메뉴 건너뛰기




Volumn 6, Issue , 2006, Pages 967-983

ER-associated degradation of membrane proteins in yeast

Author keywords

ABC transporters; ER associated degradation (ERAD); Plasma membrane H+ ATPase; Proteasome; Quality control system; Ubiquitin; Yeast

Indexed keywords

ADENOSINE TRIPHOSPHATE; MEMBRANE PROTEIN; PROTEASOME; PROTEIN CDC48P; PROTEIN COP2; PROTEIN NPL4P; PROTEIN SAR1P; PROTEIN SUBUNIT; PROTEIN UFD1P; UNCLASSIFIED DRUG;

EID: 33747734734     PISSN: None     EISSN: 1537744X     Source Type: Journal    
DOI: 10.1100/tsw.2006.191     Document Type: Review
Times cited : (3)

References (141)
  • 1
    • 0029872276 scopus 로고    scopus 로고
    • Coat proteins and vesicle budding
    • Schekman, R. and Orci, L. (1996) Coat proteins and vesicle budding. Science 27, 1526-1533.
    • (1996) Science , vol.27 , pp. 1526-1533
    • Schekman, R.1    Orci, L.2
  • 2
  • 3
    • 0742272120 scopus 로고    scopus 로고
    • A complete set of SNAREs in yeast
    • Burri, L. and Lithgow, T. (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
  • 4
    • 0037459076 scopus 로고    scopus 로고
    • Membrane fusion
    • Jahn, R., Lang, T., and Südhof, T.C. (2003) Membrane fusion. Cell 112, 519-533.
    • (2003) Cell , vol.112 , pp. 519-533
    • Jahn, R.1    Lang, T.2    Südhof, T.C.3
  • 6
    • 0041526467 scopus 로고    scopus 로고
    • Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles
    • Miller, E.A., Beilharz, T.H., Malkus, P.N., Lee, M.C., Hamamoto, S., Orci, L., and Schekman, R. (2003) Multiple cargo binding sites on the COPII subunit Sec24p ensure capture of diverse membrane proteins into transport vesicles. Cell 114, 497-509.
    • (2003) Cell , vol.114 , pp. 497-509
    • Miller, E.A.1    Beilharz, T.H.2    Malkus, P.N.3    Lee, M.C.4    Hamamoto, S.5    Orci, L.6    Schekman, R.7
  • 7
    • 0043029286 scopus 로고    scopus 로고
    • SNARE selectivity of the COPII coat
    • Mossessova, E., Bickford, L.C., and Goldberg, J. (2003) SNARE selectivity of the COPII coat. Cell 114, 483-495.
    • (2003) Cell , vol.114 , pp. 483-495
    • Mossessova, E.1    Bickford, L.C.2    Goldberg, J.3
  • 8
    • 0037144576 scopus 로고    scopus 로고
    • Identification of interdependent signals required for anterograde traffic of the ATP-binding cassette transporter protein Yor1p
    • Epping, E.A. and Moye-Rowley, W.S. (2002) Identification of interdependent signals required for anterograde traffic of the ATP-binding cassette transporter protein Yor1p. J. Biol. Chem. 277, 34860-34869.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34860-34869
    • Epping, E.A.1    Moye-Rowley, W.S.2
  • 9
    • 0347723909 scopus 로고    scopus 로고
    • Reconstitution of coat protein complex II (COPII) vesicle formation from cargo-reconstituted proteoliposomes reveals the potential role of GTP hydrolysis by Sar1p in protein sorting
    • Sato, K. and Nakano, A. (2004) Reconstitution of coat protein complex II (COPII) vesicle formation from cargo-reconstituted proteoliposomes reveals the potential role of GTP hydrolysis by Sar1p in protein sorting. J. Biol. Chem. 279, 1330-1335.
    • (2004) J. Biol. Chem. , vol.279 , pp. 1330-1335
    • Sato, K.1    Nakano, A.2
  • 10
    • 3142624697 scopus 로고    scopus 로고
    • Differential ER exit in yeast and mammalian cells
    • Watanabe, R. and Riezman, H. (2004) Differential ER exit in yeast and mammalian cells. Curr. Opin. Cell Biol. 16, 350-355.
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 350-355
    • Watanabe, R.1    Riezman, H.2
  • 12
    • 0026555196 scopus 로고
    • Molecular dissection of the secretory pathway
    • Rothman, J.E. and Orci, L. (1992) Molecular dissection of the secretory pathway. Nature 30, 409-415.
    • (1992) Nature , vol.30 , pp. 409-415
    • Rothman, J.E.1    Orci, L.2
  • 13
    • 0033950864 scopus 로고    scopus 로고
    • Turning on ARF: The Sec7 family of guanine-nucleotide-exchange factors
    • Jackson, C.L. and Casanova, J.E. (2000) Turning on ARF: the Sec7 family of guanine-nucleotide-exchange factors. Trends Cell Biol. 10, 60-67.
    • (2000) Trends Cell Biol. , vol.10 , pp. 60-67
    • Jackson, C.L.1    Casanova, J.E.2
  • 14
    • 0033574678 scopus 로고    scopus 로고
    • A primer on vesicle budding
    • Springer, S., Spang, A., and Schekman, R. (1999) A primer on vesicle budding. Cell 97,145-148.
    • (1999) Cell , vol.97 , pp. 145-148
    • Springer, S.1    Spang, A.2    Schekman, R.3
  • 15
    • 0035172344 scopus 로고    scopus 로고
    • The ADP ribosylation factor-nucleotide exchange factors Gea1p and Gea2p have overlapping, but not redundant functions in retrograde transport from the Golgi to the endoplasmic reticulum
    • Spang, A., Herrmann, J.M., Hamamoto, S., and Schekman, R. (2001) The ADP ribosylation factor-nucleotide exchange factors Gea1p and Gea2p have overlapping, but not redundant functions in retrograde transport from the Golgi to the endoplasmic reticulum. Mol. Biol. Cell 12, 1035-1045.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1035-1045
    • Spang, A.1    Herrmann, J.M.2    Hamamoto, S.3    Schekman, R.4
  • 16
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard, L. and Helenius, A. (2003) Quality control in the endoplasmic reticulum. Nat. Rev. Mol. Cell Biol. 4, 181-191.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 17
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg, A.L. (2003) Protein degradation and protection against misfolded or damaged proteins. Nature 246, 895-899.
    • (2003) Nature , vol.246 , pp. 895-899
    • Goldberg, A.L.1
  • 18
    • 0037566901 scopus 로고    scopus 로고
    • For whom the bell tolls: Protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection
    • Kostova, Z. and Wolf, D.H. (2003) For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection. EMBO J. 22, 2309-2317.
    • (2003) EMBO J. , vol.22 , pp. 2309-2317
    • Kostova, Z.1    Wolf, D.H.2
  • 19
    • 0031008564 scopus 로고    scopus 로고
    • The hsp70 homologue Lhs1p is involved in a novel function of the yeast endoplasmic reticulum, refolding and stabilization of heat-denatured protein aggregates
    • Saris, N., Holkeri, H., Craven, R.A., Stirling, C.J., and Makarow, M. (1997) The hsp70 homologue Lhs1p is involved in a novel function of the yeast endoplasmic reticulum, refolding and stabilization of heat-denatured protein aggregates. J. Cell Biol. 137, 813-824.
    • (1997) J. Cell Biol. , vol.137 , pp. 813-824
    • Saris, N.1    Holkeri, H.2    Craven, R.A.3    Stirling, C.J.4    Makarow, M.5
  • 20
    • 0024338964 scopus 로고
    • KAR2, a karyogamy gene, is the yeast homolog of the mammalian BIP/GRP78 gene
    • Rose, M.D., Misra, L.M., and Vogel, J.P. (1989) KAR2, a karyogamy gene, is the yeast homolog of the mammalian BIP/GRP78 gene. Cell 57, 1211-1221.
    • (1989) Cell , vol.57 , pp. 1211-1221
    • Rose, M.D.1    Misra, L.M.2    Vogel, J.P.3
  • 21
    • 0024395160 scopus 로고
    • S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP
    • Normington, K., Kohno, K., Kozutsumi, Y., Gething, M.J., and Sambrook, J. (1989) S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP. Cell 57, 1223-1236.
    • (1989) Cell , vol.57 , pp. 1223-1236
    • Normington, K.1    Kohno, K.2    Kozutsumi, Y.3    Gething, M.J.4    Sambrook, J.5
  • 22
    • 32244441705 scopus 로고    scopus 로고
    • Pbn1p: An essential endoplasmic reticulum membrane protein required for protein processing in the endoplasmic reticulum of budding yeast
    • Subramanian S., Woolford, C.A., Drill, E., Lu, M., and Jones, E.W. (2006) Pbn1p: an essential endoplasmic reticulum membrane protein required for protein processing in the endoplasmic reticulum of budding yeast. Proc. Natl. Acad. Sci. U. S. A. 103, 939-944.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 939-944
    • Subramanian, S.1    Woolford, C.A.2    Drill, E.3    Lu, M.4    Jones, E.W.5
  • 24
    • 31044452359 scopus 로고    scopus 로고
    • Generating disulfide enzymatically: Reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p
    • Gross, E., Sevier, C.S., Heldman, N., Vitu, E., Bentzur, M., Kaiser, C.A., Thorpe, C., and Fass, D. (2006) Generating disulfide enzymatically: reaction products and electron acceptors of the endoplasmic reticulum thiol oxidase Ero1p. Proc. Natl. Acad. Sci. U. S. A. 103, 299-304.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 299-304
    • Gross, E.1    Sevier, C.S.2    Heldman, N.3    Vitu, E.4    Bentzur, M.5    Kaiser, C.A.6    Thorpe, C.7    Fass, D.8
  • 25
    • 0030692139 scopus 로고    scopus 로고
    • All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae
    • Dolinski, K., Muir, S., Cardenas, M., and Heitman, J. (1997) All cyclophilins and FK506 binding proteins are, individually and collectively, dispensable for viability in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U. S. A. 94, 13093-13098.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 13093-13098
    • Dolinski, K.1    Muir, S.2    Cardenas, M.3    Heitman, J.4
  • 27
    • 0033611127 scopus 로고    scopus 로고
    • Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase
    • Gillece, P., Luz, J.M., Lennarz, W.J., de La Cruz, F.J., and Romisch, K. (1999) Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase. J. Cell Biol. 147, 1443-1456.
    • (1999) J. Cell Biol. , vol.147 , pp. 1443-1456
    • Gillece, P.1    Luz, J.M.2    Lennarz, W.J.3    De La Cruz, F.J.4    Romisch, K.5
  • 28
    • 0033230434 scopus 로고    scopus 로고
    • Eps1, a novel PDI-related protein involved in ER quality control in yeast
    • Wang, Q. and Chang, A. (1999) Eps1, a novel PDI-related protein involved in ER quality control in yeast. EMBO J. 18, 5972-5982.
    • (1999) EMBO J. , vol.18 , pp. 5972-5982
    • Wang, Q.1    Chang, A.2
  • 29
    • 0035660414 scopus 로고    scopus 로고
    • Effects of calnexin deletion in Saccharomyces cerevisiae on the secretion of glycosylated lysozymes
    • Song, Y., Sata, J., Saito, A., Usui, M., Azakami, H., and Kato, A. (2001) Effects of calnexin deletion in Saccharomyces cerevisiae on the secretion of glycosylated lysozymes. J. Biochem. (Tokyo) 130, 757-764.
    • (2001) J. Biochem. (Tokyo) , vol.130 , pp. 757-764
    • Song, Y.1    Sata, J.2    Saito, A.3    Usui, M.4    Azakami, H.5    Kato, A.6
  • 30
    • 3042838324 scopus 로고    scopus 로고
    • Expression and characterization of Saccharomyces cerevisiae Cne1p, a calnexin homologue
    • Xu, X., Kanbara, K., Azakami, H., and Kato, A. (2004) Expression and characterization of Saccharomyces cerevisiae Cne1p, a calnexin homologue. J. Biochem. (Tokyo) 135, 615-618.
    • (2004) J. Biochem. (Tokyo) , vol.135 , pp. 615-618
    • Xu, X.1    Kanbara, K.2    Azakami, H.3    Kato, A.4
  • 31
    • 0035937853 scopus 로고    scopus 로고
    • Mnl1p, an alpha-mannosidase-like protein in yeast Saccharomyces cerevisiae, is required for endoplasmic reticulum-associated degradation of glycoproteins
    • Nakatsukasa, K., Nishikawa, S., Hosokawa, N., Nagata, K., and Endo, T. (2001) Mnl1p, an alpha-mannosidase-like protein in yeast Saccharomyces cerevisiae, is required for endoplasmic reticulum-associated degradation of glycoproteins. J. Biol. Chem. 276, 8635-8638.
    • (2001) J. Biol. Chem. , vol.276 , pp. 8635-8638
    • Nakatsukasa, K.1    Nishikawa, S.2    Hosokawa, N.3    Nagata, K.4    Endo, T.5
  • 33
    • 24944478240 scopus 로고    scopus 로고
    • Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD
    • Szathmary, R., Bielmann, R., Nita-Lazar, M., Burda, P., and Jakob, C.A. (2005) Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD. Mol. Cell 19, 765-775.
    • (2005) Mol. Cell , vol.19 , pp. 765-775
    • Szathmary, R.1    Bielmann, R.2    Nita-Lazar, M.3    Burda, P.4    Jakob, C.A.5
  • 34
    • 24944583185 scopus 로고    scopus 로고
    • Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor of misfolded glycoproteins in the ER lumen
    • Bhamidipati, A., Denic, V., Quan, E.M., and Weissman, J.S. (2005) Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor of misfolded glycoproteins in the ER lumen. Mol. Cell 19, 741-751.
    • (2005) Mol. Cell , vol.19 , pp. 741-751
    • Bhamidipati, A.1    Denic, V.2    Quan, E.M.3    Weissman, J.S.4
  • 35
    • 0036270698 scopus 로고    scopus 로고
    • Retro-translocation of proteins from the endoplasmic reticulum into the cytosol
    • Tsai, B., Ye, Y., and Rapoport, T.A. (2002) Retro-translocation of proteins from the endoplasmic reticulum into the cytosol. Nat. Rev. Mol. Cell Biol. 3, 246-255.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 246-255
    • Tsai, B.1    Ye, Y.2    Rapoport, T.A.3
  • 36
    • 0037769904 scopus 로고    scopus 로고
    • Stress tolerance of misfolded carboxypeptidase Y requires maintenance of protein trafficking and degradative pathways
    • Spear, E.D. and Ng, D.T. (2003) Stress tolerance of misfolded carboxypeptidase Y requires maintenance of protein trafficking and degradative pathways. Mol. Biol. Cell 14, 2756-2767.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2756-2767
    • Spear, E.D.1    Ng, D.T.2
  • 37
    • 0036843023 scopus 로고    scopus 로고
    • Secretory pathway quality control operating in Golgi, plasmalemma, and endosomal systems
    • Arvan, P., Zhao, X., Ramos-Castaneda, J., and Chang, A. (2002) Secretory pathway quality control operating in Golgi, plasmalemma, and endosomal systems. Traffic 3, 771-780.
    • (2002) Traffic , vol.3 , pp. 771-780
    • Arvan, P.1    Zhao, X.2    Ramos-Castaneda, J.3    Chang, A.4
  • 38
    • 0029829005 scopus 로고    scopus 로고
    • A pathway for targeting soluble misfolded proteins to the yeast vacuole
    • Hong, E., Davidson, A.R., and Kaiser, C.A. (1996) A pathway for targeting soluble misfolded proteins to the yeast vacuole. J. Cell Biol. 135, 623-633.
    • (1996) J. Cell Biol. , vol.135 , pp. 623-633
    • Hong, E.1    Davidson, A.R.2    Kaiser, C.A.3
  • 39
    • 0038785977 scopus 로고    scopus 로고
    • Ligand recognition and domain structure of Vps10, a vacuolar protein sorting receptor in Saccharomyces cerevisiae
    • Jorgensen, M.U., Emr, S.D., and Winther, J.R. (1999) Ligand recognition and domain structure of Vps10, a vacuolar protein sorting receptor in Saccharomyces cerevisiae. Eur. J. Biochem. 260, 461-469.
    • (1999) Eur. J. Biochem. , vol.260 , pp. 461-469
    • Jorgensen, M.U.1    Emr, S.D.2    Winther, J.R.3
  • 40
    • 0036166924 scopus 로고    scopus 로고
    • A transmembrane ubiquitin ligase required to sort membrane proteins into multivesicular bodies
    • Reggiori, F. and Pelham, H.R. (2002) A transmembrane ubiquitin ligase required to sort membrane proteins into multivesicular bodies. Nat. Cell Biol. 4, 117-123.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 117-123
    • Reggiori, F.1    Pelham, H.R.2
  • 41
    • 0028971506 scopus 로고
    • NPI1, an essential yeast gene involved in induced degradation of Gap1 and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase
    • Hein, C., Springael, J.Y., Volland, C., Haguenauer-Tsapis, R., and André, B. (1995) NPI1, an essential yeast gene involved in induced degradation of Gap1 and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase. Mol. Microbiol. 18, 77-87.
    • (1995) Mol. Microbiol. , vol.18 , pp. 77-87
    • Hein, C.1    Springael, J.Y.2    Volland, C.3    Haguenauer-Tsapis, R.4    André, B.5
  • 42
    • 15844424064 scopus 로고    scopus 로고
    • Ubiquitination mediated by the Npi1p/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease
    • Galan, J.M., Moreau, V., André, B., Volland, C., and Haguenauer-Tsapis, R. (1996) Ubiquitination mediated by the Npi1p/Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease. J. Biol. Chem. 271, 10946-10952.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10946-10952
    • Galan, J.M.1    Moreau, V.2    André, B.3    Volland, C.4    Haguenauer-Tsapis, R.5
  • 43
    • 0031867271 scopus 로고    scopus 로고
    • Nitrogen-regulated ubiquitination of the Gap1 permease of Saccharomyces cerevisiae
    • Springael, J.Y. and André, B. (1998) Nitrogen-regulated ubiquitination of the Gap1 permease of Saccharomyces cerevisiae. Mol. Biol. Cell 9, 1253-1263.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1253-1263
    • Springael, J.Y.1    André, B.2
  • 44
    • 0035941194 scopus 로고    scopus 로고
    • Ubiquitin is required for sorting to the vacuole of the yeast general amino acid permease, Gap1
    • Soetens, O., De Craene, J.O., and André, B. (2001) Ubiquitin is required for sorting to the vacuole of the yeast general amino acid permease, Gap1. J. Biol. Chem. 276, 43949-43957.
    • (2001) J. Biol. Chem. , vol.276 , pp. 43949-43957
    • Soetens, O.1    De Craene, J.O.2    André, B.3
  • 45
    • 0037043340 scopus 로고    scopus 로고
    • An HRD/DER-independent ER quality control mechanism involves Rsp5p-dependent ubiquitination and ER-Golgi transport
    • Haynes, C.M., Caldwell, S., and Cooper, A.A. (2002) An HRD/DER-independent ER quality control mechanism involves Rsp5p-dependent ubiquitination and ER-Golgi transport. J. Cell Biol. 158, 91-101.
    • (2002) J. Cell Biol. , vol.158 , pp. 91-101
    • Haynes, C.M.1    Caldwell, S.2    Cooper, A.A.3
  • 46
    • 0035968205 scopus 로고    scopus 로고
    • Degradation of endoplasmic reticulum (ER) quality control substrates requires transport between the ER and Golgi
    • Caldwell, S.R., Hill, K.J., and Cooper, A.A. (2001) Degradation of endoplasmic reticulum (ER) quality control substrates requires transport between the ER and Golgi. J. Biol. Chem. 276, 23296-23303.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23296-23303
    • Caldwell, S.R.1    Hill, K.J.2    Cooper, A.A.3
  • 47
    • 0035851911 scopus 로고    scopus 로고
    • Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding
    • Vashist, S., Kim, W., Belden, W.J., Spear, E.D., Barlowe, C., and Ng, D.T. (2001) Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding. J. Cell. Biol. 155, 355-368.
    • (2001) J. Cell. Biol. , vol.155 , pp. 355-368
    • Vashist, S.1    Kim, W.2    Belden, W.J.3    Spear, E.D.4    Barlowe, C.5    Ng, D.T.6
  • 48
    • 0035985150 scopus 로고    scopus 로고
    • ER-Golgi traffic is a prerequisite for efficient ER degradation
    • Taxis, C., Vogel, F., and Wolf, D.H. (2002) ER-Golgi traffic is a prerequisite for efficient ER degradation. Mol. Biol. Cell 13, 1806-1818.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1806-1818
    • Taxis, C.1    Vogel, F.2    Wolf, D.H.3
  • 49
    • 0028084733 scopus 로고
    • The unfolded-protein-response pathway in yeast
    • Shamu, C.E., Cox, J.S., and Walter, P. (1994) The unfolded-protein- response pathway in yeast. Trends Cell Biol. 4, 56-60.
    • (1994) Trends Cell Biol. , vol.4 , pp. 56-60
    • Shamu, C.E.1    Cox, J.S.2    Walter, P.3
  • 50
    • 0032101239 scopus 로고    scopus 로고
    • The unfolded protein response: An intracellular signaling pathway with many surprising features
    • Sidrausky, C., Chapman, R., and Walter, P. (1998) The unfolded protein response: an intracellular signaling pathway with many surprising features. Trends Cell Biol. 8, 245-249.
    • (1998) Trends Cell Biol. , vol.8 , pp. 245-249
    • Sidrausky, C.1    Chapman, R.2    Walter, P.3
  • 51
    • 0347285295 scopus 로고    scopus 로고
    • A trip to the ER: Coping with stress
    • Rutkowski, D.T. and Kaufman, R.J. (2004) A trip to the ER: coping with stress. Trends Cell Biol. 14, 20-28.
    • (2004) Trends Cell Biol. , vol.14 , pp. 20-28
    • Rutkowski, D.T.1    Kaufman, R.J.2
  • 52
    • 33645996396 scopus 로고    scopus 로고
    • Protein folding in the endoplasmic reticulum and the unfolded protein response
    • Zhang, K. and Kaufman, R.J. (2006) Protein folding in the endoplasmic reticulum and the unfolded protein response. Handb. Exp. Pharmacol. 172, 69-91.
    • (2006) Handb. Exp. Pharmacol. , vol.172 , pp. 69-91
    • Zhang, K.1    Kaufman, R.J.2
  • 53
    • 0033780610 scopus 로고    scopus 로고
    • A regulatory link between ER-associated protein degradation and the unfolded-protein response
    • Friedlander, R., Jarosch, E., Urban, J., Volkwein, C., and Sommer, T. (2000) A regulatory link between ER-associated protein degradation and the unfolded-protein response. Nat. Cell Biol. 2, 379-384.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 379-384
    • Friedlander, R.1    Jarosch, E.2    Urban, J.3    Volkwein, C.4    Sommer, T.5
  • 54
    • 0033637082 scopus 로고    scopus 로고
    • Degradation of proteins from the ER of S. cerevisiae requires an intact unfolded protein response pathway
    • Casagrande, R., Stern, P., Diehn, M., Shamu, C., Osario, M., Zuniga, M., Brown, P.O., and Ploegh, H. (2000) Degradation of proteins from the ER of S. cerevisiae requires an intact unfolded protein response pathway. Mol. Cell 5, 729-735.
    • (2000) Mol. Cell , vol.5 , pp. 729-735
    • Casagrande, R.1    Stern, P.2    Diehn, M.3    Shamu, C.4    Osario, M.5    Zuniga, M.6    Brown, P.O.7    Ploegh, H.8
  • 55
    • 0037320333 scopus 로고    scopus 로고
    • IRE1: A role in UPREgulation of ER degradation
    • Hampton, R.Y. (2003) IRE1: a role in UPREgulation of ER degradation. Dev. Cell. 4, 144-146.
    • (2003) Dev. Cell. , vol.4 , pp. 144-146
    • Hampton, R.Y.1
  • 56
    • 0030297537 scopus 로고    scopus 로고
    • A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response
    • Cox, J.S. and Walter, P. (1996) A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response. Cell 87, 391-404.
    • (1996) Cell , vol.87 , pp. 391-404
    • Cox, J.S.1    Walter, P.2
  • 57
    • 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., Patil, C.K., Wodicka, L., Lockhart, D.J., Weissman, J.S., and Walter, P. (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    Patil, C.K.2    Wodicka, L.3    Lockhart, D.J.4    Weissman, J.S.5    Walter, P.6
  • 58
    • 0042318739 scopus 로고    scopus 로고
    • Evolving questions and paradigm shifts in endoplasmic-reticulum- associated degradation (ERAD)
    • McCracken, A.A. and Brodsky, J.L. (2003) Evolving questions and paradigm shifts in endoplasmic-reticulum-associated degradation (ERAD). Bioessays 25, 868-877.
    • (2003) Bioessays , vol.25 , pp. 868-877
    • McCracken, A.A.1    Brodsky, J.L.2
  • 59
    • 0742270608 scopus 로고    scopus 로고
    • A striking quality control subcompartment in Saccharomyces cerevisiae: The endoplasmic reticulum-associated compartment
    • Huyer, G., Longsworth, G.L., Mason, D.L., Mallampalli, M.P., McCaffery, J.M., Wright, R.L., and Michaelis, S. (2004) A striking quality control subcompartment in Saccharomyces cerevisiae: the endoplasmic reticulum-associated compartment. Mol. Biol. Cell 15, 908-921.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 908-921
    • Huyer, G.1    Longsworth, G.L.2    Mason, D.L.3    Mallampalli, M.P.4    McCaffery, J.M.5    Wright, R.L.6    Michaelis, S.7
  • 60
    • 0028838294 scopus 로고
    • Functional complementation of a null mutation of the yeast Saccharomyces cerevisiae plasma membrane H(+)-ATPase by a plant H(+)-ATPase gene
    • de Kerchove d'Exaerde, A., Supply, P., Dufour, J.P., Bogaerts, P., Thines, D., Goffeau, A., and Boutry, M. (1995) Functional complementation of a null mutation of the yeast Saccharomyces cerevisiae plasma membrane H(+)-ATPase by a plant H(+)-ATPase gene. J. Biol. Chem. 270, 23828-23837.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23828-23837
    • De Kerchove D'Exaerde, A.1    Supply, P.2    Dufour, J.P.3    Bogaerts, P.4    Thines, D.5    Goffeau, A.6    Boutry, M.7
  • 61
    • 0023788653 scopus 로고
    • Increased amounts of HMG-CoA reductase induce "karmellae": A proliferation of stacked membrane pairs surrounding the yeast nucleus
    • Wright, R., Basson, M., D'Ari, L., and Rine, J. (1988) Increased amounts of HMG-CoA reductase induce "karmellae": a proliferation of stacked membrane pairs surrounding the yeast nucleus. J. Cell Biol. 107, 101-114.
    • (1988) J. Cell Biol. , vol.107 , pp. 101-114
    • Wright, R.1    Basson, M.2    D'Ari, L.3    Rine, J.4
  • 63
    • 0031690373 scopus 로고    scopus 로고
    • Ste6p mutants defective in exit from the endoplasmic reticulum (ER) reveal aspects of an ER quality control pathway in Saccharomyces cerevisiae
    • Loayza, D., Tam, A., Schmidt, W.K., and Michaelis, S. (1998) Ste6p mutants defective in exit from the endoplasmic reticulum (ER) reveal aspects of an ER quality control pathway in Saccharomyces cerevisiae. Mol. Biol. Cell 9, 2767-2784.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2767-2784
    • Loayza, D.1    Tam, A.2    Schmidt, W.K.3    Michaelis, S.4
  • 64
    • 0027169843 scopus 로고
    • Proliferation of intracellular structures upon overexpression of the PMA2 ATPase in Saccharomyces cerevisiae
    • Supply, P., Wach, A., Thinès-Sempoux, D., and Goffeau, A. (1993) Proliferation of intracellular structures upon overexpression of the PMA2 ATPase in Saccharomyces cerevisiae. J. Biol. Chem. 268, 19744-19752.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19744-19752
    • Supply, P.1    Wach, A.2    Thinès-Sempoux, D.3    Goffeau, A.4
  • 65
    • 0037455585 scopus 로고    scopus 로고
    • Traffic-independent function of the Sar1p/COPII machinery in proteasomal sorting of the cystic fibrosis transmembrane conductance regulator
    • Fu, L. and Sztul, E. (2003) Traffic-independent function of the Sar1p/COPII machinery in proteasomal sorting of the cystic fibrosis transmembrane conductance regulator. J. Cell Biol. 160, 157-163.
    • (2003) J. Cell Biol. , vol.160 , pp. 157-163
    • Fu, L.1    Sztul, E.2
  • 66
    • 0030202773 scopus 로고    scopus 로고
    • Review: Subcellular traffic of the plasma membrane H+-ATPase in Saccharomyces cerevisiae
    • de Kerchove d'Exaerde, A., Supply, P., and Goffeau, A. (1996) Review: subcellular traffic of the plasma membrane H+-ATPase in Saccharomyces cerevisiae. Yeast 12, 907-916.
    • (1996) Yeast , vol.12 , pp. 907-916
    • De Kerchove D'Exaerde, A.1    Supply, P.2    Goffeau, A.3
  • 67
    • 0032571325 scopus 로고    scopus 로고
    • Substitutions of aspartate 378 in the phosphorylation domain of the yeast PMA1 H+-ATPase disrupt protein folding and biogenesis
    • Nakamoto, R.K., Verjovski-Almeida, S., Allen, K.E., Ambesi, A., Rao, R., and Slayman, C.W. (1998) Substitutions of aspartate 378 in the phosphorylation domain of the yeast PMA1 H+-ATPase disrupt protein folding and biogenesis. J. Biol. Chem. 273, 7338-7344.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7338-7344
    • Nakamoto, R.K.1    Verjovski-Almeida, S.2    Allen, K.E.3    Ambesi, A.4    Rao, R.5    Slayman, C.W.6
  • 68
    • 0037036391 scopus 로고    scopus 로고
    • Quality control in the yeast secretory pathway: A misfolded PMA1 H+-ATPase reveals two checkpoints
    • Ferreira, T., Mason, A.B., Pypaert, M., Allen, K.E., and Slayman, C.W. (2002) Quality control in the yeast secretory pathway: a misfolded PMA1 H+-ATPase reveals two checkpoints. J. Biol. Chem. 277, 21027-21040.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21027-21040
    • Ferreira, T.1    Mason, A.B.2    Pypaert, M.3    Allen, K.E.4    Slayman, C.W.5
  • 69
    • 0042205318 scopus 로고    scopus 로고
    • The role of ubiquitin in down-regulation and intracellular sorting of membrane proteins: Insights from yeast
    • Horák, J. (2003) The role of ubiquitin in down-regulation and intracellular sorting of membrane proteins: insights from yeast. Biochim. Biophys. Acta 1614, 139-155.
    • (2003) Biochim. Biophys. Acta , vol.1614 , pp. 139-155
    • Horák, J.1
  • 70
    • 2442717708 scopus 로고    scopus 로고
    • The ubiquitin ligase Rsp5p is required for modification and sorting of membrane proteins into multivesicular bodies
    • Morvan, J., Froissard, M., Haguenauer-Tsapis, R., and Urban-Grimal, D. (2004) The ubiquitin ligase Rsp5p is required for modification and sorting of membrane proteins into multivesicular bodies. Traffic 5, 383-392.
    • (2004) Traffic , vol.5 , pp. 383-392
    • Morvan, J.1    Froissard, M.2    Haguenauer-Tsapis, R.3    Urban-Grimal, D.4
  • 72
    • 0034327504 scopus 로고    scopus 로고
    • Ubiquitin in chains
    • Pickart, C.M. (2000) Ubiquitin in chains. Trends Biochem. Sci. 25, 544-548.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 544-548
    • Pickart, C.M.1
  • 73
    • 0021099710 scopus 로고
    • Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown
    • Hershko, A., Heller, H., Elias, S., and Ciechanover, A. (1983) Components of ubiquitin-protein ligase system. Resolution, affinity purification, and role in protein breakdown. J. Biol. Chem. 258, 8206-8214.
    • (1983) J. Biol. Chem. , vol.258 , pp. 8206-8214
    • Hershko, A.1    Heller, H.2    Elias, S.3    Ciechanover, A.4
  • 74
    • 0033989986 scopus 로고    scopus 로고
    • Modes of regulation of ubiquitin-mediated protein degradation
    • Kornitzer, D. and Ciechanover, A. (2000) Modes of regulation of ubiquitin-mediated protein degradation. J. Cell Physiol. 182, 1-11.
    • (2000) J. Cell Physiol. , vol.182 , pp. 1-11
    • Kornitzer, D.1    Ciechanover, A.2
  • 75
    • 0028146192 scopus 로고
    • Inhibition of proteolysis and cell cycle progression in a multiubiquitination-deficient yeast mutant
    • Finley, D., Sadis, S., Monia, B.P., Boucher, P., Ecker, D.J., Crooke, S.T., and Chau, V. (1994) Inhibition of proteolysis and cell cycle progression in a multiubiquitination-deficient yeast mutant. Mol. Cell Biol. 14, 5501-5509.
    • (1994) Mol. Cell Biol. , vol.14 , pp. 5501-5509
    • Finley, D.1    Sadis, S.2    Monia, B.P.3    Boucher, P.4    Ecker, D.J.5    Crooke, S.T.6    Chau, V.7
  • 76
    • 0027707607 scopus 로고
    • Structural features of 26S and 20S proteasomes
    • Lupas, A., Koster, A.J., and Baumeister, W. (1993) Structural features of 26S and 20S proteasomes. Enzyme Protein 47, 252-273.
    • (1993) Enzyme Protein , vol.47 , pp. 252-273
    • Lupas, A.1    Koster, A.J.2    Baumeister, W.3
  • 77
    • 11844287006 scopus 로고    scopus 로고
    • Mobilizing the proteolytic machine: Cell biological roles of proteasome activators and inhibitors
    • Rechsteiner, M. and Hill, C.P. (2005) Mobilizing the proteolytic machine: cell biological roles of proteasome activators and inhibitors. Trends Cell Biol. 15, 27-33.
    • (2005) Trends Cell Biol. , vol.15 , pp. 27-33
    • Rechsteiner, M.1    Hill, C.P.2
  • 78
    • 11844263929 scopus 로고    scopus 로고
    • A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting
    • Richly, H., Rape, M., Braun, S., Rumpf, S., Hoege, C., and Jentsch, S. (2005) A series of ubiquitin binding factors connects CDC48/p97 to substrate multiubiquitylation and proteasomal targeting. Cell 120, 73-84.
    • (2005) Cell , vol.120 , pp. 73-84
    • Richly, H.1    Rape, M.2    Braun, S.3    Rumpf, S.4    Hoege, C.5    Jentsch, S.6
  • 79
    • 1442331636 scopus 로고    scopus 로고
    • Yeast N-glycanase distinguishes between native and non-native glycoproteins
    • Hirsch, C., Misaghi, S., Blom, D., Pacold, M.E., and Ploegh, H.L. (2004) Yeast N-glycanase distinguishes between native and non-native glycoproteins. EMBO Rep. 5, 201-206.
    • (2004) EMBO Rep. , vol.5 , pp. 201-206
    • Hirsch, C.1    Misaghi, S.2    Blom, D.3    Pacold, M.E.4    Ploegh, H.L.5
  • 80
    • 19444362526 scopus 로고    scopus 로고
    • Pkc1p modifies CPY* degradation in the ERAD pathway
    • Nita-Lazar, M. and Lennarz, W.J. (2005) Pkc1p modifies CPY* degradation in the ERAD pathway. Biochem. Biophys. Res. Commun. 332, 357-361.
    • (2005) Biochem. Biophys. Res. Commun. , vol.332 , pp. 357-361
    • Nita-Lazar, M.1    Lennarz, W.J.2
  • 81
    • 1842409617 scopus 로고    scopus 로고
    • Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
    • Plemper, R.K., Böhmler, S., Bordallo, J., Sommer, T., and Wolf, D.H. (1997) Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature 388, 891-895.
    • (1997) Nature , vol.388 , pp. 891-895
    • Plemper, R.K.1    Böhmler, S.2    Bordallo, J.3    Sommer, T.4    Wolf, D.H.5
  • 82
    • 0030041781 scopus 로고    scopus 로고
    • Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast
    • Knop, M., Finger, A., Braun, T., Hellmuth, K., and Wolf, D.H. (1996) Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast. EMBO J. 15, 753-763.
    • (1996) EMBO J. , vol.15 , pp. 753-763
    • Knop, M.1    Finger, A.2    Braun, T.3    Hellmuth, K.4    Wolf, D.H.5
  • 83
    • 3042677637 scopus 로고    scopus 로고
    • A membrane protein complex mediates retrotranslocation from the ER lumen into the cytosol
    • Ye, Y., Shibata, Y., Yun, C., Ron, D., and Rapoport, T.A. (2004) A membrane protein complex mediates retrotranslocation from the ER lumen into the cytosol. Nature 429, 841-847.
    • (2004) Nature , vol.429 , pp. 841-847
    • Ye, Y.1    Shibata, Y.2    Yun, C.3    Ron, D.4    Rapoport, T.A.5
  • 84
    • 0029811218 scopus 로고    scopus 로고
    • Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein
    • Hampton, R.Y., Gardner, R.G., and Rine, J. (1996) Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein. Mol. Biol. Cell 7, 2029-2044.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 2029-2044
    • Hampton, R.Y.1    Gardner, R.G.2    Rine, J.3
  • 85
    • 0033492290 scopus 로고    scopus 로고
    • Genetic interactions of Hrd3p and Der3p/Hrd1p with Sec61p suggest a retro-translocation complex mediating protein transport for ER degradation
    • Plemper, R.K., Bordallo, J., Deak, P.M., Taxis, C., Hitt, R., and Wolf, D.H. (1999) Genetic interactions of Hrd3p and Der3p/Hrd1p with Sec61p suggest a retro-translocation complex mediating protein transport for ER degradation. J. Cell Sci. 112, 4123-4134.
    • (1999) J. Cell Sci. , vol.112 , pp. 4123-4134
    • Plemper, R.K.1    Bordallo, J.2    Deak, P.M.3    Taxis, C.4    Hitt, R.5    Wolf, D.H.6
  • 86
    • 0035887277 scopus 로고    scopus 로고
    • A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation
    • Swanson, R., Locher, M., and Hochstrasser, M. (2001) A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation. Genes Dev. 15, 2660-2674.
    • (2001) Genes Dev. , vol.15 , pp. 2660-2674
    • Swanson, R.1    Locher, M.2    Hochstrasser, M.3
  • 87
    • 0033490112 scopus 로고    scopus 로고
    • Surfing the Sec61 channel: Bidirectional protein translocation across the ER membrane
    • Römisch, K. (1999) Surfing the Sec61 channel: bidirectional protein translocation across the ER membrane. J. Cell Sci. 112, 4185-4191.
    • (1999) J. Cell Sci. , vol.112 , pp. 4185-4191
    • Römisch, K.1
  • 88
  • 89
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • Ye, Y., Meyer, H.H., and Rapoport, T.A. (2001) The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature 414, 652-656.
    • (2001) Nature , vol.414 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 90
    • 0034746779 scopus 로고    scopus 로고
    • The conserved npl4 protein complex mediates proteasome-dependent membrane-bound transcription factor activation
    • Hitchcock, A.L., Krebber, H., Frietze, S., Lin, A., Latterich, M., and Silver, P.A. (2001) The conserved npl4 protein complex mediates proteasome-dependent membrane-bound transcription factor activation. Mol. Biol. Cell 12, 3226-3241.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3226-3241
    • Hitchcock, A.L.1    Krebber, H.2    Frietze, S.3    Lin, A.4    Latterich, M.5    Silver, P.A.6
  • 91
    • 0037084028 scopus 로고    scopus 로고
    • Role of the ubiquitin-selective CDC48(UFD1/NPL4 )chaperone (segregase) in ERAD of OLE1 and other substrates
    • Braun, S., Matuschewski, K., Rape, M., Thoms, S., and Jentsch, S. (2002) Role of the ubiquitin-selective CDC48(UFD1/NPL4 )chaperone (segregase) in ERAD of OLE1 and other substrates. EMBO J. 21, 615-621.
    • (2002) EMBO J. , vol.21 , pp. 615-621
    • Braun, S.1    Matuschewski, K.2    Rape, M.3    Thoms, S.4    Jentsch, S.5
  • 93
    • 0036136901 scopus 로고    scopus 로고
    • AAA-ATPase p97/Cdc48p; a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation
    • Rabinovich, E., Kerem, A., Frölich, K.-U., Diamant, N., and Bar-Nun, S. (2002) AAA-ATPase p97/Cdc48p; a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation. Mol. Cell Biol. 22, 626-634.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 626-634
    • Rabinovich, E.1    Kerem, A.2    Frölich, K.-U.3    Diamant, N.4    Bar-Nun, S.5
  • 94
    • 30744451400 scopus 로고    scopus 로고
    • Functional division of substrate processing cofactors of the ubiquitin-selective cdc48 chaperone
    • Rumpf, S. and Jentsch, S. (2006) Functional division of substrate processing cofactors of the ubiquitin-selective cdc48 chaperone. Mol. Cell 21, 261-269.
    • (2006) Mol. Cell , vol.21 , pp. 261-269
    • Rumpf, S.1    Jentsch, S.2
  • 95
    • 0036277299 scopus 로고    scopus 로고
    • Rad23 promotes the targeting of proteolytic substrates to the proteasome
    • Chen, L. and Madura, K. (2002) Rad23 promotes the targeting of proteolytic substrates to the proteasome. Mol. Cell Biol. 22, 4902-4913.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 4902-4913
    • Chen, L.1    Madura, K.2
  • 96
    • 0037154160 scopus 로고    scopus 로고
    • Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome
    • Funakoshi, M., Sasaki, T., Nishimoto, T., and Kobayashi, H. (2002) Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome. Proc. Natl. Acad. Sci. U. S. A. 99, 745-750.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 745-750
    • Funakoshi, M.1    Sasaki, T.2    Nishimoto, T.3    Kobayashi, H.4
  • 97
    • 0025913947 scopus 로고
    • Yeast cell cycle protein CDC48p shows full-length homology to the mammalian protein VCP and is a member of a protein family involved in secretion, peroxisome formation, and gene expression
    • Frohlich, K.U., Fries, H.W., Rudiger, M., Erdmann, R., Botstein, D., and Mecke, D. (1991) Yeast cell cycle protein CDC48p shows full-length homology to the mammalian protein VCP and is a member of a protein family involved in secretion, peroxisome formation, and gene expression. J. Cell Biol. 114, 443-453.
    • (1991) J. Cell Biol. , vol.114 , pp. 443-453
    • Frohlich, K.U.1    Fries, H.W.2    Rudiger, M.3    Erdmann, R.4    Botstein, D.5    Mecke, D.6
  • 98
    • 0141507032 scopus 로고    scopus 로고
    • Complete structure of p97/valosin-containing protein reveals communication between nucleotide domains
    • DeLaBarre, B. and Brunger, A.T. (2003) Complete structure of p97/valosin-containing protein reveals communication between nucleotide domains. Nat. Struct. Biol. 10, 856-863.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 856-863
    • DeLaBarre, B.1    Brunger, A.T.2
  • 99
    • 1842576796 scopus 로고    scopus 로고
    • Structural basis of the interaction between the AAA ATPase p97/VCP and its adaptor protein p47
    • Dreveny, I., Kondo, H., Uchiyama, K., Shaw, A., Zhang, X., and Freemont, P.S. (2004) Structural basis of the interaction between the AAA ATPase p97/VCP and its adaptor protein p47. EMBO J. 23, 1030-1039.
    • (2004) EMBO J. , vol.23 , pp. 1030-1039
    • Dreveny, I.1    Kondo, H.2    Uchiyama, K.3    Shaw, A.4    Zhang, X.5    Freemont, P.S.6
  • 100
    • 0034602845 scopus 로고    scopus 로고
    • Recognition of the polyubiquitin proteolytic signal
    • Thrower, J.S., Hoffman, L., Rechsteiner, M., and Pickart, C.M. (2000) Recognition of the polyubiquitin proteolytic signal. EMBO J. 19, 94-102.
    • (2000) EMBO J. , vol.19 , pp. 94-102
    • Thrower, J.S.1    Hoffman, L.2    Rechsteiner, M.3    Pickart, C.M.4
  • 101
    • 0032561398 scopus 로고    scopus 로고
    • The p47 co-factor regulates the ATPase activity of the membrane fusion protein, p97
    • Meyer, H.H., Kondo, H., and Warren, G. (1998) The p47 co-factor regulates the ATPase activity of the membrane fusion protein, p97. FEBS Lett. 437, 255-257.
    • (1998) FEBS Lett. , vol.437 , pp. 255-257
    • Meyer, H.H.1    Kondo, H.2    Warren, G.3
  • 102
    • 17044386675 scopus 로고    scopus 로고
    • p97/p47-Mediated biogenesis of Golgi and ER
    • Uchiyama, K. and Kondo, H. (2005) p97/p47-Mediated biogenesis of Golgi and ER. J. Biochem. (Tokyo) 137, 115-119.
    • (2005) J. Biochem. (Tokyo) , vol.137 , pp. 115-119
    • Uchiyama, K.1    Kondo, H.2
  • 103
    • 1242341446 scopus 로고    scopus 로고
    • Binding of Cdc48p to a ubiquitin-related UBX domain from novel yeast proteins involved in intracellular proteolysis and sporulation
    • Decottignies, A., Evain, A., and Ghislain, M. (2004) Binding of Cdc48p to a ubiquitin-related UBX domain from novel yeast proteins involved in intracellular proteolysis and sporulation. Yeast 21, 127-139.
    • (2004) Yeast , vol.21 , pp. 127-139
    • Decottignies, A.1    Evain, A.2    Ghislain, M.3
  • 104
    • 4444284299 scopus 로고    scopus 로고
    • Shp1 and Ubx2 are adaptors of Cdc48 involved in ubiquitin-dependent protein degradation
    • Schuberth, C., Richly, H., Rumpf, S., and Buchberger, A. (2004) Shp1 and Ubx2 are adaptors of Cdc48 involved in ubiquitin-dependent protein degradation. EMBO Rep. 5, 818-824.
    • (2004) EMBO Rep. , vol.5 , pp. 818-824
    • Schuberth, C.1    Richly, H.2    Rumpf, S.3    Buchberger, A.4
  • 105
    • 27144535945 scopus 로고    scopus 로고
    • Ubx2 links the Cdc48 complex to ERassociated protein degradation
    • Neuber, O., Jarosch, E., Volkwein, C., Walter, J., and Sommer, T. (2005) Ubx2 links the Cdc48 complex to ERassociated protein degradation. Nat. Cell Biol. 7, 993-998.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 993-998
    • Neuber, O.1    Jarosch, E.2    Volkwein, C.3    Walter, J.4    Sommer, T.5
  • 106
    • 27144539523 scopus 로고    scopus 로고
    • Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated protein degradation
    • Schuberth, C. and Buchberger, A. (2005) Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated protein degradation. Nat. Cell Biol. 7, 999-1006.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 999-1006
    • Schuberth, C.1    Buchberger, A.2
  • 107
    • 30944437203 scopus 로고    scopus 로고
    • Cdc48p is UBX-linked to ER ubiquitin ligases
    • Römisch, K. (2006) Cdc48p is UBX-linked to ER ubiquitin ligases. Trends Biochem. Sci. 31, 24-25.
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 24-25
    • Römisch, K.1
  • 108
    • 0029119522 scopus 로고
    • A proteolytic pathway that recognizes ubiquitin as a degradation signal
    • Johnson, E.S., Ma, P.C., Ota, I.M., and Varshavsky, A. (1995) A proteolytic pathway that recognizes ubiquitin as a degradation signal. J. Biol. Chem. 270, 17442-17456.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17442-17456
    • Johnson, E.S.1    Ma, P.C.2    Ota, I.M.3    Varshavsky, A.4
  • 109
    • 21744460209 scopus 로고    scopus 로고
    • Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites
    • Park, S., Isaacson, R., Kim, H.T., Silver, P.A., and Wagner, G. (2005) Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites. Structure 13, 995-1005.
    • (2005) Structure , vol.13 , pp. 995-1005
    • Park, S.1    Isaacson, R.2    Kim, H.T.3    Silver, P.A.4    Wagner, G.5
  • 110
    • 0029904102 scopus 로고    scopus 로고
    • Nuclear transport defects and nuclear envelope alterations are associated with mutation of the Saccharomyces cerevisiae NPL4 gene
    • DeHoratius, C. and Silver, P.A. (1996) Nuclear transport defects and nuclear envelope alterations are associated with mutation of the Saccharomyces cerevisiae NPL4 gene. Mol. Biol. Cell 7, 1835-1855.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1835-1855
    • DeHoratius, C.1    Silver, P.A.2
  • 111
    • 9644255751 scopus 로고    scopus 로고
    • The AAA ATPase p97/VCP interacts with its alternative co-factors, Ufd1-Npl4 and p47, through a common bipartite binding mechanism
    • Bruderer, R.M., Brasseur, C., and Meyer, H.H. (2004) The AAA ATPase p97/VCP interacts with its alternative co-factors, Ufd1-Npl4 and p47, through a common bipartite binding mechanism. J. Biol. Chem. 279, 49609-49616.
    • (2004) J. Biol. Chem. , vol.279 , pp. 49609-49616
    • Bruderer, R.M.1    Brasseur, C.2    Meyer, H.H.3
  • 112
    • 0029814693 scopus 로고    scopus 로고
    • Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae
    • Ghislain, M., Dohmen, R.J., Levy, F., and Varshavsky, A. (1996) Cdc48p interacts with Ufd3p, a WD repeat protein required for ubiquitin-mediated proteolysis in Saccharomyces cerevisiae. EMBO J. 15, 4884-4899.
    • (1996) EMBO J. , vol.15 , pp. 4884-4899
    • Ghislain, M.1    Dohmen, R.J.2    Levy, F.3    Varshavsky, A.4
  • 113
  • 114
    • 0033231014 scopus 로고    scopus 로고
    • A 'distributed degron' allows regulated entry into the ER degradation pathway
    • Gardner, R.G. and Hampton, R.H. (1999) A 'distributed degron' allows regulated entry into the ER degradation pathway. EMBO J. 18, 5994-6004.
    • (1999) EMBO J. , vol.18 , pp. 5994-6004
    • Gardner, R.G.1    Hampton, R.H.2
  • 115
    • 0036702298 scopus 로고    scopus 로고
    • ER-associated degradation in protein quality control and cellular regulation
    • Hampton, R.Y. (2002) ER-associated degradation in protein quality control and cellular regulation. Curr. Opin. Cell Biol. 14, 476-482.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 476-482
    • Hampton, R.Y.1
  • 116
    • 0024424620 scopus 로고
    • Isolation and characterization of OLE1, a gene affecting fatty acid desaturation from Saccharomyces cerevisiae
    • Stukey, J.E., McDonough, V.M., and Martin, C.E. (1989) Isolation and characterization of OLE1, a gene affecting fatty acid desaturation from Saccharomyces cerevisiae. J. Biol. Chem. 264, 16537-16544.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16537-16544
    • Stukey, J.E.1    McDonough, V.M.2    Martin, C.E.3
  • 117
    • 0032962409 scopus 로고    scopus 로고
    • MGA2 or SPT23 is required for transcription of the delta9 fatty acid desaturase gene, OLE1, and nuclear membrane integrity in Saccharomyces cerevisiae
    • Zhang, S., Skalsky, Y., and Garfinkel, D.J. (1999) MGA2 or SPT23 is required for transcription of the delta9 fatty acid desaturase gene, OLE1, and nuclear membrane integrity in Saccharomyces cerevisiae. Genetics 151, 473-483.
    • (1999) Genetics , vol.151 , pp. 473-483
    • Zhang, S.1    Skalsky, Y.2    Garfinkel, D.J.3
  • 118
    • 0034268493 scopus 로고    scopus 로고
    • Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing
    • Hoppe, T., Matuschewski, K., Rape, M., Schlenker, S., Ulrich, H.D., and Jentsch, S. (2000) Activation of a membrane-bound transcription factor by regulated ubiquitin/proteasome-dependent processing. Cell 102, 577-586.
    • (2000) Cell , vol.102 , pp. 577-586
    • Hoppe, T.1    Matuschewski, K.2    Rape, M.3    Schlenker, S.4    Ulrich, H.D.5    Jentsch, S.6
  • 119
    • 0035977095 scopus 로고    scopus 로고
    • Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone
    • Rape, M., Hoppe, T., Gorr, I., Kalocay, M., Richly, H., and Jentsch, S. (2001) Mobilization of processed, membrane-tethered SPT23 transcription factor by CDC48(UFD1/NPL4), a ubiquitin-selective chaperone. Cell 107, 667-677.
    • (2001) Cell , vol.107 , pp. 667-677
    • Rape, M.1    Hoppe, T.2    Gorr, I.3    Kalocay, M.4    Richly, H.5    Jentsch, S.6
  • 120
    • 0038376459 scopus 로고    scopus 로고
    • Rsp5p is required for ER bound Mga2p120 polyubiquitination and release of the processed/tethered transactivator Mga2p90
    • Shcherbik, N., Zoladek, T., Nickels, J.T., and Haines, D.S. (2003) Rsp5p is required for ER bound Mga2p120 polyubiquitination and release of the processed/tethered transactivator Mga2p90. Curr. Biol. 13, 1227-1233.
    • (2003) Curr. Biol. , vol.13 , pp. 1227-1233
    • Shcherbik, N.1    Zoladek, T.2    Nickels, J.T.3    Haines, D.S.4
  • 121
    • 0027137885 scopus 로고
    • Analysis of two mutated vacuolar proteins reveals a degradation pathway in the endoplasmic reticulum or a related compartment of yeast
    • Finger, A., Knop, M., and Wolf, D.H. (1993) Analysis of two mutated vacuolar proteins reveals a degradation pathway in the endoplasmic reticulum or a related compartment of yeast. Eur. J. Biochem. 218, 565-574.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 565-574
    • Finger, A.1    Knop, M.2    Wolf, D.H.3
  • 122
    • 2442451126 scopus 로고    scopus 로고
    • Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control
    • Vashist, S. and Ng, D.T. (2004) Misfolded proteins are sorted by a sequential checkpoint mechanism of ER quality control. J. Cell Biol. 165, 41-52.
    • (2004) J. Cell Biol. , vol.165 , pp. 41-52
    • Vashist, S.1    Ng, D.T.2
  • 123
    • 0028073895 scopus 로고
    • Inhibition of endoplasmic reticulum (ER)-to-Golgi transport induces relocalization of binding protein (BiP) within the ER to form the BiP bodies
    • Nishikawa, S., Hirata, A., and Nakano, A. (1994) Inhibition of endoplasmic reticulum (ER)-to-Golgi transport induces relocalization of binding protein (BiP) within the ER to form the BiP bodies. Mol. Biol. Cell 5, 1129-1143.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 1129-1143
    • Nishikawa, S.1    Hirata, A.2    Nakano, A.3
  • 124
    • 0034618102 scopus 로고    scopus 로고
    • Mutants affecting the structure of the cortical endoplasmic reticulum in Saccharomyces cerevisiae
    • Prinz, W.A., Grzyb, L., Veenhuis, M., Kahana, J.A., Silver, P.A., and Rapoport, T.A. (2000) Mutants affecting the structure of the cortical endoplasmic reticulum in Saccharomyces cerevisiae. J. Cell Biol. 150, 461-474.
    • (2000) J. Cell Biol. , vol.150 , pp. 461-474
    • Prinz, W.A.1    Grzyb, L.2    Veenhuis, M.3    Kahana, J.A.4    Silver, P.A.5    Rapoport, T.A.6
  • 125
    • 0035947773 scopus 로고    scopus 로고
    • Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation
    • Nishikawa, S.I., Fewell, S.W., Kato, Y., Brodsky, J.L., and Endo, T. (2001) Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation. J. Cell Biol. 153, 1061-1070.
    • (2001) J. Cell Biol. , vol.153 , pp. 1061-1070
    • Nishikawa, S.I.1    Fewell, S.W.2    Kato, Y.3    Brodsky, J.L.4    Endo, T.5
  • 126
    • 0029838640 scopus 로고    scopus 로고
    • ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
    • Hiller, M.M., Finger, A., Schweiger, M., and Wolf, D.H. (1996) ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science 273, 1725-1728.
    • (1996) Science , vol.273 , pp. 1725-1728
    • Hiller, M.M.1    Finger, A.2    Schweiger, M.3    Wolf, D.H.4
  • 127
    • 0032484024 scopus 로고    scopus 로고
    • Endoplasmic reticulum degradation of a mutated ATP-binding cassette transporter Pdr5 proceeds in a concerted action of Sec61 and the proteasome
    • Plemper, R.K., Egner, R., Kuchler, K., and Wolf, D.H. (1998) Endoplasmic reticulum degradation of a mutated ATP-binding cassette transporter Pdr5 proceeds in a concerted action of Sec61 and the proteasome. J. Biol. Chem. 273, 32848-32856.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32848-32856
    • Plemper, R.K.1    Egner, R.2    Kuchler, K.3    Wolf, D.H.4
  • 129
    • 0024375860 scopus 로고
    • The yeast STE6 gene encodes a homologue of the mammalian multidrug resistance P-glycoprotein
    • McGrath, J.P. and Varshavsky, A. (1989) The yeast STE6 gene encodes a homologue of the mammalian multidrug resistance P-glycoprotein. Nature 340, 400-404.
    • (1989) Nature , vol.340 , pp. 400-404
    • McGrath, J.P.1    Varshavsky, A.2
  • 130
    • 0028277963 scopus 로고
    • The ABC-transporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants
    • Kolling, R. and Hollenberg, C.P. (1994) The ABC-transporter Ste6 accumulates in the plasma membrane in a ubiquitinated form in endocytosis mutants. EMBO J. 13, 3261-3271.
    • (1994) EMBO J. , vol.13 , pp. 3261-3271
    • Kolling, R.1    Hollenberg, C.P.2
  • 131
    • 4444355303 scopus 로고    scopus 로고
    • Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein
    • Huyer, G., Piluek, W.F., Fansler, Z, Kreft, S.G., Hochstrasser, M., Brodsky, J.L., and Michaelis, S. (2004) Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein. J. Biol. Chem. 279, 38369-38378.
    • (2004) J. Biol. Chem. , vol.279 , pp. 38369-38378
    • Huyer, G.1    Piluek, W.F.2    Fansler, Z.3    Kreft, S.G.4    Hochstrasser, M.5    Brodsky, J.L.6    Michaelis, S.7
  • 132
    • 0028082188 scopus 로고
    • PDR5, a novel yeast multidrug resistance conferring transporter controlled by the transcription regulator PDR1
    • Balzi, E., Wang, M., Leterme, S., Van Dyck, L., and Goffeau, A. (1994) PDR5, a novel yeast multidrug resistance conferring transporter controlled by the transcription regulator PDR1. J. Biol. Chem. 269, 2206-2214.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2206-2214
    • Balzi, E.1    Wang, M.2    Leterme, S.3    Van Dyck, L.4    Goffeau, A.5
  • 133
    • 0028111508 scopus 로고
    • Molecular cloning and expression of the Saccharomyces cerevisiae STS1 gene product. A yeast ABC transporter conferring mycotoxin resistance
    • Bissinger, P.H. and Kuchler, K. (1994) Molecular cloning and expression of the Saccharomyces cerevisiae STS1 gene product. A yeast ABC transporter conferring mycotoxin resistance. J. Biol. Chem. 269, 4180-4186.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4180-4186
    • Bissinger, P.H.1    Kuchler, K.2
  • 134
    • 0031905588 scopus 로고    scopus 로고
    • Genetic separation of FK506 susceptibility and drug transport in the yeast Pdr5 ATP-binding cassette multidrug resistance transporter
    • Egner, R., Rosenthal, F.E., Kralli, A., Sanglard, D., and Kuchler, K. (1998) Genetic separation of FK506 susceptibility and drug transport in the yeast Pdr5 ATP-binding cassette multidrug resistance transporter. Mol. Biol. Cell 9, 523-543.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 523-543
    • Egner, R.1    Rosenthal, F.E.2    Kralli, A.3    Sanglard, D.4    Kuchler, K.5
  • 135
    • 4344560565 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane conductance regulator degradation depends on the lectins Htm1p/EDEM and the Cdc48 protein complex in yeast
    • Gnann, A., Riordan, J.R., and Wolf, D.H. (2004) Cystic fibrosis transmembrane conductance regulator degradation depends on the lectins Htm1p/EDEM and the Cdc48 protein complex in yeast. Mol. Biol. Cell 15, 4125-4135.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4125-4135
    • Gnann, A.1    Riordan, J.R.2    Wolf, D.H.3
  • 136
    • 0344721493 scopus 로고    scopus 로고
    • Characterization of the Wsc1 protein, a putative receptor in the stress response of Saccharomyces cerevisiae
    • Lodder, A.L., Lee, T.K., and Ballester, R. (1999) Characterization of the Wsc1 protein, a putative receptor in the stress response of Saccharomyces cerevisiae. Genetics 152, 1487-1499.
    • (1999) Genetics , vol.152 , pp. 1487-1499
    • Lodder, A.L.1    Lee, T.K.2    Ballester, R.3
  • 137
    • 0141592584 scopus 로고    scopus 로고
    • Use of modular substrates demonstrates mechanistic diversity and reveals differences in chaperone requirement of ERAD
    • Taxis, C., Hitt, R., Park, S.H., Deak, P.M., Kostova, Z., and Wolf, D.H. (2003) Use of modular substrates demonstrates mechanistic diversity and reveals differences in chaperone requirement of ERAD. J. Biol. Chem. 278, 35903-35913.
    • (2003) J. Biol. Chem. , vol.278 , pp. 35903-35913
    • Taxis, C.1    Hitt, R.2    Park, S.H.3    Deak, P.M.4    Kostova, Z.5    Wolf, D.H.6
  • 138
    • 4444320698 scopus 로고    scopus 로고
    • A genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradation
    • Medicherla, B., Kostova, Z., Schaefer, A., and Wolf, D.H. (2004) A genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradation. EMBO Rep. 5, 692-697.
    • (2004) EMBO Rep. , vol.5 , pp. 692-697
    • Medicherla, B.1    Kostova, Z.2    Schaefer, A.3    Wolf, D.H.4
  • 139
    • 27244462469 scopus 로고    scopus 로고
    • Expression and degradation of the cystic fibrosis transmembrane conductance regulator in Saccharomyces cerevisiae
    • Kiser, G.L., Gentzsch, M., Kloser, A.K., Balzi, E., Wolf, D.H., Goffeau, A., and Riordan, J.R. (2001) Expression and degradation of the cystic fibrosis transmembrane conductance regulator in Saccharomyces cerevisiae. Arch. Biochem. Biophys. 390, 195-205.
    • (2001) Arch. Biochem. Biophys. , vol.390 , pp. 195-205
    • Kiser, G.L.1    Gentzsch, M.2    Kloser, A.K.3    Balzi, E.4    Wolf, D.H.5    Goffeau, A.6    Riordan, J.R.7
  • 140
    • 0034757165 scopus 로고    scopus 로고
    • Hsp70 molecular chaperone facilitates endoplasmic reticulum-associated protein degradation of cystic fibrosis transmembrane conductance regulator in yeast
    • Zhang, Y., Nijbroek, G., Sullivan, M.L., McCracken, A.A., Watkins, S.C., Michaelis, S., and Brodsky, J.L. (2001) Hsp70 molecular chaperone facilitates endoplasmic reticulum-associated protein degradation of cystic fibrosis transmembrane conductance regulator in yeast. Mol. Biol. Cell 12, 1303-1314.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1303-1314
    • Zhang, Y.1    Nijbroek, G.2    Sullivan, M.L.3    McCracken, A.A.4    Watkins, S.C.5    Michaelis, S.6    Brodsky, J.L.7
  • 141
    • 5444220240 scopus 로고    scopus 로고
    • COPII-dependent export of cystic fibrosis transmembrane conductance regulator from the ER uses a di-acidic exit code
    • Wang, X., Matteson, J., An, Y., Moyer, B., Yoo, J.S., Bannykh, S., Wilson, I.A., Riordan, J.R., and Balch, W.E. (2004) COPII-dependent export of cystic fibrosis transmembrane conductance regulator from the ER uses a di-acidic exit code. J. Cell Biol. 167, 65-74.
    • (2004) J. Cell Biol. , vol.167 , pp. 65-74
    • Wang, X.1    Matteson, J.2    An, Y.3    Moyer, B.4    Yoo, J.S.5    Bannykh, S.6    Wilson, I.A.7    Riordan, J.R.8    Balch, W.E.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.