메뉴 건너뛰기




Volumn 458, Issue 2, 2015, Pages 424-428

Identification of ERAD components essential for dislocation of the null Hong Kong variant of α-1-antitrypsin (NHK)

Author keywords

Dislocation retrotranslocation; drGFP; ERAD; Hrd1; p97 VCP; Sel1L

Indexed keywords

ALPHA 1 ANTITRYPSIN; BINDING PROTEIN; GLUCOSE REGULATED PROTEIN 94; GREEN FLUORESCENT PROTEIN; KARYOPHERIN BETA; LACTACYSTIN; MEMBRANE PROTEIN; PROTEIN; PROTEIN DERLIN1; PROTEIN DERLIN2; PROTEIN HRD1; PROTEIN P97; PROTEIN SEL1L; PROTEIN UBAC2; PROTEIN UBXD8; SMALL INTERFERING RNA; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; SERPINA1 PROTEIN, HUMAN;

EID: 84923223113     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2015.01.133     Document Type: Article
Times cited : (21)

References (23)
  • 2
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: Endoplasmic reticulum-associated degradation
    • S.S. Vembar, and J.L. Brodsky One step at a time: endoplasmic reticulum-associated degradation Nat. Rev. Mol. Cell. Biol. 9 2008 944 957
    • (2008) Nat. Rev. Mol. Cell. Biol. , vol.9 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 3
    • 33845917801 scopus 로고    scopus 로고
    • The role of a novel p97/valosin-containing protein-interacting motif of gp78 in endoplasmic reticulum-associated degradation
    • P. Ballar, Y. Shen, H. Yang, and S. Fang The role of a novel p97/valosin-containing protein-interacting motif of gp78 in endoplasmic reticulum-associated degradation J. Biol. Chem. 281 2006 35359 35368
    • (2006) J. Biol. Chem. , vol.281 , pp. 35359-35368
    • Ballar, P.1    Shen, Y.2    Yang, H.3    Fang, S.4
  • 4
    • 0036270698 scopus 로고    scopus 로고
    • Retro-translocation of proteins from the endoplasmic reticulum into the cytosol
    • B. Tsai, Y. Ye, and T.A. Rapoport Retro-translocation of proteins from the endoplasmic reticulum into the cytosol Nat. Rev. Mol. Cell. Biol. 3 2002 246 255
    • (2002) Nat. Rev. Mol. Cell. Biol. , vol.3 , pp. 246-255
    • Tsai, B.1    Ye, Y.2    Rapoport, T.A.3
  • 5
    • 36248988054 scopus 로고    scopus 로고
    • Ubiquitin ligases, critical mediators of endoplasmic reticulum-associated degradation
    • Z. Kostova, Y.C. Tsai, and A.M. Weissman Ubiquitin ligases, critical mediators of endoplasmic reticulum-associated degradation Semin. Cell. Dev. Biol. 18 2007 770 779
    • (2007) Semin. Cell. Dev. Biol. , vol.18 , pp. 770-779
    • Kostova, Z.1    Tsai, Y.C.2    Weissman, A.M.3
  • 6
    • 80053176398 scopus 로고    scopus 로고
    • Importin beta interacts with the endoplasmic reticulum-associated degradation machinery and promotes ubiquitination and degradation of mutant alpha1-antitrypsin
    • Y. Zhong, Y. Wang, H. Yang, P. Ballar, J.G. Lee, Y. Ye, M.J. Monteiro, and S. Fang Importin beta interacts with the endoplasmic reticulum-associated degradation machinery and promotes ubiquitination and degradation of mutant alpha1-antitrypsin J. Biol. Chem. 286 2011 33921 33930
    • (2011) J. Biol. Chem. , vol.286 , pp. 33921-33930
    • Zhong, Y.1    Wang, Y.2    Yang, H.3    Ballar, P.4    Lee, J.G.5    Ye, Y.6    Monteiro, M.J.7    Fang, S.8
  • 7
    • 40249088336 scopus 로고    scopus 로고
    • OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD
    • J.C. Christianson, T.A. Shaler, R.E. Tyler, and R.R. Kopito OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD Nat. Cell. Biol. 10 2008 272 282
    • (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
  • 10
    • 84884308471 scopus 로고    scopus 로고
    • Previously unknown role for the ubiquitin ligase Ubr1 in endoplasmic reticulum-associated protein degradation
    • A. Stolz, S. Besser, H. Hottmann, and D.H. Wolf Previously unknown role for the ubiquitin ligase Ubr1 in endoplasmic reticulum-associated protein degradation Proc. Natl. Acad. Sci. U. S. A. 110 2013 15271 15276
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 15271-15276
    • Stolz, A.1    Besser, S.2    Hottmann, H.3    Wolf, D.H.4
  • 11
    • 84886701135 scopus 로고    scopus 로고
    • RNF185 is a novel E3 ligase of endoplasmic reticulum-associated degradation (ERAD) that targets cystic fibrosis transmembrane conductance regulator (CFTR)
    • E. El Khouri, G. Le Pavec, M.B. Toledano, and A. Delaunay-Moisan RNF185 is a novel E3 ligase of endoplasmic reticulum-associated degradation (ERAD) that targets cystic fibrosis transmembrane conductance regulator (CFTR) J. Biol. Chem. 288 2013 31177 31191
    • (2013) J. Biol. Chem. , vol.288 , pp. 31177-31191
    • El Khouri, E.1    Le Pavec, G.2    Toledano, M.B.3    Delaunay-Moisan, A.4
  • 13
    • 84908072286 scopus 로고    scopus 로고
    • Key steps in ERAD of luminal ER proteins reconstituted with purified components
    • A. Stein, A. Ruggiano, P. Carvalho, and T.A. Rapoport Key steps in ERAD of luminal ER proteins reconstituted with purified components Cell 158 2014 1375 1388
    • (2014) Cell , vol.158 , pp. 1375-1388
    • Stein, A.1    Ruggiano, A.2    Carvalho, P.3    Rapoport, T.A.4
  • 14
    • 84864976096 scopus 로고    scopus 로고
    • Live cell imaging of protein dislocation from the endoplasmic reticulum
    • Y. Zhong, and S. Fang Live cell imaging of protein dislocation from the endoplasmic reticulum J. Biol. Chem. 287 2012 28057 28066
    • (2012) J. Biol. Chem. , vol.287 , pp. 28057-28066
    • Zhong, Y.1    Fang, S.2
  • 15
    • 36348954034 scopus 로고    scopus 로고
    • Identification of SVIP as an endogenous inhibitor of endoplasmic reticulum-associated degradation
    • P. Ballar, Y. Zhong, M. Nagahama, M. Tagaya, Y. Shen, and S. Fang Identification of SVIP as an endogenous inhibitor of endoplasmic reticulum-associated degradation J. Biol. Chem. 282 2007 33908 33914
    • (2007) J. Biol. Chem. , vol.282 , pp. 33908-33914
    • Ballar, P.1    Zhong, Y.2    Nagahama, M.3    Tagaya, M.4    Shen, Y.5    Fang, S.6
  • 16
    • 33846696670 scopus 로고    scopus 로고
    • Ubiquitin ligase Hrd1 enhances the degradation and suppresses the toxicity of polyglutamine-expanded huntingtin
    • H. Yang, X. Zhong, P. Ballar, S. Luo, Y. Shen, D.C. Rubinsztein, M.J. Monteiro, and S. Fang Ubiquitin ligase Hrd1 enhances the degradation and suppresses the toxicity of polyglutamine-expanded huntingtin Exp. Cell. Res. 313 2007 538 550
    • (2007) Exp. Cell. Res. , vol.313 , pp. 538-550
    • Yang, H.1    Zhong, X.2    Ballar, P.3    Luo, S.4    Shen, Y.5    Rubinsztein, D.C.6    Monteiro, M.J.7    Fang, S.8
  • 17
    • 31044437051 scopus 로고    scopus 로고
    • The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding site
    • B. Chen, J. Mariano, Y.C. Tsai, A.H. Chan, M. Cohen, and A.M. Weissman The activity of a human endoplasmic reticulum-associated degradation E3, gp78, requires its Cue domain, RING finger, and an E2-binding site Proc. Natl. Acad. Sci. U. S. A. 103 2006 341 346
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 341-346
    • Chen, B.1    Mariano, J.2    Tsai, Y.C.3    Chan, A.H.4    Cohen, M.5    Weissman, A.M.6
  • 18
    • 26244431960 scopus 로고    scopus 로고
    • Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane
    • B.N. Lilley, and H.L. Ploegh Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane Proc. Natl. Acad. Sci. U. S. A. 102 2005 14296 14301
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 14296-14301
    • Lilley, B.N.1    Ploegh, H.L.2
  • 19
    • 13244296604 scopus 로고    scopus 로고
    • Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein
    • S. Cabantous, T.C. Terwilliger, and G.S. Waldo Protein tagging and detection with engineered self-assembling fragments of green fluorescent protein Nat. Biotechnol. 23 2005 102 107
    • (2005) Nat. Biotechnol. , vol.23 , pp. 102-107
    • Cabantous, S.1    Terwilliger, T.C.2    Waldo, G.S.3
  • 20
    • 37649025515 scopus 로고    scopus 로고
    • Dissecting the ER-associated degradation of a misfolded polytopic membrane protein
    • K. Nakatsukasa, G. Huyer, S. Michaelis, and J.L. Brodsky Dissecting the ER-associated degradation of a misfolded polytopic membrane protein Cell 132 2008 101 112
    • (2008) Cell , vol.132 , pp. 101-112
    • Nakatsukasa, K.1    Huyer, G.2    Michaelis, S.3    Brodsky, J.L.4
  • 21
    • 67649371174 scopus 로고    scopus 로고
    • In vitro analysis of Hrd1p-mediated retrotranslocation of its multispanning membrane substrate 3-hydroxy-3-methylglutaryl (HMG)-CoA reductase
    • R.M. Garza, B.K. Sato, and R.Y. Hampton In vitro analysis of Hrd1p-mediated retrotranslocation of its multispanning membrane substrate 3-hydroxy-3-methylglutaryl (HMG)-CoA reductase J. Biol. Chem. 284 2009 14710 14722
    • (2009) J. Biol. Chem. , vol.284 , pp. 14710-14722
    • Garza, R.M.1    Sato, B.K.2    Hampton, R.Y.3
  • 22
    • 80054801259 scopus 로고    scopus 로고
    • Dual role of ancient ubiquitous protein 1 (AUP1) in lipid droplet accumulation and endoplasmic reticulum (ER) protein quality control
    • E.J. Klemm, E. Spooner, and H.L. Ploegh Dual role of ancient ubiquitous protein 1 (AUP1) in lipid droplet accumulation and endoplasmic reticulum (ER) protein quality control J. Biol. Chem. 286 2011 37602 37614
    • (2011) J. Biol. Chem. , vol.286 , pp. 37602-37614
    • Klemm, E.J.1    Spooner, E.2    Ploegh, H.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.