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Volumn 54, Issue 1, 2014, Pages 166-179

Quality Control Autophagy Degrades Soluble ERAD-Resistant Conformers of the Misfolded Membrane Protein GnRHR

Author keywords

[No Author keywords available]

Indexed keywords

BECLIN 1; BORTEZOMIB; CHLOROQUINE; GONADORELIN RECEPTOR; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN P97; ATM PROTEIN; BIOLOGICAL MARKER; CALNEXIN; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; MEMBRANE PROTEIN; PHOSPHATIDYLINOSITOL 3 PHOSPHATE; PROTEASOME; SEL1L PROTEIN; TRITON X 100; TUBULIN; UNCLASSIFIED DRUG;

EID: 84897986050     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2014.02.025     Document Type: Article
Times cited : (128)

References (38)
  • 1
    • 0028971172 scopus 로고
    • Sequential coupling between COPII and COPI vesicle coats in endoplasmic reticulum to Golgi transport
    • Aridor M., Bannykh S.I., Rowe T., Balch W.E. Sequential coupling between COPII and COPI vesicle coats in endoplasmic reticulum to Golgi transport. J.Cell Biol. 1995, 131:875-893.
    • (1995) J.Cell Biol. , vol.131 , pp. 875-893
    • Aridor, M.1    Bannykh, S.I.2    Rowe, T.3    Balch, W.E.4
  • 2
    • 50249084987 scopus 로고    scopus 로고
    • Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum
    • Axe E.L., Walker S.A., Manifava M., Chandra P., Roderick H.L., Habermann A., Griffiths G., Ktistakis N.T. Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum. J.Cell Biol. 2008, 182:685-701.
    • (2008) J.Cell Biol. , vol.182 , pp. 685-701
    • Axe, E.L.1    Walker, S.A.2    Manifava, M.3    Chandra, P.4    Roderick, H.L.5    Habermann, A.6    Griffiths, G.7    Ktistakis, N.T.8
  • 3
    • 74049099496 scopus 로고    scopus 로고
    • Protein disulfide isomerase chaperone ERP-57 decreases plasma membrane expression of the human GnRH receptor
    • Ayala Yáñez R., Conn P.M. Protein disulfide isomerase chaperone ERP-57 decreases plasma membrane expression of the human GnRH receptor. Cell Biochem. Funct. 2010, 28:66-73.
    • (2010) Cell Biochem. Funct. , vol.28 , pp. 66-73
    • Ayala Yáñez, R.1    Conn, P.M.2
  • 4
    • 34248581851 scopus 로고    scopus 로고
    • ER-phagy: selective autophagy of the endoplasmic reticulum
    • Bernales S., Schuck S., Walter P. ER-phagy: selective autophagy of the endoplasmic reticulum. Autophagy 2007, 3:285-287.
    • (2007) Autophagy , vol.3 , pp. 285-287
    • Bernales, S.1    Schuck, S.2    Walter, P.3
  • 6
    • 84870907436 scopus 로고    scopus 로고
    • Cleaning up: ER-associated degradation to the rescue
    • Brodsky J.L. Cleaning up: ER-associated degradation to the rescue. Cell 2012, 151:1163-1167.
    • (2012) Cell , vol.151 , pp. 1163-1167
    • Brodsky, J.L.1
  • 9
    • 80052682475 scopus 로고    scopus 로고
    • Pharmacological chaperones for misfolded gonadotropin-releasing hormone receptors
    • Conn P.M., Ulloa-Aguirre A. Pharmacological chaperones for misfolded gonadotropin-releasing hormone receptors. Adv. Pharmacol. 2011, 62:109-141.
    • (2011) Adv. Pharmacol. , vol.62 , pp. 109-141
    • Conn, P.M.1    Ulloa-Aguirre, A.2
  • 10
    • 67549142261 scopus 로고    scopus 로고
    • Life and death partners: apoptosis, autophagy and the cross-talk between them
    • Eisenberg-Lerner A., Bialik S., Simon H.U., Kimchi A. Life and death partners: apoptosis, autophagy and the cross-talk between them. Cell Death Differ. 2009, 16:966-975.
    • (2009) Cell Death Differ. , vol.16 , pp. 966-975
    • Eisenberg-Lerner, A.1    Bialik, S.2    Simon, H.U.3    Kimchi, A.4
  • 11
    • 34247113888 scopus 로고    scopus 로고
    • Two endoplasmic reticulum-associated degradation (ERAD) systems for the novel variant of the mutant dysferlin: ubiquitin/proteasome ERAD(I) and autophagy/lysosome ERAD(II)
    • Fujita E., Kouroku Y., Isoai A., Kumagai H., Misutani A., Matsuda C., Hayashi Y.K., Momoi T. Two endoplasmic reticulum-associated degradation (ERAD) systems for the novel variant of the mutant dysferlin: ubiquitin/proteasome ERAD(I) and autophagy/lysosome ERAD(II). Hum. Mol. Genet. 2007, 16:618-629.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 618-629
    • Fujita, E.1    Kouroku, Y.2    Isoai, A.3    Kumagai, H.4    Misutani, A.5    Matsuda, C.6    Hayashi, Y.K.7    Momoi, T.8
  • 12
    • 79551609332 scopus 로고    scopus 로고
    • BAG3 mediates chaperone-based aggresome-targeting and selective autophagy of misfolded proteins
    • Gamerdinger M., Kaya A.M., Wolfrum U., Clement A.M., Behl C. BAG3 mediates chaperone-based aggresome-targeting and selective autophagy of misfolded proteins. EMBO Rep. 2011, 12:149-156.
    • (2011) EMBO Rep. , vol.12 , pp. 149-156
    • Gamerdinger, M.1    Kaya, A.M.2    Wolfrum, U.3    Clement, A.M.4    Behl, C.5
  • 14
    • 79551678082 scopus 로고    scopus 로고
    • The endoplasmic reticulum-associated Hsp40 DNAJB12 and Hsc70 cooperate to facilitate RMA1 E3-dependent degradation of nascent CFTRDeltaF508
    • Grove D.E., Fan C.Y., Ren H.Y., Cyr D.M. The endoplasmic reticulum-associated Hsp40 DNAJB12 and Hsc70 cooperate to facilitate RMA1 E3-dependent degradation of nascent CFTRDeltaF508. Mol. Biol. Cell 2011, 22:301-314.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 301-314
    • Grove, D.E.1    Fan, C.Y.2    Ren, H.Y.3    Cyr, D.M.4
  • 16
    • 63649161943 scopus 로고    scopus 로고
    • The ubiquitylation machinery of the endoplasmic reticulum
    • Hirsch C., Gauss R., Horn S.C., Neuber O., Sommer T. The ubiquitylation machinery of the endoplasmic reticulum. Nature 2009, 458:453-460.
    • (2009) Nature , vol.458 , pp. 453-460
    • Hirsch, C.1    Gauss, R.2    Horn, S.C.3    Neuber, O.4    Sommer, T.5
  • 17
    • 84857648264 scopus 로고    scopus 로고
    • Mechanisms for quality control of misfolded transmembrane proteins
    • Houck S.A., Cyr D.M. Mechanisms for quality control of misfolded transmembrane proteins. Biochim. Biophys. Acta 2012, 1818:1108-1114.
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 1108-1114
    • Houck, S.A.1    Cyr, D.M.2
  • 18
    • 59249089394 scopus 로고    scopus 로고
    • Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG
    • Itakura E., Kishi C., Inoue K., Mizushima N. Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG. Mol. Biol. Cell 2008, 19:5360-5372.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 5360-5372
    • Itakura, E.1    Kishi, C.2    Inoue, K.3    Mizushima, N.4
  • 19
    • 33646849270 scopus 로고    scopus 로고
    • Regulation of G protein-coupled receptor trafficking by inefficient plasma membrane expression: molecular basis of an evolved strategy
    • Janovick J.A., Knollman P.E., Brothers S.P., Ayala-Yáñez R., Aziz A.S., Conn P.M. Regulation of G protein-coupled receptor trafficking by inefficient plasma membrane expression: molecular basis of an evolved strategy. J.Biol. Chem. 2006, 281:8417-8425.
    • (2006) J.Biol. Chem. , vol.281 , pp. 8417-8425
    • Janovick, J.A.1    Knollman, P.E.2    Brothers, S.P.3    Ayala-Yáñez, R.4    Aziz, A.S.5    Conn, P.M.6
  • 20
    • 51849164641 scopus 로고    scopus 로고
    • Modeling and molecular dynamics simulation of the human gonadotropin-releasing hormone receptor in a lipid bilayer
    • Jardón-Valadez E., Ulloa-Aguirre A., Piñeiro A. Modeling and molecular dynamics simulation of the human gonadotropin-releasing hormone receptor in a lipid bilayer. J.Phys. Chem. B 2008, 112:10704-10713.
    • (2008) J.Phys. Chem. B , vol.112 , pp. 10704-10713
    • Jardón-Valadez, E.1    Ulloa-Aguirre, A.2    Piñeiro, A.3
  • 22
    • 33947660889 scopus 로고    scopus 로고
    • Effect of rapamycin on the fate of P23H opsin associated with retinitis pigmentosa (an American Ophthalmological Society thesis)
    • Kaushal S. Effect of rapamycin on the fate of P23H opsin associated with retinitis pigmentosa (an American Ophthalmological Society thesis). Trans. Am. Ophthalmol. Soc. 2006, 104:517-529.
    • (2006) Trans. Am. Ophthalmol. Soc. , vol.104 , pp. 517-529
    • Kaushal, S.1
  • 23
    • 84872586081 scopus 로고    scopus 로고
    • Differential regulation of distinct Vps34 complexes by AMPK in nutrient stress and autophagy
    • Kim J., Kim Y.C., Fang C., Russell R.C., Kim J.H., Fan W., Liu R., Zhong Q., Guan K.L. Differential regulation of distinct Vps34 complexes by AMPK in nutrient stress and autophagy. Cell 2013, 152:290-303.
    • (2013) Cell , vol.152 , pp. 290-303
    • Kim, J.1    Kim, Y.C.2    Fang, C.3    Russell, R.C.4    Kim, J.H.5    Fan, W.6    Liu, R.7    Zhong, Q.8    Guan, K.L.9
  • 26
    • 84885662059 scopus 로고    scopus 로고
    • Temporal analysis of recruitment of mammalian ATG proteins to the autophagosome formation site
    • Koyama-Honda I., Itakura E., Fujiwara T.K., Mizushima N. Temporal analysis of recruitment of mammalian ATG proteins to the autophagosome formation site. Autophagy 2013, 9:9.
    • (2013) Autophagy , vol.9 , pp. 9
    • Koyama-Honda, I.1    Itakura, E.2    Fujiwara, T.K.3    Mizushima, N.4
  • 27
    • 0038147442 scopus 로고    scopus 로고
    • Endoplasmic reticulum retention, degradation, and aggregation of olfactory G-protein coupled receptors
    • Lu M., Echeverri F., Moyer B.D. Endoplasmic reticulum retention, degradation, and aggregation of olfactory G-protein coupled receptors. Traffic 2003, 4:416-433.
    • (2003) Traffic , vol.4 , pp. 416-433
    • Lu, M.1    Echeverri, F.2    Moyer, B.D.3
  • 30
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • Meacham G.C., Patterson C., Zhang W., Younger J.M., Cyr D.M. The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat. Cell Biol. 2001, 3:100-105.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 100-105
    • Meacham, G.C.1    Patterson, C.2    Zhang, W.3    Younger, J.M.4    Cyr, D.M.5
  • 34
    • 0033671965 scopus 로고    scopus 로고
    • Retention of mutant alpha(1)-antitrypsin Z in endoplasmic reticulum is associated with an autophagic response
    • Teckman J.H., Perlmutter D.H. Retention of mutant alpha(1)-antitrypsin Z in endoplasmic reticulum is associated with an autophagic response. Am. J. Physiol. Gastrointest. Liver Physiol. 2000, 279:G961-G974.
    • (2000) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.279
    • Teckman, J.H.1    Perlmutter, D.H.2
  • 35
    • 43149099696 scopus 로고    scopus 로고
    • Inhibition of p97-dependent protein degradation by Eeyarestatin I
    • Wang Q., Li L., Ye Y. Inhibition of p97-dependent protein degradation by Eeyarestatin I. J.Biol. Chem. 2008, 283:7445-7454.
    • (2008) J.Biol. Chem. , vol.283 , pp. 7445-7454
    • Wang, Q.1    Li, L.2    Ye, Y.3
  • 38
    • 33746675669 scopus 로고    scopus 로고
    • Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator
    • Younger J.M., Chen L., Ren H.Y., Rosser M.F., Turnbull E.L., Fan C.Y., Patterson C., Cyr D.M. Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator. Cell 2006, 126:571-582.
    • (2006) Cell , vol.126 , pp. 571-582
    • Younger, J.M.1    Chen, L.2    Ren, H.Y.3    Rosser, M.F.4    Turnbull, E.L.5    Fan, C.Y.6    Patterson, C.7    Cyr, D.M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.