • Sec72p contributes to the selective recognition of signal peptides by the secretory polypeptide translocation complex
    • Feldheim, D., and R. Schekman. 1994. Sec72p contributes to the selective recognition of signal peptides by the secretory polypeptide translocation complex. J. Cell Biol. 126:935-943.
    • (1994) J. Cell Biol , vol.126 , pp. 935-943
    • Feldheim, D.1    Schekman, R.2
  • 20
    • 0027507707 scopus 로고
    • Structural and functional characterization of Sec66p, a new subunit of the polypeptide translocation apparatus in the yeast endoplasmic reticulum
    • Feldheim, D., K. Yoshimura, A. Admon, and R. Schekman. 1993. Structural and functional characterization of Sec66p, a new subunit of the polypeptide translocation apparatus in the yeast endoplasmic reticulum. Mol. Biol. Cell 4:931-939.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 931-939
    • Feldheim, D.1    Yoshimura, K.2    Admon, A.3    Schekman, R.4
  • 21
    • 0142215475 scopus 로고    scopus 로고
    • Global analysis of protein expression in yeast
    • Ghaemmaghami, S., et al. 2003. Global analysis of protein expression in yeast. Nature 425:737-741.
    • (2003) Nature , vol.425 , pp. 737-741
    • Ghaemmaghami, S.1
  • 22
    • 0032514213 scopus 로고    scopus 로고
    • Assembly of the yeast vacuolar H+-ATPase occurs in the endoplasmic reticulum and requires a Vma12p/Vma22p assembly complex
    • Graham, L. A., K. J. Hill, and T. H. Stevens. 1998. Assembly of the yeast vacuolar H+-ATPase occurs in the endoplasmic reticulum and requires a Vma12p/Vma22p assembly complex. J. Cell Biol. 142:39-49.
    • (1998) J. Cell Biol , vol.142 , pp. 39-49
    • Graham, L.A.1    Hill, K.J.2    Stevens, T.H.3
  • 23
    • 0026531641 scopus 로고
    • Mutants in three novel complementation groups inhibit membrane protein insertion into and soluble protein translocation across the endoplasmic reticulum membrane of Saccharomyces cerevisiae
    • Green, N., H. Fang, and P. Walter. 1992. Mutants in three novel complementation groups inhibit membrane protein insertion into and soluble protein translocation across the endoplasmic reticulum membrane of Saccharomyces cerevisiae. J. Cell Biol. 116:597-604.
    • (1992) J. Cell Biol , vol.116 , pp. 597-604
    • Green, N.1    Fang, H.2    Walter, P.3
  • 24
    • 2942633721 scopus 로고    scopus 로고
    • Hph1p and Hph2p, novel components of calcineurin-mediated stress responses in Saccharomyces cerevisiae
    • Heath, V. L., S. L. Shaw, S. Roy, and M. S. Cyert. 2004. Hph1p and Hph2p, novel components of calcineurin-mediated stress responses in Saccharomyces cerevisiae. Eukaryot. Cell 3:695-704.
    • (2004) Eukaryot. Cell , vol.3 , pp. 695-704
    • Heath, V.L.1    Shaw, S.L.2    Roy, S.3    Cyert, M.S.4
  • 25
    • 48249151759 scopus 로고    scopus 로고
    • The concept of translocation regulation
    • Hegde, R. S., and S. W. Kang. 2008. The concept of translocation regulation. J. Cell Biol. 182:225-232.
    • (2008) J. Cell Biol , vol.182 , pp. 225-232
    • Hegde, R.S.1    Kang, S.W.2
  • 26
    • 0034651604 scopus 로고    scopus 로고
    • Degradation of unassembled Vph1p reveals novel aspects of the yeast ER quality control system
    • Hill, K. C., and A. Anthony. 2000. Degradation of unassembled Vph1p reveals novel aspects of the yeast ER quality control system. EMBO J. 19:550-561.
    • (2000) EMBO J , vol.19 , pp. 550-561
    • Hill, K.C.1    Anthony, A.2
  • 27
    • 0028109216 scopus 로고
    • Vma21p is a yeast membrane protein retained in the endoplasmic reticulum by a di-lysine motif and is required for the assembly of the vacuolar H()-ATPase complex
    • Hill, K. J., and T. H. Stevens. 1994. Vma21p is a yeast membrane protein retained in the endoplasmic reticulum by a di-lysine motif and is required for the assembly of the vacuolar H()-ATPase complex. Mol. Biol. Cell 5:1039-1050.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 1039-1050
    • Hill, K.J.1    Stevens, T.H.2
  • 28
    • 0030845189 scopus 로고    scopus 로고
    • Vma12 encodes a yeast endoplasmic reticulum protein required for vacuolar Hδ-ATPase assembl
    • Jackson, D. D., and T. H. Stevens. 1997. Vma12 encodes a yeast endoplasmic reticulum protein required for vacuolar Hδ-ATPase assembly. J. Biol. Chem. 272:25928-25934.
    • (1997) J. Biol. Chem , vol.272 , pp. 25928-25934
    • Jackson, D.D.1    Stevens, T.H.2
  • 29
    • 33645119556 scopus 로고    scopus 로고
    • The where, when, and how of organelle acidification by the yeast vacuolar H+-ATPase
    • Kane, P. M. 2006. The where, when, and how of organelle acidification by the yeast vacuolar H+-ATPase. Microbiol. Mol. Biol. Rev. 70:177-191.
    • (2006) Microbiol. Mol. Biol. Rev , vol.70 , pp. 177-191
    • Kane, P.M.1
  • 30
    • 0035861664 scopus 로고    scopus 로고
    • The amino-terminal domain of the vacuolar proton-translocating ATPase a subunit controls targeting and in vivo dissociation, and the carboxyl-terminal domain affects coupling of proton transport and ATP hydrolysis
    • Kawasaki-Nishi, S., K. Bowers, T. Nishi, M. Forgac, and T. H. Stevens. 2001. The amino-terminal domain of the vacuolar proton-translocating ATPase a subunit controls targeting and in vivo dissociation, and the carboxyl-terminal domain affects coupling of proton transport and ATP hydrolysis. J. Biol. Chem. 276:47411-47420.
    • (2001) J. Biol. Chem , vol.276 , pp. 47411-47420
    • Kawasaki-Nishi, S.1    Bowers, K.2    Nishi, T.3    Forgac, M.4    Stevens, T.H.5
  • 31
    • 0028224791 scopus 로고
    • STV1 gene encodes functional homologue of 95-kDa yeast vacuolar H(+)-ATPase subunit Vph1p
    • Manolson, M. F., et al. 1994. STV1 gene encodes functional homologue of 95-kDa yeast vacuolar H(+)-ATPase subunit Vph1p. J. Biol. Chem. 269: 14064-14074.
    • (1994) J. Biol. Chem , vol.269 , pp. 14064-14074
    • Manolson, M.F.1
  • 32
    • 34147107933 scopus 로고    scopus 로고
    • Loss of vacuolar proton-translocatin ATPase activity in yeast results in chronic oxidative stress
    • Milgrom, E., H. Diab, F. Middleton, and P. M. Kane. 2007. Loss of vacuolar proton-translocatin ATPase activity in yeast results in chronic oxidative stress. J. Biol. Chem. 282:7125-7136.
    • (2007) J. Biol. Chem , vol.282 , pp. 7125-7136
    • Milgrom, E.1    Diab, H.2    Middleton, F.3    Kane, P.M.4
  • 33
    • 24744436626 scopus 로고    scopus 로고
    • Large-scale identification of yeast integral membrane protein interactions
    • Miller, J. P., et al. 2005. Large-scale identification of yeast integral membrane protein interactions. Proc. Natl. Acad. Sci. U. S. A. 102:12123-12128.
    • (2005) Proc. Natl. Acad. Sci. U. S. A , vol.102 , pp. 12123-12128
    • Miller, J.P.1
  • 34
    • 0029952547 scopus 로고    scopus 로고
    • Signal sequences specify the targeting route to the endoplasmic reticulum membrane
    • Ng, D. T., J. D. Brown, and P. Walter. 1996. Signal sequences specify the targeting route to the endoplasmic reticulum membrane. J. Cell Biol. 134: 269-278.
    • (1996) J. Cell Biol , vol.134 , pp. 269-278
    • Ng, D.T.1    Brown, J.D.2    Walter, P.3
  • 35
    • 77958046490 scopus 로고    scopus 로고
    • {alpha}- Arrestins Aly1 and Aly2 regulate intracellular trafficking in response to nutrient signaling
    • O'Donnell, A. F., A. Apffel, R. G. Gardner, and M. S. Cyert. 2010. {alpha}- Arrestins Aly1 and Aly2 regulate intracellular trafficking in response to nutrient signaling. Mol Biol Cell 21:3552-3566.
    • (2010) Mol Biol Cell , vol.21 , pp. 3552-3566
    • O'Donnell, A.F.1    Apffel, A.2    Gardner, R.G.3    Cyert, M.S.4
  • 36
    • 34548496285 scopus 로고    scopus 로고
    • Inhibiting endoplasmic reticulum (ER)-associated degradation of misfolded Yor1p does not permit ER export despite the presence of a diacidic sorting signal
    • Pagant, S., L. Kung, M. Dorrington, M. C. S. Lee, and E. A. Miller. 2007. Inhibiting endoplasmic reticulum (ER)-associated degradation of misfolded Yor1p does not permit ER export despite the presence of a diacidic sorting signal. Mol. Biol. Cell 18:3398-3413.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3398-3413
    • Pagant, S.1    Kung, L.2    Dorrington, M.3    Lee, M.C.S.4    Miller, E.A.5
  • 37
    • 18844387083 scopus 로고    scopus 로고
    • Signal recognition particles in chloroplasts, bacteria, yeast, and mammals
    • Pool, M. R. 2005. Signal recognition particles in chloroplasts, bacteria, yeast, and mammals. Mol. Membr. Biol. 22:3-15.
    • (2005) Mol. Membr. Biol , vol.22 , pp. 3-15
    • Pool, M.R.1
  • 39
    • 61649121557 scopus 로고    scopus 로고
    • A conserved docking surface on calcineurin mediates interaction with substrates and immunosuppressants
    • Rodríguez, A., et al. 2009. A conserved docking surface on calcineurin mediates interaction with substrates and immunosuppressants. Mol. Cell 33: 616-626.
    • (2009) Mol. Cell , vol.33 , pp. 616-626
    • Rodríguez, A.1
  • 40
    • 59449088040 scopus 로고    scopus 로고
    • Voa1p functions in V-ATPase assembly in the yeast endoplasmic reticulum
    • Ryan, M., L. A. Graham, and T. H. Stevens. 2008. Voa1p functions in V-ATPase assembly in the yeast endoplasmic reticulum. Mol. Biol. Cell 19:5131-5142.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 5131-5142
    • Ryan, M.1    Graham, L.A.2    Stevens, T.H.3
  • 41
    • 0026589260 scopus 로고
    • Sec61p and BiP directly facilitate polypeptide translocation into the ER
    • Sanders, S. L., K. M. Whitfield, J. P. Vogel, M. D. Rose, and R. W. Schekman. 1992. Sec61p and BiP directly facilitate polypeptide translocation into the ER. Cell 69:353-365.
    • (1992) Cell , vol.69 , pp. 353-365
    • Sanders, S.L.1    Whitfield, K.M.2    Vogel, J.P.3    Rose, M.D.4    Schekman, R.W.5
  • 42
    • 0035067367 scopus 로고    scopus 로고
    • Skp1 forms multiple protein complexes, including RAVE, a regulator of VATPase assembly
    • Seol, J. H., A. Shevchenko, A. Shevchenko, and R. J. Deshaies. 2001. Skp1 forms multiple protein complexes, including RAVE, a regulator of VATPase assembly. Nat. Cell Biol. 3:384-391.
    • (2001) Nat. Cell Biol , vol.3 , pp. 384-391
    • Seol, J.H.1    Shevchenko, A.2    Shevchenko, A.3    Deshaies, R.J.4
  • 43
    • 0025978949 scopus 로고
    • Getting started with yeast
    • Sherman, F. 1991. Getting started with yeast. Methods Enzymol. 194:3-21.
    • (1991) Methods Enzymol , vol.194 , pp. 3-21
    • Sherman, F.1
  • 44
    • 0029937560 scopus 로고    scopus 로고
    • Yeast protein translocation complex: Isolation of two genes SEB1 and SEB2 encoding proteins homologous to the Sec61 beta subunit
    • Toikkanen, J., et al. 1996. Yeast protein translocation complex: isolation of two genes SEB1 and SEB2 encoding proteins homologous to the Sec61 beta subunit. Yeast 12:425-438.
    • (1996) Yeast , vol.12 , pp. 425-438
    • Toikkanen, J.1
  • 45
    • 0034724520 scopus 로고    scopus 로고
    • Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation
    • Travers, K. J., et al. 2000. Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation. Cell 101:249-258.
    • (2000) Cell , vol.101 , pp. 249-258
    • Travers, K.J.1
  • 46
    • 14944361914 scopus 로고    scopus 로고
    • Protein kinase CK2 phosphorylates Sec63p to stimulate the assembly of the endoplasmic reticulum protein translocation apparatus
    • Wang, X., and N. Johnsson. 2005. Protein kinase CK2 phosphorylates Sec63p to stimulate the assembly of the endoplasmic reticulum protein translocation apparatus. J. Cell Sci. 118:723-732.
    • (2005) J. Cell Sci , vol.118 , pp. 723-732
    • Wang, X.1    Johnsson, N.2
  • 47
    • 0037472522 scopus 로고    scopus 로고
    • Identification of novel protein-protein interactions at the cytosolic surface of the Sec63 complex in the yeast ER membrane
    • Willer, M., A. J. Jermy, B. P. Young, and C. J. Stirling. 2003. Identification of novel protein-protein interactions at the cytosolic surface of the Sec63 complex in the yeast ER membrane. Yeast 20:133-148.
    • (2003) Yeast , vol.20 , pp. 133-148
    • Willer, M.1    Jermy, A.J.2    Young, B.P.3    Stirling, C.J.4
  • 48
    • 77953306152 scopus 로고    scopus 로고
    • Yet1p and Yet3p, the yeast homologs of BAP29 and BAP31, interact with the endoplasmic reticulum translocation apparatus and are required for inositol prototrophy
    • Wilson, J. D., and C. Barlowe. 2010. Yet1p and Yet3p, the yeast homologs of BAP29 and BAP31, interact with the endoplasmic reticulum translocation apparatus and are required for inositol prototrophy. J. Biol. Chem. 285: 18252-18261.
    • (2010) J. Biol. Chem , vol.285 , pp. 18252-18261
    • Wilson, J.D.1    Barlowe, C.2
  • 49
    • 0037163129 scopus 로고    scopus 로고
    • Genome-wide analysis of gene expression regulated by the calcineurin/Crz1p signaling pathway in Saccharomyces cerevisiae
    • Yoshimoto, H., et al. 2002. Genome-wide analysis of gene expression regulated by the calcineurin/Crz1p signaling pathway in Saccharomyces cerevisiae. J. Biol. Chem. 277:31079-31088.
    • (2002) J. Biol. Chem , vol.277 , pp. 31079-31088
    • Yoshimoto, H.1
  • 50
    • 78651521169 scopus 로고    scopus 로고
    • Protein translocation across the ER membrane
    • doi: 10.1016/j.bbamem.2010.06.016
    • Zimmermann, R., S. Eyrisch, M. Ahmad, and V. Helms. 2010. Protein translocation across the ER membrane. Biochim. Biophys. Acta. doi: 10.1016/j.bbamem.2010.06.016.
    • (2010) Biochim. Biophys. Acta
    • Zimmermann, R.1    Eyrisch, S.2    Ahmad, M.3    Helms, V.4


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