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Volumn 26, Issue 21, 2015, Pages 3719-3727

Proteasomal degradation of preemptive quality control (pQC) substrates is mediated by an AIRAPL-p97 complex

Author keywords

[No Author keywords available]

Indexed keywords

C PEPTIDE; CHAPERONE; GLYCOSYLATED PROTEIN; INSULIN; POLYPEPTIDE; PREPROINSULIN; PROTEIN P97; SIGNAL PEPTIDE; TRANSLOCON; VASCULAR CELL ADHESION MOLECULE 1; CARRIER PROTEIN; CELL CYCLE PROTEIN; KARYOPHERIN BETA; KPNB1 PROTEIN, HUMAN; NUCLEAR PROTEIN; PROTEASOME; UBIQUITIN; ZFAND2B PROTEIN, HUMAN;

EID: 84945916821     PISSN: 10591524     EISSN: 19394586     Source Type: Journal    
DOI: 10.1091/mbc.E15-02-0085     Document Type: Article
Times cited : (26)

References (46)
  • 1
    • 52649138958 scopus 로고    scopus 로고
    • UBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1alpha turnover
    • Alexandru G, Graumann J, Smith GT, Kolawa NJ, Fang R, Deshaies RJ (2008). UBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1alpha turnover. Cell 134, 804-816.
    • (2008) Cell , vol.134 , pp. 804-816
    • Alexandru, G.1    Graumann, J.2    Smith, G.T.3    Kolawa, N.J.4    Fang, R.5    Deshaies, R.J.6
  • 2
    • 0025013749 scopus 로고
    • Mutation of the signal peptide-encoding region of the preproparathyroid hormone gene in familial isolated hypoparathyroidism
    • Arnold A, Horst SA, Gardella TJ, Baba H, Levine MA, Kronenberg HM (1990). Mutation of the signal peptide-encoding region of the preproparathyroid hormone gene in familial isolated hypoparathyroidism. J Clin Invest 86, 1084-1087.
    • (1990) J Clin Invest , vol.86 , pp. 1084-1087
    • Arnold, A.1    Horst, S.A.2    Gardella, T.J.3    Baba, H.4    Levine, M.A.5    Kronenberg, H.M.6
  • 3
    • 84878466615 scopus 로고    scopus 로고
    • All roads lead to Rome (but some may be harder to travel): SRP-independent translocation into the endoplasmic reticulum
    • Ast T, Schuldiner M (2013). All roads lead to Rome (but some may be harder to travel): SRP-independent translocation into the endoplasmic reticulum. Crit Rev Biochem Mol Biol 48, 273-288.
    • (2013) Crit Rev Biochem Mol Biol , vol.48 , pp. 273-288
    • Ast, T.1    Schuldiner, M.2
  • 7
    • 84898729879 scopus 로고    scopus 로고
    • Cleaning up in the endoplasmic reticulum: Ubiquitin in charge
    • Christianson JC, Ye Y (2014). Cleaning up in the endoplasmic reticulum: ubiquitin in charge. Nat Struct Mol Biol 21, 325-335.
    • (2014) Nat Struct Mol Biol , vol.21 , pp. 325-335
    • Christianson, J.C.1    Ye, Y.2
  • 8
    • 84855195340 scopus 로고    scopus 로고
    • Cdc48/p97, a key actor in the interplay between autophagy and ubiquitin/proteasome catabolic pathways
    • Dargemont C, Ossareh-Nazari B (2012). Cdc48/p97, a key actor in the interplay between autophagy and ubiquitin/proteasome catabolic pathways. Biochim Biophys Acta 1823, 138-144.
    • (2012) Biochim Biophys Acta , vol.1823 , pp. 138-144
    • Dargemont, C.1    Ossareh-Nazari, B.2
  • 9
    • 0023567026 scopus 로고
    • A yeast mutant defective at an early stage in import of secretory protein precursors into the endoplasmic reticulum
    • Deshaies RJ, Schekman R (1987). A yeast mutant defective at an early stage in import of secretory protein precursors into the endoplasmic reticulum. J Cell Biol 105, 633-645.
    • (1987) J Cell Biol , vol.105 , pp. 633-645
    • Deshaies, R.J.1    Schekman, R.2
  • 10
    • 0012295328 scopus 로고
    • Purification of microsomal signal peptidase as a complex
    • Evans EA, Gilmore R, Blobel G (1986). Purification of microsomal signal peptidase as a complex. Proc Natl Acad Sci USA 83, 581-585.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 581-585
    • Evans, E.A.1    Gilmore, R.2    Blobel, G.3
  • 11
    • 0021134628 scopus 로고
    • Mammalian signal peptidase: Partial purification and general characterization of the signal peptidase from microsomal membranes of porcine pancreas
    • Fujimoto Y, Watanabe Y, Uchida M, Ozaki M (1984). Mammalian signal peptidase: partial purification and general characterization of the signal peptidase from microsomal membranes of porcine pancreas. J Biochem 96, 1125-1131.
    • (1984) J Biochem , vol.96 , pp. 1125-1131
    • Fujimoto, Y.1    Watanabe, Y.2    Uchida, M.3    Ozaki, M.4
  • 12
    • 22444450987 scopus 로고    scopus 로고
    • A substrate-specific inhibitor of protein translocation into the endoplasmic reticulum
    • Garrison JL, Kunkel EJ, Hegde RS, Taunton J (2005). A substrate-specific inhibitor of protein translocation into the endoplasmic reticulum. Nature 436, 285-289.
    • (2005) Nature , vol.436 , pp. 285-289
    • Garrison, J.L.1    Kunkel, E.J.2    Hegde, R.S.3    Taunton, J.4
  • 14
    • 69249124617 scopus 로고    scopus 로고
    • Mechanisms of emphysema in alpha1-antitrypsin deficiency: Molecular and cellular insights
    • Gooptu B, Ekeowa UI, Lomas DA (2009). Mechanisms of emphysema in alpha1-antitrypsin deficiency: molecular and cellular insights. Eur Respir J 34, 475-488.
    • (2009) Eur Respir J , vol.34 , pp. 475-488
    • Gooptu, B.1    Ekeowa, U.I.2    Lomas, D.A.3
  • 15
    • 0026466143 scopus 로고
    • A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation
    • Gorlich D, Prehn S, Hartmann E, Kalies KU, Rapoport TA (1992). A mammalian homolog of SEC61p and SECYp is associated with ribosomes and nascent polypeptides during translocation. Cell 71, 489-503.
    • (1992) Cell , vol.71 , pp. 489-503
    • Gorlich, D.1    Prehn, S.2    Hartmann, E.3    Kalies, K.U.4    Rapoport, T.A.5
  • 16
    • 0027424601 scopus 로고
    • Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane
    • Gorlich D, Rapoport TA (1993). Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane. Cell 75, 615-630.
    • (1993) Cell , vol.75 , pp. 615-630
    • Gorlich, D.1    Rapoport, T.A.2
  • 18
    • 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, Hegde RS (2011). Protein targeting and degradation are coupled for elimination of mislocalized proteins. Nature 475, 394-397.
    • (2011) Nature , vol.475 , pp. 394-397
    • Hessa, T.1    Sharma, A.2    Mariappan, M.3    Eshleman, H.D.4    Gutierrez, E.5    Hegde, R.S.6
  • 20
    • 80052212289 scopus 로고    scopus 로고
    • Stalled proteasomes are directly relieved by P97 recruitment
    • Isakov E, Stanhill A (2011). Stalled proteasomes are directly relieved by P97 recruitment. J Biol Chem 286, 30274-30283.
    • (2011) J Biol Chem , vol.286 , pp. 30274-30283
    • Isakov, E.1    Stanhill, A.2
  • 22
    • 22744456680 scopus 로고    scopus 로고
    • The protein translocation channel binds proteasomes to the endoplasmic reticulum membrane
    • Kalies KU, Allan S, Sergeyenko T, Kroger H, Romisch K (2005). The protein translocation channel binds proteasomes to the endoplasmic reticulum membrane. EMBO J 24, 2284-2293.
    • (2005) EMBO J , vol.24 , pp. 2284-2293
    • Kalies, K.U.1    Allan, S.2    Sergeyenko, T.3    Kroger, H.4    Romisch, K.5
  • 23
    • 0027953913 scopus 로고
    • Binding of ribosomes to the rough endoplasmic reticulum mediated by the Sec61p-complex
    • Kalies KU, Gorlich D, Rapoport TA (1994). Binding of ribosomes to the rough endoplasmic reticulum mediated by the Sec61p-complex. J Cell Biol 126, 925-934.
    • (1994) J Cell Biol , vol.126 , pp. 925-934
    • Kalies, K.U.1    Gorlich, D.2    Rapoport, T.A.3
  • 24
    • 65849109465 scopus 로고    scopus 로고
    • Assembly pathway of the mammalian proteasome base subcomplex is mediated by multiple specific chaperones
    • Kaneko T, Hamazaki J, Iemura S, Sasaki K, Furuyama K, Natsume T, Tanaka K, Murata S (2009). Assembly pathway of the mammalian proteasome base subcomplex is mediated by multiple specific chaperones. Cell 137, 914-925.
    • (2009) Cell , vol.137 , pp. 914-925
    • Kaneko, T.1    Hamazaki, J.2    Iemura, S.3    Sasaki, K.4    Furuyama, K.5    Natsume, T.6    Tanaka, K.7    Murata, S.8
  • 25
    • 33751333201 scopus 로고    scopus 로고
    • Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway
    • Kang SW, Rane NS, Kim SJ, Garrison JL, Taunton J, Hegde RS (2006). Substrate-specific translocational attenuation during ER stress defines a pre-emptive quality control pathway. Cell 127, 999-1013.
    • (2006) Cell , vol.127 , pp. 999-1013
    • Kang, S.W.1    Rane, N.S.2    Kim, S.J.3    Garrison, J.L.4    Taunton, J.5    Hegde, R.S.6
  • 26
    • 84874976264 scopus 로고    scopus 로고
    • Bag6/Bat3/Scythe: A novel chaperone activity with diverse regulatory functions in protein biogenesis and degradation
    • Lee JG, Ye Y (2013). Bag6/Bat3/Scythe: a novel chaperone activity with diverse regulatory functions in protein biogenesis and degradation. BioEssays 35, 377-385.
    • (2013) BioEssays , vol.35 , pp. 377-385
    • Lee, J.G.1    Ye, Y.2
  • 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
  • 29
    • 77950348445 scopus 로고    scopus 로고
    • Insulin gene mutations resulting in early-onset diabetes: Marked differences in clinical presentation, metabolic status, and pathogenic effect through endoplasmic reticulum retention
    • Meur G, Simon A, Harun N, Virally M, Dechaume A, Bonnefond A, Fetita S, Tarasov AI, Guillausseau PJ, Boesgaard TW, et al. (2010). Insulin gene mutations resulting in early-onset diabetes: marked differences in clinical presentation, metabolic status, and pathogenic effect through endoplasmic reticulum retention. Diabetes 59, 653-661.
    • (2010) Diabetes , vol.59 , pp. 653-661
    • Meur, G.1    Simon, A.2    Harun, N.3    Virally, M.4    Dechaume, A.5    Bonnefond, A.6    Fetita, S.7    Tarasov, A.I.8    Guillausseau, P.J.9    Boesgaard, T.W.10
  • 30
    • 0029952547 scopus 로고    scopus 로고
    • Signal sequences specify the targeting route to the endoplasmic reticulum membrane
    • Ng DT, Brown JD, Walter P (1996). Signal sequences specify the targeting route to the endoplasmic reticulum membrane. J Cell Biol 134, 269-278.
    • (1996) J Cell Biol , vol.134 , pp. 269-278
    • Ng, D.T.1    Brown, J.D.2    Walter, P.3
  • 31
    • 84861361690 scopus 로고    scopus 로고
    • Mechanisms of Sec61/SecY-mediated protein translocation across membranes
    • Park E, Rapoport TA (2012). Mechanisms of Sec61/SecY-mediated protein translocation across membranes. Annu Rev Biophys 41, 21-40.
    • (2012) Annu Rev Biophys , vol.41 , pp. 21-40
    • Park, E.1    Rapoport, T.A.2
  • 32
    • 0034597099 scopus 로고    scopus 로고
    • Spontaneous release of cytosolic proteins from posttranslational substrates before their transport into the endoplasmic reticulum
    • Plath K, Rapoport TA (2000). Spontaneous release of cytosolic proteins from posttranslational substrates before their transport into the endoplasmic reticulum. J Cell Biol 151, 167-178.
    • (2000) J Cell Biol , vol.151 , pp. 167-178
    • Plath, K.1    Rapoport, T.A.2
  • 33
    • 51449098355 scopus 로고    scopus 로고
    • Reduced translocation of nascent prion protein during ER stress contributes to neurodegeneration
    • Rane NS, Kang SW, Chakrabarti O, Feigenbaum L, Hegde RS (2008). Reduced translocation of nascent prion protein during ER stress contributes to neurodegeneration. Dev Cell 15, 359-370.
    • (2008) Dev Cell , vol.15 , pp. 359-370
    • Rane, N.S.1    Kang, S.W.2    Chakrabarti, O.3    Feigenbaum, L.4    Hegde, R.S.5
  • 34
    • 84904567733 scopus 로고    scopus 로고
    • Cytosolic quality control of mislocalized proteins requires RNF126 recruitment to Bag6
    • Rodrigo-Brenni MC, Gutierrez E, Hegde RS (2014). Cytosolic quality control of mislocalized proteins requires RNF126 recruitment to Bag6. Mol Cell 55, 227-237.
    • (2014) Mol Cell , vol.55 , pp. 227-237
    • Rodrigo-Brenni, M.C.1    Gutierrez, E.2    Hegde, R.S.3
  • 35
    • 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
  • 36
    • 34248679167 scopus 로고    scopus 로고
    • Tricine-SDS-PAGE
    • Schagger H (2006). Tricine-SDS-PAGE. Nat Protocols 1, 16-22.
    • (2006) Nat Protocols , vol.1 , pp. 16-22
    • Schagger, H.1
  • 37
    • 0026472576 scopus 로고
    • Structural requirements for transport of preprocecropinA and related presecretory proteins into mammalian microsomes
    • Schlenstedt G, Gudmundsson GH, Boman HG, Zimmermann R (1992). Structural requirements for transport of preprocecropinA and related presecretory proteins into mammalian microsomes. J Biol Chem 267, 24328-24332.
    • (1992) J Biol Chem , vol.267 , pp. 24328-24332
    • Schlenstedt, G.1    Gudmundsson, G.H.2    Boman, H.G.3    Zimmermann, R.4
  • 38
    • 14544302354 scopus 로고    scopus 로고
    • Co-translational protein targeting by the signal recognition particle
    • Shan SO, Walter P (2005). Co-translational protein targeting by the signal recognition particle. FEBS Lett 579, 921-926.
    • (2005) FEBS Lett , vol.579 , pp. 921-926
    • Shan, S.O.1    Walter, P.2
  • 39
    • 80054041334 scopus 로고    scopus 로고
    • Membrane protein insertion at the endoplasmic reticulum
    • Shao S, Hegde RS (2011). Membrane protein insertion at the endoplasmic reticulum. Annu Rev Cell Dev Biol 27, 25-56.
    • (2011) Annu Rev Cell Dev Biol , vol.27 , pp. 25-56
    • Shao, S.1    Hegde, R.S.2
  • 40
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin E, von Heijne G (1998). Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci 7, 1029-1038.
    • (1998) Protein Sci , vol.7 , pp. 1029-1038
    • Wallin, E.1    Von Heijne, G.2
  • 41
    • 0020994721 scopus 로고
    • Preparation of microsomal membranes for cotranslational protein translocation
    • Walter P, Blobel G (1983). Preparation of microsomal membranes for cotranslational protein translocation. Methods Enzymol 96, 84-93.
    • (1983) Methods Enzymol , vol.96 , pp. 84-93
    • Walter, P.1    Blobel, G.2
  • 42
    • 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, Ye Y (2011). A ubiquitin ligase-associated chaperone holdase maintains polypeptides in soluble states for proteasome degradation. Mol Cell 42, 758-770.
    • (2011) Mol Cell , vol.42 , pp. 758-770
    • Wang, Q.1    Liu, Y.2    Soetandyo, N.3    Baek, K.4    Hegde, R.5    Ye, Y.6
  • 43
    • 84880048596 scopus 로고    scopus 로고
    • A ubiquitin-like domain recruits an oligomeric chaperone to a retrotranslocation complex in endoplasmic reticulum-associated degradation
    • Xu Y, Liu Y, Lee JG, Ye Y (2013). A ubiquitin-like domain recruits an oligomeric chaperone to a retrotranslocation complex in endoplasmic reticulum-associated degradation. J Biol Chem 288, 18068-18076.
    • (2013) J Biol Chem , vol.288 , pp. 18068-18076
    • Xu, Y.1    Liu, Y.2    Lee, J.G.3    Ye, Y.4
  • 44
    • 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


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