메뉴 건너뛰기




Volumn 6, Issue 12, 2011, Pages

BAT3 guides misfolded glycoproteins out of the endoplasmic reticulum

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; CHAPERONE; DERLIN2 PROTEIN; GLYCOPROTEIN; PROTEASOME; PROTEIN BAT3; UNCLASSIFIED DRUG; BAG6 PROTEIN, HUMAN; DERL2 PROTEIN, HUMAN; LYMPHOCYTE ANTIGEN RECEPTOR; MEMBRANE PROTEIN;

EID: 82955207151     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0028542     Document Type: Article
Times cited : (41)

References (30)
  • 2
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron D, 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
  • 3
    • 36749001066 scopus 로고    scopus 로고
    • Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes
    • Rapoport TA, (2007) Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes. Nature 450: 663-669.
    • (2007) Nature , vol.450 , pp. 663-669
    • Rapoport, T.A.1
  • 4
    • 0029915568 scopus 로고    scopus 로고
    • The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol
    • Wiertz EJ, Jones TR, Sun L, Bogyo M, Geuze HJ, et al. (1996) The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol. Cell 84: 769-779.
    • (1996) Cell , vol.84 , pp. 769-779
    • Wiertz, E.J.1    Jones, T.R.2    Sun, L.3    Bogyo, M.4    Geuze, H.J.5
  • 5
    • 0029828991 scopus 로고    scopus 로고
    • Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
    • Wiertz EJ, Tortorella D, Bogyo M, Yu J, Mothes W, et al. (1996) Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 384: 432-438.
    • (1996) Nature , vol.384 , pp. 432-438
    • Wiertz, E.J.1    Tortorella, D.2    Bogyo, M.3    Yu, J.4    Mothes, W.5
  • 6
    • 0035818999 scopus 로고    scopus 로고
    • The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol
    • Ye Y, Meyer HH, Rapoport TA, (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
  • 7
    • 0036173013 scopus 로고    scopus 로고
    • Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48
    • Jarosch E, Taxis C, Volkwein C, Bordallo J, Finley D, et al. (2002) Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48. Nat Cell Biol 4: 134-139.
    • (2002) Nat Cell Biol , vol.4 , pp. 134-139
    • Jarosch, E.1    Taxis, C.2    Volkwein, C.3    Bordallo, J.4    Finley, D.5
  • 8
    • 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, 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
  • 9
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley D, (2009) Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu Rev Biochem 78: 477-513.
    • (2009) Annu Rev Biochem , vol.78 , pp. 477-513
    • Finley, D.1
  • 10
    • 0035694696 scopus 로고    scopus 로고
    • Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome
    • Navon A, Goldberg AL, (2001) Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome. Mol Cell 8: 1339-1349.
    • (2001) Mol Cell , vol.8 , pp. 1339-1349
    • Navon, A.1    Goldberg, A.L.2
  • 11
    • 33646535590 scopus 로고    scopus 로고
    • Central pore residues mediate the p97/VCP activity required for ERAD
    • DeLaBarre B, Christianson JC, Kopito RR, Brunger AT, (2006) Central pore residues mediate the p97/VCP activity required for ERAD. Mol Cell 22: 451-462.
    • (2006) Mol Cell , vol.22 , pp. 451-462
    • DeLaBarre, B.1    Christianson, J.C.2    Kopito, R.R.3    Brunger, A.T.4
  • 13
    • 79959347089 scopus 로고    scopus 로고
    • A Ubiquitin Ligase-Associated Chaperone Holdase Maintains Polypeptides in Soluble States for Proteasome Degradation
    • Wang Q, Liu Y, Soetandyo N, Baek K, Hegde R, et al. (2011) A Ubiquitin Ligase-Associated Chaperone Holdase Maintains Polypeptides in Soluble States for Proteasome Degradation. Mol Cell 42 (6): 758-70.
    • (2011) Mol Cell , vol.42 , Issue.6 , pp. 758-770
    • Wang, Q.1    Liu, Y.2    Soetandyo, N.3    Baek, K.4    Hegde, R.5
  • 14
    • 26244431960 scopus 로고    scopus 로고
    • Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane
    • Lilley BN, Ploegh HL, (2005) Multiprotein complexes that link dislocation, ubiquitination, and extraction of misfolded proteins from the endoplasmic reticulum membrane. Proc Natl Acad Sci U S A 102: 14296-14301.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 14296-14301
    • Lilley, B.N.1    Ploegh, H.L.2
  • 15
    • 31944450850 scopus 로고    scopus 로고
    • Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation
    • Oda Y, Okada T, Yoshida H, Kaufman RJ, Nagata K, et al. (2006) Derlin-2 and Derlin-3 are regulated by the mammalian unfolded protein response and are required for ER-associated degradation. J Cell Biol 172: 383-393.
    • (2006) J Cell Biol , vol.172 , pp. 383-393
    • Oda, Y.1    Okada, T.2    Yoshida, H.3    Kaufman, R.J.4    Nagata, K.5
  • 16
    • 0035850749 scopus 로고    scopus 로고
    • Human Scythe contains a functional nuclear localization sequence and remains in the nucleus during staurosporine-induced apoptosis
    • Manchen ST, Hubberstey AV, (2001) Human Scythe contains a functional nuclear localization sequence and remains in the nucleus during staurosporine-induced apoptosis. Biochem Biophys Res Commun 287: 1075-1082.
    • (2001) Biochem Biophys Res Commun , vol.287 , pp. 1075-1082
    • Manchen, S.T.1    Hubberstey, A.V.2
  • 17
    • 77956183398 scopus 로고    scopus 로고
    • A ribosome-associating factor chaperones tail-anchored membrane proteins
    • Mariappan M, Li X, Stefanovic S, Sharma A, Mateja A, et al. (2010) A ribosome-associating factor chaperones tail-anchored membrane proteins. Nature 466: 1120-1124.
    • (2010) Nature , vol.466 , pp. 1120-1124
    • Mariappan, M.1    Li, X.2    Stefanovic, S.3    Sharma, A.4    Mateja, A.5
  • 18
    • 3042616595 scopus 로고    scopus 로고
    • A membrane protein required for dislocation of misfolded proteins from the ER
    • Lilley BN, Ploegh HL, (2004) A membrane protein required for dislocation of misfolded proteins from the ER. Nature 429: 834-840.
    • (2004) Nature , vol.429 , pp. 834-840
    • Lilley, B.N.1    Ploegh, H.L.2
  • 19
    • 3042677637 scopus 로고    scopus 로고
    • A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol
    • Ye Y, Shibata Y, Yun C, Ron D, Rapoport TA, (2004) A membrane protein complex mediates retro-translocation 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
  • 20
    • 70349778618 scopus 로고    scopus 로고
    • The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER
    • Ernst R, Mueller B, Ploegh HL, Schlieker C, (2009) The otubain YOD1 is a deubiquitinating enzyme that associates with p97 to facilitate protein dislocation from the ER. Mol Cell 36: 28-38.
    • (2009) Mol Cell , vol.36 , pp. 28-38
    • Ernst, R.1    Mueller, B.2    Ploegh, H.L.3    Schlieker, C.4
  • 21
    • 0030744415 scopus 로고    scopus 로고
    • The alpha chain of the T cell antigen receptor is degraded in the cytosol
    • Huppa JB, Ploegh HL, (1997) The alpha chain of the T cell antigen receptor is degraded in the cytosol. Immunity 7: 113-122.
    • (1997) Immunity , vol.7 , pp. 113-122
    • Huppa, J.B.1    Ploegh, H.L.2
  • 22
    • 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 HH, Rapoport TA, (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
  • 23
    • 78649357985 scopus 로고    scopus 로고
    • Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms
    • Buchberger A, Bukau B, Sommer T, (2010) Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms. Mol Cell 40: 238-252.
    • (2010) Mol Cell , vol.40 , pp. 238-252
    • Buchberger, A.1    Bukau, B.2    Sommer, T.3
  • 24
    • 33746675669 scopus 로고    scopus 로고
    • Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator
    • Younger JM, Chen L, Ren HY, Rosser MF, Turnbull EL, et al. (2006) Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator. Cell 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
  • 25
    • 77955878748 scopus 로고    scopus 로고
    • BAG-6 is essential for selective elimination of defective proteasomal substrates
    • Minami R, Hayakawa A, Kagawa H, Yanagi Y, Yokosawa H, et al. (2010) BAG-6 is essential for selective elimination of defective proteasomal substrates. J Cell Biol 190: 637-650.
    • (2010) J Cell Biol , vol.190 , pp. 637-650
    • Minami, R.1    Hayakawa, A.2    Kagawa, H.3    Yanagi, Y.4    Yokosawa, H.5
  • 26
    • 79960637590 scopus 로고    scopus 로고
    • Protein targeting and degradation are coupled for elimination of mislocalized proteins
    • Hessa T, Sharma A, Mariappan M, Eshleman HD, Gutierrez E, et al. (2011) Protein targeting and degradation are coupled for elimination of mislocalized proteins. Nature.
    • (2011) Nature
    • Hessa, T.1    Sharma, A.2    Mariappan, M.3    Eshleman, H.D.4    Gutierrez, E.5
  • 27
    • 77954352789 scopus 로고    scopus 로고
    • Bat3 promotes the membrane integration of tail-anchored proteins
    • Leznicki P, Clancy A, Schwappach B, High S, (2010) Bat3 promotes the membrane integration of tail-anchored proteins. J Cell Sci 123: 2170-2178.
    • (2010) J Cell Sci , vol.123 , pp. 2170-2178
    • Leznicki, P.1    Clancy, A.2    Schwappach, B.3    High, S.4
  • 28
    • 56749176947 scopus 로고    scopus 로고
    • One step at a time: endoplasmic reticulum-associated degradation
    • Vembar SS, Brodsky JL, (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
  • 29
    • 0028918657 scopus 로고
    • A transient three-plasmid expression system for the production of high titer retroviral vectors
    • Soneoka Y, Cannon PM, Ramsdale EE, Griffiths JC, Romano G, et al. (1995) A transient three-plasmid expression system for the production of high titer retroviral vectors. Nucleic Acids Res 23: 628-633.
    • (1995) Nucleic Acids Res , vol.23 , pp. 628-633
    • Soneoka, Y.1    Cannon, P.M.2    Ramsdale, E.E.3    Griffiths, J.C.4    Romano, G.5
  • 30
    • 77954234135 scopus 로고    scopus 로고
    • The transmembrane segment of a tail-anchored protein determines its degradative fate through dislocation from the endoplasmic reticulum
    • Claessen JH, Mueller B, Spooner E, Pivorunas VL, Ploegh HL, (2010) The transmembrane segment of a tail-anchored protein determines its degradative fate through dislocation from the endoplasmic reticulum. J Biol Chem 285: 20732-20739.
    • (2010) J Biol Chem , vol.285 , pp. 20732-20739
    • Claessen, J.H.1    Mueller, B.2    Spooner, E.3    Pivorunas, V.L.4    Ploegh, H.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.