메뉴 건너뛰기




Volumn 35, Issue 4, 2013, Pages 291-297

Inhibition of endoplasmic reticulum associated degradation reduces endoplasmic reticulum stress and alters lysosomal morphology and distribution

Author keywords

Alzheimer's disease; endoplasmic reticulum stress; lysosome; unfolded protein response

Indexed keywords

CATHEPSIN D; KIFUNENSINE; LYSOSOME ASSOCIATED MEMBRANE PROTEIN 1;

EID: 84880698490     PISSN: 10168478     EISSN: 02191032     Source Type: Journal    
DOI: 10.1007/s10059-013-2286-9     Document Type: Article
Times cited : (16)

References (36)
  • 1
    • 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
    • 18003979 10.1091/mbc.E07-05-0505 1:CAS:528:DC%2BD1cXlslensbY%3D
    • Avezov, E., Frenkel, Z., Ehrlich, M., Herscovics, A., and Lederkremer, G.Z. (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, 216-225.
    • (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
  • 2
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • 18276881 10.1126/science.1141448 1:CAS:528:DC%2BD1cXhslOmtLw%3D
    • Balch, W.E., Morimoto, R.I., Dillin, A., and Kelly, J.W. (2008). Adapting proteostasis for disease intervention. Science 319, 916-919.
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 3
    • 33845480131 scopus 로고    scopus 로고
    • Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response
    • 17132049 10.1371/journal.pbio.0040423
    • Bernales, S., McDonald, K.L., and Walter, P. (2006). Autophagy counterbalances endoplasmic reticulum expansion during the unfolded protein response. PLoS Biol. 4, e423.
    • (2006) PLoS Biol. , vol.4 , pp. 423
    • Bernales, S.1    McDonald, K.L.2    Walter, P.3
  • 4
    • 34248581851 scopus 로고    scopus 로고
    • ER-phagy: Selective autophagy of the endoplasmic reticulum
    • 17351330
    • Bernales, S., Schuck, S., and Walter, P. (2007). ER-phagy: selective autophagy of the endoplasmic reticulum. Autophagy 3, 285-287.
    • (2007) Autophagy , vol.3 , pp. 285-287
    • Bernales, S.1    Schuck, S.2    Walter, P.3
  • 5
    • 43549087339 scopus 로고    scopus 로고
    • Segregation and rapid turnover of EDEM1 by an autophagy-like mechanism modulates standard ERAD and folding activities
    • 18452703 10.1016/j.bbrc.2008.04.098 1:CAS:528:DC%2BD1cXmsVehu70%3D
    • 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, 405-410.
    • (2008) Biochem. Biophys. Res. Commun. , vol.371 , pp. 405-410
    • Cali, T.1    Galli, C.2    Olivari, S.3    Molinari, M.4
  • 6
    • 33947497050 scopus 로고    scopus 로고
    • Differential effects of endoplasmic reticulum stress-induced autophagy on cell survival
    • 17135238 10.1074/jbc.M609267200 1:CAS:528:DC%2BD2sXhsFKgsLs%3D
    • Ding, W.X., Ni, H.M., Gao, W., Hou, Y.F., Melan, M.A., Chen, X., Stolz, D.B., Shao, Z.M., and Yin, X.M. (2007). Differential effects of endoplasmic reticulum stress-induced autophagy on cell survival. J. Biol. Chem. 282, 4702-4710.
    • (2007) J. Biol. Chem. , vol.282 , pp. 4702-4710
    • Ding, W.X.1    Ni, H.M.2    Gao, W.3    Hou, Y.F.4    Melan, M.A.5    Chen, X.6    Stolz, D.B.7    Shao, Z.M.8    Yin, X.M.9
  • 7
    • 84858022581 scopus 로고    scopus 로고
    • Rab6 is a modulator of the unfolded protein response: Implications for Alzheimer's disease
    • 22124028 1:CAS:528:DC%2BC38XisFejtbw%3D
    • Elfrink, H.L., Zwart, R., Cavanillas, M.L., Schindler, A.J., Baas, F., and Scheper, W. (2012). Rab6 is a modulator of the unfolded protein response: implications for Alzheimer's disease. J. Alzheimers Dis. 28, 917-929.
    • (2012) J. Alzheimers Dis. , vol.28 , pp. 917-929
    • Elfrink, H.L.1    Zwart, R.2    Cavanillas, M.L.3    Schindler, A.J.4    Baas, F.5    Scheper, W.6
  • 8
    • 0035918223 scopus 로고    scopus 로고
    • Glycoprotein quality control in the endoplasmic reticulum. Mannose trimming by endoplasmic reticulum mannosidase i times the proteasomal degradation of unassembled immunoglobulin subunits
    • 11278527 10.1074/jbc.M009603200 1:CAS:528:DC%2BD3MXjtFynu7o%3D
    • Fagioli, C., and Sitia, R. (2001). Glycoprotein quality control in the endoplasmic reticulum. Mannose trimming by endoplasmic reticulum mannosidase I times the proteasomal degradation of unassembled immunoglobulin subunits. J. Biol. Chem. 276, 12885-12892.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12885-12892
    • Fagioli, C.1    Sitia, R.2
  • 9
    • 84863045190 scopus 로고    scopus 로고
    • The synaptic vesicle SNARE neuronal Synaptobrevin promotes endolysosomal degradation and prevents neurodegeneration
    • 22270918 10.1083/jcb.201108088 1:CAS:528:DC%2BC38XhsFymtb8%3D
    • Haberman, A., Williamson, W.R., Epstein, D., Wang, D., Rina, S., Meinertzhagen, I.A., and Hiesinger, P.R. (2012). The synaptic vesicle SNARE neuronal Synaptobrevin promotes endolysosomal degradation and prevents neurodegeneration. J. Cell Biol. 196, 261-276.
    • (2012) J. Cell Biol. , vol.196 , pp. 261-276
    • Haberman, A.1    Williamson, W.R.2    Epstein, D.3    Wang, D.4    Rina, S.5    Meinertzhagen, I.A.6    Hiesinger, P.R.7
  • 10
    • 0037353039 scopus 로고    scopus 로고
    • An integrated stress response regulates amino acid metabolism and resis-tance to oxidative stress
    • 12667446 10.1016/S1097-2765(03)00105-9 1:CAS:528:DC%2BD3sXjtVWkt74%3D
    • Harding, H.P., Zhang, Y., Zeng, H., Novoa, I., Lu, P.D., Calfon, M., Sadri, N., Yun, C., Popko, B., Paules, R., et al. (2003). An integrated stress response regulates amino acid metabolism and resis-tance to oxidative stress. Mol. Cell 11, 619-633.
    • (2003) Mol. Cell , vol.11 , pp. 619-633
    • Harding, H.P.1    Zhang, Y.2    Zeng, H.3    Novoa, I.4    Lu, P.D.5    Calfon, M.6    Sadri, N.7    Yun, C.8    Popko, B.9    Paules, R.10
  • 11
    • 21744447192 scopus 로고    scopus 로고
    • The glycan code of the endoplasmic reticulum: Asparagine-linked carbohydrates as protein maturation and quality-control tags
    • 15939591 10.1016/j.tcb.2005.05.007 1:CAS:528:DC%2BD2MXlvFygt7o%3D
    • Hebert, D.N., Garman, S.C., and Molinari, M. (2005). The glycan code of the endoplasmic reticulum: asparagine-linked carbohydrates as protein maturation and quality-control tags. Trends Cell Biol. 15, 364-370.
    • (2005) Trends Cell Biol. , vol.15 , pp. 364-370
    • Hebert, D.N.1    Garman, S.C.2    Molinari, M.3
  • 12
    • 70349627027 scopus 로고    scopus 로고
    • XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy
    • 19762508 10.1101/gad.1830709 1:CAS:528:DC%2BD1MXht12qtbfP
    • Hetz, C., Thielen, P., Matus, S., Nassif, M., Court, F., Kiffin, R., Martinez, G., Cuervo, A.M., Brown, R.H., and Glimcher, L.H. (2009). XBP-1 deficiency in the nervous system protects against amyotrophic lateral sclerosis by increasing autophagy. Genes Dev. 23, 2294-2306.
    • (2009) Genes Dev. , vol.23 , pp. 2294-2306
    • Hetz, C.1    Thielen, P.2    Matus, S.3    Nassif, M.4    Court, F.5    Kiffin, R.6    Martinez, G.7    Cuervo, A.M.8    Brown, R.H.9    Glimcher, L.H.10
  • 14
    • 65349093893 scopus 로고    scopus 로고
    • The Unfolded Protein Response is activated in pretangle neurons in Alzheimer's disease hippocampus
    • 19264902 10.2353/ajpath.2009.080814 1:CAS:528:DC%2BD1MXksVOkt74%3D
    • Hoozemans, J.J.M., Van Haastert, E.S., Nijholt, D.A.T., Rozemuller, A.J.M., Eikelenboom, P., and Scheper, W. (2009). The Unfolded Protein Response is activated in pretangle neurons in Alzheimer's disease hippocampus. Am. J. Pathol. 174, 1241-1251.
    • (2009) Am. J. Pathol. , vol.174 , pp. 1241-1251
    • Hoozemans, J.J.M.1    Van Haastert, E.S.2    Nijholt, D.A.T.3    Rozemuller, A.J.M.4    Eikelenboom, P.5    Scheper, W.6
  • 15
    • 0037829617 scopus 로고    scopus 로고
    • Enhancement of endoplasmic reticulum (ER) degradation of misfolded Null Hong Kong alpha1-Antitrypsin by human ER mannosidase i
    • 12736254 10.1074/jbc.M303395200 1:CAS:528:DC%2BD3sXlt1CltbY%3D
    • 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, 26287-26294.
    • (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
  • 16
    • 33646204392 scopus 로고    scopus 로고
    • Generation of cell lines with tetracycline-regulated autophagy and a role for autophagy in controlling cell size
    • 16647067 10.1016/j.febslet.2006.04.008 1:CAS:528:DC%2BD28XksFaqsr4%3D
    • Hosokawa, N., Hara, Y., and Mizushima, N. (2006). Generation of cell lines with tetracycline-regulated autophagy and a role for autophagy in controlling cell size. FEBS Lett. 580, 2623-2629.
    • (2006) FEBS Lett. , vol.580 , pp. 2623-2629
    • Hosokawa, N.1    Hara, Y.2    Mizushima, N.3
  • 17
    • 0141816730 scopus 로고    scopus 로고
    • Cytosol-endoplasmic reticulum interplay by Sec61alpha translocon in polyglutamine-mediated neurotoxicity in Drosophila
    • 14504396 10.1073/pnas.1934748100 1:CAS:528:DC%2BD3sXotFKmtbg%3D
    • Kanuka, H., Kuranaga, E., Hiratou, T., Igaki, T., Nelson, B., Okano, H., and Miura, M. (2003). Cytosol-endoplasmic reticulum interplay by Sec61alpha translocon in polyglutamine-mediated neurotoxicity in Drosophila. Proc. Natl. Acad. Sci. USA 100, 11723-11728.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 11723-11728
    • Kanuka, H.1    Kuranaga, E.2    Hiratou, T.3    Igaki, T.4    Nelson, B.5    Okano, H.6    Miura, M.7
  • 18
    • 27944438529 scopus 로고    scopus 로고
    • Gain-offunction screen identifies a role of the Sec61alpha translocon in Drosophila postmitotic neurotoxicity
    • 16243437 10.1016/j.bbagen.2005.06.020 1:CAS:528:DC%2BD2MXht1Gns77O
    • Kanuka, H., Hiratou, T., Igaki, T., Kanda, H., Kuranaga, E., Sawamoto, K., Aigaki, T., Okano, H., and Miura, M. (2005). Gain-offunction screen identifies a role of the Sec61alpha translocon in Drosophila postmitotic neurotoxicity. Biochim. Biophys. Acta 1726, 225-237.
    • (2005) Biochim. Biophys. Acta , vol.1726 , pp. 225-237
    • Kanuka, H.1    Hiratou, T.2    Igaki, T.3    Kanda, H.4    Kuranaga, E.5    Sawamoto, K.6    Aigaki, T.7    Okano, H.8    Miura, M.9
  • 21
    • 0037470410 scopus 로고    scopus 로고
    • Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle
    • 12610306 10.1126/science.1079474 1:CAS:528:DC%2BD3sXhsFWrs7s%3D
    • Molinari, M., Calanca, V., Galli, C., Lucca, P., and Paganetti, P. (2003). Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle. Science 299, 1397-1400.
    • (2003) Science , vol.299 , pp. 1397-1400
    • Molinari, M.1    Calanca, V.2    Galli, C.3    Lucca, P.4    Paganetti, P.5
  • 22
    • 43149096666 scopus 로고    scopus 로고
    • The recognition and retrotranslocation of misfolded proteins from the endoplasmic reticulum
    • 18315532 10.1111/j.1600-0854.2008.00729.x 1:CAS:528:DC%2BD1cXntlamsLs%3D
    • Nakatsukasa, K., and Brodsky, J.L. (2008). The recognition and retrotranslocation of misfolded proteins from the endoplasmic reticulum. Traffic 9, 861-870.
    • (2008) Traffic , vol.9 , pp. 861-870
    • Nakatsukasa, K.1    Brodsky, J.L.2
  • 24
    • 79957947433 scopus 로고    scopus 로고
    • Removing protein aggregates: The role of proteolysis in neurodegeneration
    • 21568912 10.2174/092986711795843236 1:CAS:528:DC%2BC3MXotFOrtr8%3D
    • Nijholt, D.A., De, K.L., Elfrink, H.L., Hoozemans, J.J., and Scheper, W. (2011b). Removing protein aggregates: the role of proteolysis in neurodegeneration. Curr. Med. Chem. 18, 2459-2476.
    • (2011) Curr. Med. Chem. , vol.18 , pp. 2459-2476
    • Nijholt, D.A.1    De, K.L.2    Elfrink, H.L.3    Hoozemans, J.J.4    Scheper, W.5
  • 25
    • 84858000638 scopus 로고    scopus 로고
    • The unfolded protein response is associated with early tau pathology in the hippocampus of tauopathies
    • 22102449 10.1002/path.3969 1:CAS:528:DC%2BC38XjsVWht7w%3D
    • Nijholt, D.A., Van Haastert, E.S., Rozemuller, A.J., Scheper, W., and Hoozemans, J.J. (2012). The unfolded protein response is associated with early tau pathology in the hippocampus of tauopathies. J. Pathol. 226, 693-702.
    • (2012) J. Pathol. , vol.226 , pp. 693-702
    • Nijholt, D.A.1    Van Haastert, E.S.2    Rozemuller, A.J.3    Scheper, W.4    Hoozemans, J.J.5
  • 26
    • 79955969705 scopus 로고    scopus 로고
    • Autophagy failure in Alzheimer's disease-locating the primary defect
    • 21296668 10.1016/j.nbd.2011.01.021 1:CAS:528:DC%2BC3MXmtFCktbw%3D
    • Nixon, R.A., and Yang, D.S. (2011). Autophagy failure in Alzheimer's disease-locating the primary defect. Neurobiol. Dis. 43, 38-45.
    • (2011) Neurobiol. Dis. , vol.43 , pp. 38-45
    • Nixon, R.A.1    Yang, D.S.2
  • 28
    • 80051519015 scopus 로고    scopus 로고
    • Mutations in the alpha 1,2-mannosidase gene, MAN1B1, cause autosomal-recessive intellectual disability
    • 21763484 10.1016/j.ajhg.2011.06.006 1:CAS:528:DC%2BC3MXovF2mt7Y%3D
    • Rafiq, M.A., Kuss, A.W., Puettmann, L., Noor, A., Ramiah, A., Ali, G., Hu, H., Kerio, N.A., Xiang, Y., Garshasbi, M., et al. (2011). Mutations in the alpha 1,2-mannosidase gene, MAN1B1, cause autosomal-recessive intellectual disability. Am. J. Hum. Genet. 89, 176-182.
    • (2011) Am. J. Hum. Genet. , vol.89 , pp. 176-182
    • Rafiq, M.A.1    Kuss, A.W.2    Puettmann, L.3    Noor, A.4    Ramiah, A.5    Ali, G.6    Hu, H.7    Kerio, N.A.8    Xiang, Y.9    Garshasbi, M.10
  • 29
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • 17565364 10.1038/nrm2199 1:CAS:528:DC%2BD2sXmvVaktLY%3D
    • Ron, D., and Walter, P. (2007). Signal integration in the endoplasmic reticulum unfolded protein response. Nat. Rev. Mol. Cell Biol. 8, 519-529.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 30
    • 80655144729 scopus 로고    scopus 로고
    • Bypass of glycan-dependent glycoprotein delivery to ERAD by up-regulated EDEM1
    • 21917589 10.1091/mbc.E10-12-0944 1:CAS:528:DC%2BC3MXhsV2qu7jL
    • Ron, E., Shenkman, M., Groisman, B., Izenshtein, Y., Leitman, J., and Lederkremer, G.Z. (2011). Bypass of glycan-dependent glycoprotein delivery to ERAD by up-regulated EDEM1. Mol. Biol. Cell 22, 3945-3954.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 3945-3954
    • Ron, E.1    Shenkman, M.2    Groisman, B.3    Izenshtein, Y.4    Leitman, J.5    Lederkremer, G.Z.6
  • 31
    • 63149175877 scopus 로고    scopus 로고
    • Endoplasmic reticulum protein quality control in neurodegenerative disease: The good, the bad and the therapy
    • 19199926 10.2174/092986709787458506 1:CAS:528:DC%2BD1MXjsFGqsbs%3D
    • Scheper, W., and Hoozemans, J.J. (2009). Endoplasmic reticulum protein quality control in neurodegenerative disease: the good, the bad and the therapy. Curr. Med. Chem. 16, 615-626.
    • (2009) Curr. Med. Chem. , vol.16 , pp. 615-626
    • Scheper, W.1    Hoozemans, J.J.2
  • 32
    • 79961124071 scopus 로고    scopus 로고
    • The unfolded protein response and proteostasis in Alzheimer disease: Preferential activation of autophagy by endoplasmic reticulum stress
    • 21494086 10.4161/auto.7.8.15761
    • Scheper, W., Nijholt, D.A., and Hoozemans, J.J. (2011). The unfolded protein response and proteostasis in Alzheimer disease: preferential activation of autophagy by endoplasmic reticulum stress. Autophagy 7, 910-911.
    • (2011) Autophagy , vol.7 , pp. 910-911
    • Scheper, W.1    Nijholt, D.A.2    Hoozemans, J.J.3
  • 33
    • 33748789479 scopus 로고    scopus 로고
    • Mediators of endoplasmic reticulum stress-induced apoptosis
    • 16953201 10.1038/sj.embor.7400779 1:CAS:528:DC%2BD28XptVSlsLo%3D
    • Szegezdi, E., Logue, S.E., Gorman, A.M., and Samali, A. (2006). Mediators of endoplasmic reticulum stress-induced apoptosis. EMBO Rep. 7, 880-885.
    • (2006) EMBO Rep. , vol.7 , pp. 880-885
    • Szegezdi, E.1    Logue, S.E.2    Gorman, A.M.3    Samali, A.4
  • 34
    • 84871197818 scopus 로고    scopus 로고
    • Unassembled CD147 is an endogenous endoplasmic reticulum-Associated degradation substrate
    • 23097496 10.1091/mbc.E12-06-0428 1:CAS:528:DC%2BC3sXps1GgsQ%3D%3D
    • Tyler, R.E., Pearce, M.M., Shaler, T.A., Olzmann, J.A., Greenblatt, E.J., and Kopito, R.R. (2012). Unassembled CD147 is an endogenous endoplasmic reticulum-Associated degradation substrate. Mol. Biol. Cell 23, 4668-4678.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 4668-4678
    • Tyler, R.E.1    Pearce, M.M.2    Shaler, T.A.3    Olzmann, J.A.4    Greenblatt, E.J.5    Kopito, R.R.6
  • 35
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: Endoplasmic reticulum-Associated degradation
    • 19002207 10.1038/nrm2546 1:CAS:528:DC%2BD1cXhsVWhurjI
    • Vembar, S.S., and Brodsky, J.L. (2008). One step at a time: endoplasmic reticulum-Associated degradation. Nat. Rev. Mol. Cell Biol. 9, 944-957.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 36
    • 83355169702 scopus 로고    scopus 로고
    • Inhibition of endoplasmic reticulum-Associated degradation rescues native folding in loss of function protein misfolding diseases
    • 22006919 10.1074/jbc.M111.274332 1:CAS:528:DC%2BC3MXhs1ShurfE
    • Wang, F., Song, W., Brancati, G., and Segatori, L. (2011). Inhibition of endoplasmic reticulum-Associated degradation rescues native folding in loss of function protein misfolding diseases. J. Biol. Chem. 286, 43454-43464.
    • (2011) J. Biol. Chem. , vol.286 , pp. 43454-43464
    • Wang, F.1    Song, W.2    Brancati, G.3    Segatori, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.