메뉴 건너뛰기




Volumn 32, Issue 1, 2013, Pages 2-7

Compartmentalization of endoplasmic reticulum quality control and ER-associated degradation factors

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CALCIUM CHANNEL; CALNEXIN; CALRETICULIN; HEAT SHOCK PROTEIN 70; INITIATION FACTOR 2ALPHA; INOSITOL 1,4,5 TRISPHOSPHATE RECEPTOR; INOSITOL REQUIRING ENZYME 1; MANNOSE; MITOCHONDRIAL FISSION PROTEIN; PROTEIN; PROTEIN DISULFIDE ISOMERASE; PROTEIN KINASE R; PROTEIN KINASE RNA; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 84873027092     PISSN: 10445498     EISSN: 15577430     Source Type: Journal    
DOI: 10.1089/dna.2012.1889     Document Type: Article
Times cited : (28)

References (66)
  • 1
    • 58149336774 scopus 로고    scopus 로고
    • Mammalian OS-9 is upregulated in response to endoplasmic reticulum stress and facilitates ubiquitination of misfolded glycoproteins
    • Alcock, F., and Swanton, E. (2009). Mammalian OS-9 is upregulated in response to endoplasmic reticulum stress and facilitates ubiquitination of misfolded glycoproteins. J Mol Biol 385, 1032-42
    • (2009) J Mol Biol , vol.385 , pp. 1032-1042
    • Alcock, F.1    Swanton, E.2
  • 3
    • 38749122389 scopus 로고    scopus 로고
    • Endoplasmic reticulum (ER) mannosidase i is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradation
    • Avezov, E., Frenkel, Z., Ehrlich, M., Herscovics, A., and Lederkremer, GZ. (2008). Endoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradation. Mol Biol Cell 19, 216-25
    • (2008) Mol Biol Cell , vol.19 , pp. 216-225
    • Avezov, E.1    Frenkel, Z.2    Ehrlich, M.3    Herscovics, A.4    Lederkremer, G.Z.5
  • 4
    • 80855139444 scopus 로고    scopus 로고
    • Protein quality control, retention, and degradation at the endoplasmic reticulum
    • Benyair, R., Ron, E., and Lederkremer, G.Z. (2011). Protein quality control, retention, and degradation at the endoplasmic reticulum. Int Rev Cell Mol Biol 292, 197-280
    • (2011) Int Rev Cell Mol Biol , vol.292 , pp. 197-280
    • Benyair, R.1    Ron, E.2    Lederkremer, G.Z.3
  • 5
    • 84862976027 scopus 로고    scopus 로고
    • Role of the SEL1L, LC3-I complex as an ERAD tuning receptor in the mammalian ER
    • Bernasconi, R., Galli, C., Noack, J., Bianchi, S., de Haan, C.A., Reggiori, F., et al.(2012). Role of the SEL1L, LC3-I complex as an ERAD tuning receptor in the mammalian ER. Mol Cell 46, 809-19
    • (2012) Mol Cell , vol.46 , pp. 809-819
    • Bernasconi, R.1    Galli, C.2    Noack, J.3    Bianchi, S.4    De Haan, C.A.5    Reggiori, F.6
  • 6
    • 79954423426 scopus 로고    scopus 로고
    • ERAD and ERAD tuning, disposal of cargo and of ERAD regulators from the mammalian ER
    • Bernasconi, R., and Molinari, M. (2011). ERAD and ERAD tuning, disposal of cargo and of ERAD regulators from the mammalian ER. Curr Opin Cell Biol 23, 176-83
    • (2011) Curr Opin Cell Biol , vol.23 , pp. 176-183
    • Bernasconi, R.1    Molinari, M.2
  • 7
    • 0344825875 scopus 로고    scopus 로고
    • Cytochrome c binds to inositol 1 45) trisphosphate receptors amplifying calciumdependent apoptosis
    • Boehning, D., Patterson, R.L., Sedaghat, L., Glebova, N.O., Kurosaki, T., and Snyder, S.H. (2003). Cytochrome c binds to inositol (1,4,5) trisphosphate receptors: Amplifying calciumdependent apoptosis. Nat Cell Biol 5, 1051-61
    • (2003) Nat Cell Biol 5 , pp. 1051-1061
    • Boehning, D.1    Patterson, R.L.2    Sedaghat, L.3    Glebova, N.O.4    Kurosaki, T.5    Snyder, S.H.6
  • 8
    • 70450225048 scopus 로고    scopus 로고
    • ER exit sites-localization and control of COPII vesicle formation
    • Budnik, A., and Stephens, D.J. (2009). ER exit sites-localization and control of COPII vesicle formation. FEBS Lett 583, 3796- 803
    • (2009) FEBS Lett , vol.583 , pp. 3796-3803
    • Budnik, A.1    Stephens, D.J.2
  • 9
    • 43549087339 scopus 로고    scopus 로고
    • Segregation and rapid turnover of EDEM1 by an autophagy-like mechanism modulates standard ERAD and folding activities
    • Cali, T., Galli, C., Olivari, S., and Molinari, M. (2008). Segregation and rapid turnover of EDEM1 by an autophagy-like mechanism modulates standard ERAD and folding activities. Biochem Biophys Res Commun 371, 405-10
    • (2008) Biochem Biophys Res Commun , vol.371 , pp. 405-410
    • Cali, T.1    Galli, C.2    Olivari, S.3    Molinari, M.4
  • 10
    • 0033548479 scopus 로고    scopus 로고
    • Trimming and readdition of glucose to N-linked oligosaccharides determines calnexin association of a substrate glycoprotein in living cells
    • Cannon, K.S., and Helenius, A. (1999). Trimming and readdition of glucose to N-linked oligosaccharides determines calnexin association of a substrate glycoprotein in living cells. J Biol Chem 274, 7537-44
    • (1999) J Biol Chem , vol.274 , pp. 7537-7544
    • Cannon, K.S.1    Helenius, A.2
  • 11
    • 40249088336 scopus 로고    scopus 로고
    • OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD
    • Christianson, J.C., Shaler, T.A., Tyler, R.E., and Kopito, R.R. (2008). OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD. Nat Cell Biol 10, 272-82
    • (2008) Nat Cell Biol , vol.10 , pp. 272-282
    • Christianson, J.C.1    Shaler, T.A.2    Tyler, R.E.3    Kopito, R.R.4
  • 12
    • 77953809347 scopus 로고    scopus 로고
    • ERp57: A multifunctional endoplasmic reticulum resident oxidoreductase
    • Coe, H., and Michalak, M. (2010). ERp57: A multifunctional endoplasmic reticulum resident oxidoreductase. Int J Biochem Cell Biol 42, 796-9
    • (2010) Int J Biochem Cell Biol , vol.42 , pp. 796-799
    • Coe, H.1    Michalak, M.2
  • 13
    • 77952583769 scopus 로고    scopus 로고
    • UDP-GlC: Glycoprotein glucosyltransferase-glucosidase II, the ying-yang of the ER quality control
    • D'Alessio, C., Caramelo, J.J., and Parodi, A.J. (2010). UDP-GlC: glycoprotein glucosyltransferase-glucosidase II, the ying-yang of the ER quality control. Semin Cell Dev Biol 21, 491-9
    • (2010) Semin Cell Dev Biol , vol.21 , pp. 491-499
    • D'Alessio, C.1    Caramelo, J.J.2    Parodi, A.J.3
  • 14
    • 2342505236 scopus 로고    scopus 로고
    • Separate roles and different routing of calnexin and ERp57 in endoplasmic reticulum quality control revealed by interactions with asialoglycoprotein receptor chains
    • Frenkel, Z., Shenkman, M., Kondratyev, M., and Lederkremer, G.Z. (2004). Separate roles and different routing of calnexin and ERp57 in endoplasmic reticulum quality control revealed by interactions with asialoglycoprotein receptor chains. Mol Biol Cell 15, 2133-42
    • (2004) Mol Biol Cell , vol.15 , pp. 2133-2142
    • Frenkel, Z.1    Shenkman, M.2    Kondratyev, M.3    Lederkremer, G.Z.4
  • 16
    • 78651394090 scopus 로고    scopus 로고
    • Mannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation steps
    • Groisman, B., Shenkman, M., Ron, E., and Lederkremer, GZ. (2011). Mannose trimming is required for delivery of a glycoprotein from EDEM1 to XTP3-B and to late endoplasmic reticulum-associated degradation steps. J Biol Chem 286, 1292-300
    • (2011) J Biol Chem , vol.286 , pp. 1292-1300
    • Groisman, B.1    Shenkman, M.2    Ron, E.3    Lederkremer, G.Z.4
  • 18
    • 84866623060 scopus 로고    scopus 로고
    • Flagging and docking: Dual roles for N-glycans in protein quality control and cellular proteostasis
    • Hebert, D.N., and Molinari, M. (2012). Flagging and docking: dual roles for N-glycans in protein quality control and cellular proteostasis. Trends Biochem Sci 37, 404-10
    • (2012) Trends Biochem Sci , vol.37 , pp. 404-410
    • Hebert, D.N.1    Molinari, M.2
  • 21
    • 67650535999 scopus 로고    scopus 로고
    • Human OS-9: A lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans
    • Hosokawa, N., Kamiya, Y., Kamiya, D., Kato, K., and Nagata, K. (2009). Human OS-9: A lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans. J Biol Chem 284, 17061-8
    • (2009) J Biol Chem , vol.284 , pp. 17061-17068
    • Hosokawa, N.1    Kamiya, Y.2    Kamiya, D.3    Kato, K.4    Nagata, K.5
  • 22
    • 77952811195 scopus 로고    scopus 로고
    • EDEM1 accelerates the trimming of alpha1,2-linked mannose on the C branch of N-glycans
    • Hosokawa, N., Tremblay, L.O., Sleno, B., Kamiya, Y., Wada, I., Nagata, K., et al.(2010). EDEM1 accelerates the trimming of alpha1,2-linked mannose on the C branch of N-glycans. Glycobiology 20, 567-75
    • (2010) Glycobiology , vol.20 , pp. 567-575
    • Hosokawa, N.1    Tremblay, L.O.2    Sleno, B.3    Kamiya, Y.4    Wada, I.5    Nagata, K.6
  • 23
    • 0037829617 scopus 로고    scopus 로고
    • Enhancement of endoplasmic reticulum (ER degradation of misfolded Null Hong Kong alpha1-antitrypsin by human ER mannosidase i
    • Hosokawa, N., Tremblay, L.O., You, Z., Herscovics, A., Wada, I., and Nagata, K. (2003). Enhancement of endoplasmic reticulum (ER) degradation of misfolded Null Hong Kong alpha1-antitrypsin by human ER mannosidase I. J Biol Chem 278, 26287-94
    • (2003) J Biol Chem , vol.278 , pp. 26287-26294
    • Hosokawa, N.1    Tremblay, L.O.2    You, Z.3    Herscovics, A.4    Wada, I.5    Nagata, K.6
  • 24
    • 51049121849 scopus 로고    scopus 로고
    • Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP
    • Hosokawa, N., Wada, I., Nagasawa, K., Moriyama, T., Okawa, K., and Nagata, K. (2008). Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP. J Biol Chem 283, 20914-24
    • (2008) J Biol Chem , vol.283 , pp. 20914-20924
    • Hosokawa, N.1    Wada, I.2    Nagasawa, K.3    Moriyama, T.4    Okawa, K.5    Nagata, K.6
  • 25
    • 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., et al.(2004). A striking quality control subcompartment in Saccharomyces cerevisiae: The endoplasmic reticulum-associated compartment. Mol Biol Cell 15, 908-21
    • (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
  • 26
    • 79955758729 scopus 로고    scopus 로고
    • SEL1L protein critically determines the stability of the HRD1-SEL1L endoplasmic reticulumassociated degradation (ERAD) complex to optimize the degradation kinetics of ERAD substrates
    • Iida, Y., Fujimori, T., Okawa, K., Nagata, K., Wada, I., and Hosokawa, N. (2011). SEL1L protein critically determines the stability of the HRD1-SEL1L endoplasmic reticulumassociated degradation (ERAD) complex to optimize the degradation kinetics of ERAD substrates. J Biol Chem 286, 16929-39
    • (2011) J Biol Chem , vol.286 , pp. 16929-16939
    • Iida, Y.1    Fujimori, T.2    Okawa, K.3    Nagata, K.4    Wada, I.5    Hosokawa, N.6
  • 27
    • 79551600416 scopus 로고    scopus 로고
    • Fis1 and Bap31 bridge the mitochondria-ER interface to establish a platform for apoptosis induction
    • Iwasawa, R., Mahul-Mellier, A.L., Datler, C., Pazarentzos, E., and Grimm, S. (2011). Fis1 and Bap31 bridge the mitochondria- ER interface to establish a platform for apoptosis induction. EMBO J 30, 556-68
    • (2011) EMBO J , vol.30 , pp. 556-568
    • Iwasawa, R.1    Mahul-Mellier, A.L.2    Datler, C.3    Pazarentzos, E.4    Grimm, S.5
  • 29
    • 0034693217 scopus 로고    scopus 로고
    • Herp: A new ubiquitin-like membrane protein induced by endoplasmic reticulum stress
    • Kokame, K., Agarwala, K.L., Kato, H., and Miyata, T. (2000 Herp: A new ubiquitin-like membrane protein induced by endoplasmic reticulum stress. J Biol Chem 275, 32846-53
    • (2000) J Biol Chem , vol.275 , pp. 32846-32853
    • Kokame, K.1    Agarwala, K.L.2    Kato, H.3    Miyata, T.4
  • 30
    • 34548651757 scopus 로고    scopus 로고
    • PERK-dependent compartmentalization of ERAD and unfolded protein response machineries during ER stress
    • Kondratyev, M., Avezov, E., Shenkman, M., Groisman, B., and Lederkremer, G.Z. (2007). PERK-dependent compartmentalization of ERAD and unfolded protein response machineries during ER stress. Exp Cell Res 313, 3395-407
    • (2007) Exp Cell Res , vol.313 , pp. 3395-3407
    • Kondratyev, M.1    Avezov, E.2    Shenkman, M.3    Groisman, B.4    Lederkremer, G.Z.5
  • 31
    • 0028178372 scopus 로고
    • Sar1 promotes vesicle budding from the endoplasmic reticulum but not Golgi compartments
    • Kuge, O., Dascher, C., Orci, L., Rowe, T., Amherdt, M., Plutner, H., et al.(1994). Sar1 promotes vesicle budding from the endoplasmic reticulum but not Golgi compartments. J Cell Biol 125, 51-65
    • (1994) J Cell Biol , vol.125 , pp. 51-65
    • Kuge, O.1    Dascher, C.2    Orci, L.3    Rowe, T.4    Amherdt, M.5    Plutner, H.6
  • 32
    • 70349855203 scopus 로고    scopus 로고
    • Glycoprotein folding, quality control and ER-associated degradation
    • Lederkremer, G.Z. (2009). Glycoprotein folding, quality control and ER-associated degradation. Curr Opin Struct Biol 19, 515-23
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 515-523
    • Lederkremer, G.Z.1
  • 33
    • 20444429745 scopus 로고    scopus 로고
    • A window of opportunity: Timing protein degradation by trimming of sugars and ubiquitins
    • Lederkremer, G.Z., and Glickman, M.H. (2005). A window of opportunity: Timing protein degradation by trimming of sugars and ubiquitins. Trends Biochem Sci 30, 297-303
    • (2005) Trends Biochem Sci , vol.30 , pp. 297-303
    • Lederkremer, G.Z.1    Glickman, M.H.2
  • 34
    • 70349905357 scopus 로고    scopus 로고
    • Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis
    • Li, G., Mongillo, M., Chin, K.T., Harding, H., Ron, D., Marks, A.R., et al.(2009). Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis. J Cell Biol 186, 783-92
    • (2009) J Cell Biol , vol.186 , pp. 783-792
    • Li, G.1    Mongillo, M.2    Chin, K.T.3    Harding, H.4    Ron, D.5    Marks, A.R.6
  • 35
    • 33744817103 scopus 로고    scopus 로고
    • The AAA ATPase p97 links peptide N-glycanase to the endoplasmic reticulum-associated E3 ligase autocrine motility factor receptor
    • Li, G., Zhao, G., Zhou, X., Schindelin, H., and Lennarz, W.J. (2006). The AAA ATPase p97 links peptide N-glycanase to the endoplasmic reticulum-associated E3 ligase autocrine motility factor receptor. Proc Natl Acad Sci U S A 103, 8348-53
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 8348-8353
    • Li, G.1    Zhao, G.2    Zhou, X.3    Schindelin, H.4    Lennarz, W.J.5
  • 36
    • 0022467150 scopus 로고
    • Immunolocalization of the oligosaccharide trimming enzyme glucosidase II
    • Lucocq, J.M., Brada, D., and Roth, J. (1986). Immunolocalization of the oligosaccharide trimming enzyme glucosidase II. J Cell Biol 102, 2137-46
    • (1986) J Cell Biol , vol.102 , pp. 2137-2146
    • Lucocq, J.M.1    Brada, D.2    Roth, J.3
  • 37
    • 84857190393 scopus 로고    scopus 로고
    • Palmitoylated TMX and calnexin target to the mitochondria-associated membrane
    • Lynes, E.M., Bui, M., Yap, M.C., Benson, M.D., Schneider, B., Ellgaard, L., et al.(2012). Palmitoylated TMX and calnexin target to the mitochondria-associated membrane. EMBO J 31, 457-70
    • (2012) EMBO J , vol.31 , pp. 457-470
    • Lynes, E.M.1    Bui, M.2    Yap, M.C.3    Benson, M.D.4    Schneider, B.5    Ellgaard, L.6
  • 38
    • 1842791361 scopus 로고    scopus 로고
    • Herp is dually regulated by both the endoplasmic reticulum stress-specific branch of the unfolded protein response and a branch that is shared with other cellular stress pathways
    • Ma, Y., and Hendershot, L.M. (2004). Herp is dually regulated by both the endoplasmic reticulum stress-specific branch of the unfolded protein response and a branch that is shared with other cellular stress pathways. J Biol Chem 279, 13792-9
    • (2004) J Biol Chem , vol.279 , pp. 13792-13799
    • Ma, Y.1    Hendershot, L.M.2
  • 40
    • 28844453210 scopus 로고    scopus 로고
    • The type III inositol 1 4,5-trisphosphate receptor preferentially transmits apoptotic Ca2 + signals into mitochondria
    • Mendes, C.C., Gomes, D.A., Thompson, M., Souto, N.C., Goes, T.S., Goes, A.M., et al.(2005). The type III inositol 1,4,5-trisphosphate receptor preferentially transmits apoptotic Ca2 + signals into mitochondria. J Biol Chem 280, 40892-900
    • (2005) J Biol Chem , vol.280 , pp. 40892-40900
    • Mendes, C.C.1    Gomes, D.A.2    Thompson, M.3    Souto, N.C.4    Goes, T.S.5    Goes, A.M.6
  • 41
    • 0036911213 scopus 로고    scopus 로고
    • A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins
    • Meunier, L., Usherwood, Y.K., Chung, K.T., and Hendershot, L.M. (2002). A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins. Mol Biol Cell 13, 4456-69
    • (2002) Mol Biol Cell , vol.13 , pp. 4456-4469
    • Meunier, L.1    Usherwood, Y.K.2    Chung, K.T.3    Hendershot, L.M.4
  • 43
    • 36249022750 scopus 로고    scopus 로고
    • Characterization of an ERAD pathway for nonglycosylated BiP substrates, which require Herp
    • Okuda-Shimizu, Y., and Hendershot, L.M. (2007). Characterization of an ERAD pathway for nonglycosylated BiP substrates, which require Herp. Mol Cell 28, 544-54
    • (2007) Mol Cell , vol.28 , pp. 544-554
    • Okuda-Shimizu, Y.1    Hendershot, L.M.2
  • 44
    • 33748795800 scopus 로고    scopus 로고
    • EDEM1 regulates ER-associated degra- dation by accelerating de-mannosylation of folding-defective polypeptides and by inhibiting their covalent aggregation
    • Olivari, S., Cali, T., Salo, K.E., Paganetti, P., Ruddock, L.W., and Molinari, M. (2006). EDEM1 regulates ER-associated degra- dation by accelerating de-mannosylation of folding-defective polypeptides and by inhibiting their covalent aggregation. Biochem Biophys Res Commun 349, 1278-84
    • (2006) Biochem Biophys Res Commun , vol.349 , pp. 1278-1284
    • Olivari, S.1    Cali, T.2    Salo, K.E.3    Paganetti, P.4    Ruddock, L.W.5    Molinari, M.6
  • 46
    • 80051686315 scopus 로고    scopus 로고
    • Golgi localization of ERManI defines spatial separation of the mammalian glycoprotein quality control system
    • Pan, S., Wang, S., Utama, B., Huang, L., Blok, N., Estes, M.K., et al.(2011). Golgi localization of ERManI defines spatial separation of the mammalian glycoprotein quality control system. Mol Biol Cell 22, 2810-22
    • (2011) Mol Biol Cell , vol.22 , pp. 2810-2822
    • Pan, S.1    Wang, S.2    Utama, B.3    Huang, L.4    Blok, N.5    Estes, M.K.6
  • 47
    • 84871726622 scopus 로고    scopus 로고
    • Where the endoplasmic reticulum and the mitochondrion tie the knot: The mitochondria- associated membrane (MAM
    • Epub ahead of print]; DOI: 10.1016/j.bbamcr.2012 04.013. in press
    • Raturi, A., and Simmen, T. (2012). Where the endoplasmic reticulum and the mitochondrion tie the knot: The mitochondria-associated membrane (MAM). Biochim Biophys Acta [Epub ahead of print]; DOI: 10.1016/j.bbamcr.2012 04.013. (in press
    • (2012) Biochim Biophys Acta
    • Raturi, A.1    Simmen, T.2
  • 48
    • 77956525570 scopus 로고    scopus 로고
    • Coronaviruses hijack the LC3-Ipositive EDEMosomes, ER-derived vesicles exporting shortlived ERAD regulators, for replication
    • Reggiori, F., Monastyrska, I., Verheije, M.H., Cali, T., Ulasli, M., Bianchi, S., et al.(2010). Coronaviruses hijack the LC3-Ipositive EDEMosomes, ER-derived vesicles exporting shortlived ERAD regulators, for replication. Cell Host Microbe 7, 500-8
    • (2010) Cell Host Microbe , vol.7 , pp. 500-508
    • Reggiori, F.1    Monastyrska, I.2    Verheije, M.H.3    Cali, T.4    Ulasli, M.5    Bianchi, S.6
  • 49
    • 0034640960 scopus 로고    scopus 로고
    • Cytosolic phosphorylation of calnexin controls intracellular Ca 2 + oscillations via an interaction with SERCA2b
    • Roderick, H.L., Lechleiter, J.D., and Camacho, P. (2000). Cytosolic phosphorylation of calnexin controls intracellular Ca(2 +) oscillations via an interaction with SERCA2b. J Cell Biol 149, 1235-48
    • (2000) J Cell Biol , vol.149 , pp. 1235-1248
    • Roderick, H.L.1    Lechleiter, J.D.2    Camacho, P.3
  • 50
    • 79952705597 scopus 로고    scopus 로고
    • Integrating stress signals at the endoplasmic reticulum: The BCL-2 protein family rheostat
    • Rodriguez, D., Rojas-Rivera, D., and Hetz, C. (2011). Integrating stress signals at the endoplasmic reticulum: The BCL-2 protein family rheostat. Biochim Biophys Acta 1813, 564-74
    • (2011) Biochim Biophys Acta , vol.1813 , pp. 564-574
    • Rodriguez, D.1    Rojas-Rivera, D.2    Hetz, C.3
  • 52
    • 1042292018 scopus 로고    scopus 로고
    • Endoplasmic reticulum-localized amyloid beta-peptide is degraded in the cytosol by two distinct degradation pathways
    • Schmitz, A., Schneider, A., Kummer, M.P., and Herzog, V. (2004). Endoplasmic reticulum-localized amyloid beta-peptide is degraded in the cytosol by two distinct degradation pathways. Traffic 5, 89-101
    • (2004) Traffic , vol.5 , pp. 89-101
    • Schmitz, A.1    Schneider, A.2    Kummer, M.P.3    Herzog, V.4
  • 53
    • 28144436887 scopus 로고    scopus 로고
    • The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway
    • Schulze,A., Standera, S., Buerger, E., Kikkert, M., van Voorden, S., Wiertz, E., et al.(2005). The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway. J Mol Biol 354, 1021-7
    • (2005) J Mol Biol , vol.354 , pp. 1021-1027
    • Schulze, A.1    Standera, S.2    Buerger, E.3    Kikkert, M.4    Van Voorden, S.5    Wiertz, E.6
  • 54
    • 20144385980 scopus 로고    scopus 로고
    • PACS-2 controls endoplasmic reticulum-mitochondria communication and Bid-mediated apoptosis
    • Simmen, T., Aslan, J.E., Blagoveshchenskaya, A.D., Thomas, L., Wan, L., Xiang, Y., et al.(2005). PACS-2 controls endoplasmic reticulum-mitochondria communication and Bid-mediated apoptosis. EMBO J 24, 717-29
    • (2005) EMBO J , vol.24 , pp. 717-729
    • Simmen, T.1    Aslan, J.E.2    Blagoveshchenskaya, A.D.3    Thomas, L.4    Wan, L.5    Xiang, Y.6
  • 55
    • 0035999994 scopus 로고    scopus 로고
    • Probing for membrane domains in the endoplasmic reticulum: Retention and degradation of unassembled MHC class i molecules
    • Spiliotis, E.T., Pentcheva, T., and Edidin, M. (2002). Probing for membrane domains in the endoplasmic reticulum: Retention and degradation of unassembled MHC class I molecules. Mol Biol Cell 13, 1566-81
    • (2002) Mol Biol Cell , vol.13 , pp. 1566-1581
    • Spiliotis, E.T.1    Pentcheva, T.2    Edidin, M.3
  • 56
    • 78650143172 scopus 로고    scopus 로고
    • Sorting things out through endoplasmic reticulum quality control
    • Tamura, T., Sunryd, J.C., and Hebert, D.N. (2010). Sorting things out through endoplasmic reticulum quality control. Mol Membr Biol 27, 412-27
    • (2010) Mol Membr Biol , vol.27 , pp. 412-427
    • Tamura, T.1    Sunryd, J.C.2    Hebert, D.N.3
  • 57
    • 0034598991 scopus 로고    scopus 로고
    • The novel MMS-inducible gene Mif1/KIAA0025 is a target of the unfolded protein response pathway
    • van Laar T., Schouten, T., Hoogervorst, E., van Eck, M., van der Eb, A.J., and Terleth, C. (2000). The novel MMS-inducible gene Mif1/KIAA0025 is a target of the unfolded protein response pathway. FEBS Lett 469, 123-31
    • (2000) FEBS Lett , vol.469 , pp. 123-131
    • Van Laar, T.1    Schouten, T.2    Hoogervorst, E.3    Van Eck, M.4    Van Der Eb, A.J.5    Terleth, C.6
  • 58
    • 0025273937 scopus 로고
    • Phospholipid synthesis in a membrane fraction associated with mitochondria
    • Vance, J.E. (1990). Phospholipid synthesis in a membrane fraction associated with mitochondria. J Biol Chem 265, 7248-56
    • (1990) J Biol Chem , vol.265 , pp. 7248-7256
    • Vance, J.E.1
  • 59
    • 84870984470 scopus 로고    scopus 로고
    • PERK is required at the ERmitochondrial contact sites to convey apoptosis after ROSbased ER stress
    • Verfaillie, T., Rubio, N., Garg, A.D., Bultynck, G., Rizzuto, R., Decuypere, J.P., et al.(2012). PERK is required at the ERmitochondrial contact sites to convey apoptosis after ROSbased ER stress. Cell Death Differ 19, 1880-91
    • (2012) Cell Death Differ , vol.19 , pp. 1880-1891
    • Verfaillie, T.1    Rubio, N.2    Garg, A.D.3    Bultynck, G.4    Rizzuto, R.5    Decuypere, J.P.6
  • 60
    • 34249069585 scopus 로고    scopus 로고
    • Real-time fluorescence detection of ERAD substrate retrotranslocation in a mammalian in vitro system
    • Wahlman, J., DeMartino, G.N., Skach, W.R., Bulleid, N.J., Brodsky, J.L., and Johnson, A.E. (2007). Real-time fluorescence detection of ERAD substrate retrotranslocation in a mammalian in vitro system. Cell 129, 943-55
    • (2007) Cell , vol.129 , pp. 943-955
    • Wahlman, J.1    Demartino, G.N.2    Skach, W.R.3    Bulleid, N.J.4    Brodsky, J.L.5    Johnson, A.E.6
  • 61
    • 48249138088 scopus 로고    scopus 로고
    • Bap31 is an itinerant protein that moves between the peripheral endoplasmic reticulum (ER and a juxtanuclear compartment related to ER-associated degradation
    • Wakana, Y., Takai, S., Nakajima, K., Tani, K., Yamamoto, A., Watson, P., et al.(2008). Bap31 is an itinerant protein that moves between the peripheral endoplasmic reticulum (ER and a juxtanuclear compartment related to ER-associated degradation. Mol Biol Cell 19, 1825-36
    • (2008) Mol Biol Cell , vol.19 , pp. 1825-1836
    • Wakana, Y.1    Takai, S.2    Nakajima, K.3    Tani, K.4    Yamamoto, A.5    Watson, P.6
  • 62
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • Walter, P., and Ron, D (2011). The unfolded protein response: from stress pathway to homeostatic regulation. Science 334, 1081-6
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 63
    • 44649096231 scopus 로고    scopus 로고
    • BAP31 interacts with Sec61 translocons and promotes retrotranslocation of CFTRDeltaF508via the derlin-1 complex
    • Wang, B., Heath-Engel, H., Zhang, D., Nguyen, N., Thomas, D.Y., Hanrahan, J.W., et al.(2008). BAP31 interacts with Sec61 translocons and promotes retrotranslocation of CFTRDeltaF508 via the derlin-1 complex. Cell 133, 1080-92
    • (2008) Cell , vol.133 , pp. 1080-1092
    • Wang, B.1    Heath-Engel, H.2    Zhang, D.3    Nguyen, N.4    Thomas, D.Y.5    Hanrahan, J.W.6
  • 64
    • 0038487228 scopus 로고    scopus 로고
    • Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: Dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains
    • Ye, Y., Meyer, H.H., and Rapoport, T.A. (2003). Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: Dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J Cell Biol 162, 71-84
    • (2003) J Cell Biol , vol.162 , pp. 71-84
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 65
    • 0037320265 scopus 로고    scopus 로고
    • A time-dependent phase shift in the mammalian unfolded protein response
    • Yoshida, H., Matsui, T., Hosokawa, N., Kaufman, R.J., Nagata, K., and Mori, K. (2003). A time-dependent phase shift in the mammalian unfolded protein response. Dev Cell 4, 265-71
    • (2003) Dev Cell , vol.4 , pp. 265-271
    • Yoshida, H.1    Matsui, T.2    Hosokawa, N.3    Kaufman, R.J.4    Nagata, K.5    Mori, K.6
  • 66
    • 34248356819 scopus 로고    scopus 로고
    • EDEM1 reveals a quality control vesicular transport pathway out of the endoplasmic reticulum not involving the COPII exit sites
    • Zuber, C., Cormier, J.H., Guhl, B., Santimaria, R., Hebert, D.N., and Roth, J. (2007). EDEM1 reveals a quality control vesicular transport pathway out of the endoplasmic reticulum not involving the COPII exit sites. Proc Natl Acad Sci U S A 104, 4407-12
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 4407-4412
    • Zuber, C.1    Cormier, J.H.2    Guhl, B.3    Santimaria, R.4    Hebert, D.N.5    Roth, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.