메뉴 건너뛰기




Volumn 110, Issue 9, 2013, Pages 3393-3398

Deglycosylation-dependent fluorescent proteins provide unique tools for the study of ER-associated degradation

Author keywords

[No Author keywords available]

Indexed keywords

GLUCAN SYNTHASE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE 1; PEPTIDES AND PROTEINS; UNCLASSIFIED DRUG; VENUS FLUORESCENT PROTEIN;

EID: 84874506918     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1300328110     Document Type: Article
Times cited : (49)

References (38)
  • 1
    • 0038349592 scopus 로고    scopus 로고
    • Mouse proteome analysis
    • RIKEN GER Group; GSL Members
    • Kanapin A, et al.; RIKEN GER Group; GSL Members (2003) Mouse proteome analysis. Genome Res 13(6B): 1335-1344.
    • (2003) Genome Res , vol.13 , Issue.6 B , pp. 1335-1344
    • Kanapin, A.1
  • 2
    • 82255161944 scopus 로고    scopus 로고
    • Road to ruin: Targeting proteins for degradation in the endoplasmic reticulum
    • Smith MH, Ploegh HL, Weissman JS (2011) Road to ruin: Targeting proteins for degradation in the endoplasmic reticulum. Science 334(6059): 1086-1090.
    • (2011) Science , vol.334 , Issue.6059 , pp. 1086-1090
    • Smith, M.H.1    Ploegh, H.L.2    Weissman, J.S.3
  • 3
    • 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(12): 944-957.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , Issue.12 , pp. 944-957
    • Vembar, S.S.1    Brodsky, J.L.2
  • 4
    • 80054026314 scopus 로고    scopus 로고
    • A review of themammalian unfolded protein response
    • Chakrabarti A, Chen AW, Varner JD (2011) A review of themammalian unfolded protein response. Biotechnol Bioeng 108(12): 2777-2793.
    • (2011) Biotechnol Bioeng , vol.108 , Issue.12 , pp. 2777-2793
    • Chakrabarti, A.1    Chen, A.W.2    Varner, J.D.3
  • 5
    • 0033208984 scopus 로고    scopus 로고
    • ER protein quality control and proteasome-mediated protein degradation
    • Brodsky JL, McCracken AA (1999) ER protein quality control and proteasome-mediated protein degradation. Semin Cell Dev Biol 10(5): 507-513.
    • (1999) Semin Cell Dev Biol , vol.10 , Issue.5 , pp. 507-513
    • Brodsky, J.L.1    McCracken, A.A.2
  • 6
    • 66749130213 scopus 로고    scopus 로고
    • A model of the unfolded protein response: Pancreatic beta-cell as a case study
    • Schnell S (2009) A model of the unfolded protein response: Pancreatic beta-cell as a case study. Cell Physiol Biochem 23(4-6): 233-244.
    • (2009) Cell Physiol Biochem , vol.23 , Issue.4-6 , pp. 233-244
    • Schnell, S.1
  • 7
    • 10644225416 scopus 로고    scopus 로고
    • Protein misfolding and aggregation: New examples in medicine and biology of the dark side of the protein world
    • Stefani M (2004) Protein misfolding and aggregation: New examples in medicine and biology of the dark side of the protein world. Biochim Biophys Acta 1739(1): 5-25.
    • (2004) Biochim Biophys Acta , vol.1739 , Issue.1 , pp. 5-25
    • Stefani, M.1
  • 8
    • 40249088336 scopus 로고    scopus 로고
    • OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD
    • Christianson JC, Shaler TA, Tyler RE, Kopito RR (2008) OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD. Nat Cell Biol 10(3): 272-282.
    • (2008) Nat Cell Biol , vol.10 , Issue.3 , pp. 272-282
    • Christianson, J.C.1    Shaler, T.A.2    Tyler, R.E.3    Kopito, R.R.4
  • 9
    • 51049121849 scopus 로고    scopus 로고
    • Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP
    • Hosokawa N, et al. (2008) Human XTP3-B forms an endoplasmic reticulum quality control scaffold with the HRD1-SEL1L ubiquitin ligase complex and BiP. J Biol Chem 283(30): 20914-20924.
    • (2008) J Biol Chem , vol.283 , Issue.30 , pp. 20914-20924
    • Hosokawa, N.1
  • 10
    • 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(6994): 834-840.
    • (2004) Nature , vol.429 , Issue.6994 , pp. 834-840
    • Lilley, B.N.1    Ploegh, H.L.2
  • 11
    • 3042677637 scopus 로고    scopus 로고
    • A membrane protein complex mediates retro-translocation fromthe ER lumen into the cytosol
    • Ye Y, Shibata Y, Yun C, Ron D, Rapoport TA (2004) A membrane protein complex mediates retro-translocation fromthe ER lumen into the cytosol. Nature 429(6994): 841-847.
    • (2004) Nature , vol.429 , Issue.6994 , pp. 841-847
    • Ye, Y.1    Shibata, Y.2    Yun, C.3    Ron, D.4    Rapoport, T.A.5
  • 12
    • 36248988054 scopus 로고    scopus 로고
    • Ubiquitin ligases, critical mediators of endoplasmic reticulum-associated degradation
    • Kostova Z, Tsai YC, Weissman AM (2007) Ubiquitin ligases, critical mediators of endoplasmic reticulum-associated degradation. Semin Cell Dev Biol 18(6): 770-779.
    • (2007) Semin Cell Dev Biol , vol.18 , Issue.6 , pp. 770-779
    • Kostova, Z.1    Tsai, Y.C.2    Weissman, A.M.3
  • 13
    • 77957189436 scopus 로고    scopus 로고
    • ERAD ubiquitin ligases: Multifunctional tools for protein quality control and waste disposal in the endoplasmic reticulum
    • Mehnert M, Sommer T, Jarosch E (2010) ERAD ubiquitin ligases: Multifunctional tools for protein quality control and waste disposal in the endoplasmic reticulum. Bioessays 32(10): 905-913.
    • (2010) Bioessays , vol.32 , Issue.10 , pp. 905-913
    • Mehnert, M.1    Sommer, T.2    Jarosch, E.3
  • 14
    • 78149482323 scopus 로고    scopus 로고
    • Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p
    • Carvalho P, Stanley AM, Rapoport TA (2010) Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p. Cell 143(4): 579-591.
    • (2010) Cell , vol.143 , Issue.4 , pp. 579-591
    • Carvalho, P.1    Stanley, A.M.2    Rapoport, T.A.3
  • 15
    • 0037084028 scopus 로고    scopus 로고
    • Role of the ubiquitinselective 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 ubiquitinselective CDC48(UFD1/NPL4) chaperone (segregase) in ERAD of OLE1 and other substrates. EMBO J 21(4): 615-621.
    • (2002) EMBO J , vol.21 , Issue.4 , pp. 615-621
    • Braun, S.1    Matuschewski, K.2    Rape, M.3    Thoms, S.4    Jentsch, S.5
  • 16
    • 0036173013 scopus 로고    scopus 로고
    • Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48
    • Jarosch E, et al. (2002) Protein dislocation from the ER requires polyubiquitination and the AAA-ATPase Cdc48. Nat Cell Biol 4(2): 134-139.
    • (2002) Nat Cell Biol , vol.4 , Issue.2 , pp. 134-139
    • Jarosch, E.1
  • 17
    • 0036136901 scopus 로고    scopus 로고
    • AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation
    • Rabinovich E, Kerem A, Fröhlich KU, Diamant N, Bar-Nun S (2002) AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation. Mol Cell Biol 22(2): 626-634.
    • (2002) Mol Cell Biol , vol.22 , Issue.2 , pp. 626-634
    • Rabinovich, E.1    Kerem, A.2    Fröhlich, K.U.3    Diamant, N.4    Bar-Nun, S.5
  • 18
    • 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(6864): 652-656.
    • (2001) Nature , vol.414 , Issue.6864 , pp. 652-656
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 19
    • 77956048943 scopus 로고    scopus 로고
    • A toolkit of proteinfragment complementation assays for studying and dissecting large-scale and dynamic protein-protein interactions in living cells
    • Michnick SW, Ear PH, Landry C, Malleshaiah MK, Messier V (2010) A toolkit of proteinfragment complementation assays for studying and dissecting large-scale and dynamic protein-protein interactions in living cells. Methods Enzymol 470: 335-368.
    • (2010) Methods Enzymol , vol.470 , pp. 335-368
    • Michnick, S.W.1    Ear, P.H.2    Landry, C.3    Malleshaiah, M.K.4    Messier, V.5
  • 20
    • 0037416196 scopus 로고    scopus 로고
    • A role for N-glycanase in the cytosolic turnover of glycoproteins
    • Hirsch C, Blom D, Ploegh HL (2003) A role for N-glycanase in the cytosolic turnover of glycoproteins. EMBO J 22(5): 1036-1046.
    • (2003) EMBO J , vol.22 , Issue.5 , pp. 1036-1046
    • Hirsch, C.1    Blom, D.2    Ploegh, H.L.3
  • 21
    • 0027259262 scopus 로고
    • Identification of peptide:Nglycanase activity in mammalian-derived cultured cells
    • Suzuki T, Seko A, Kitajima K, Inoue Y, Inoue S (1993) Identification of peptide:Nglycanase activity in mammalian-derived cultured cells. Biochem Biophys Res Commun 194(3): 1124-1130.
    • (1993) Biochem Biophys Res Commun , vol.194 , Issue.3 , pp. 1124-1130
    • Suzuki, T.1    Seko, A.2    Kitajima, K.3    Inoue, Y.4    Inoue, S.5
  • 22
    • 0017381301 scopus 로고
    • Demonstration of a new amidase acting on glycopeptides
    • Takahashi N (1977) Demonstration of a new amidase acting on glycopeptides. Biochem Biophys Res Commun 76(4): 1194-1201.
    • (1977) Biochem Biophys Res Commun , vol.76 , Issue.4 , pp. 1194-1201
    • Takahashi, N.1
  • 23
    • 10644226176 scopus 로고    scopus 로고
    • Using a small molecule inhibitor of peptide: N-glycanase to probe its role in glycoprotein turnover
    • Misaghi S, Pacold ME, Blom D, Ploegh HL, Korbel GA (2004) Using a small molecule inhibitor of peptide: N-glycanase to probe its role in glycoprotein turnover. Chem Biol 11(12): 1677-1687.
    • (2004) Chem Biol , vol.11 , Issue.12 , pp. 1677-1687
    • Misaghi, S.1    Pacold, M.E.2    Blom, D.3    Ploegh, H.L.4    Korbel, G.A.5
  • 24
    • 76149098224 scopus 로고    scopus 로고
    • Stringent requirement for HRD1, SEL1L, andOS-9/XTP3-B for disposal of ERAD-LS substrates
    • Bernasconi R, Galli C, Calanca V, Nakajima T, Molinari M (2010) Stringent requirement for HRD1, SEL1L, andOS-9/XTP3-B for disposal of ERAD-LS substrates.J CellBiol 188(2): 223-235.
    • (2010) J CellBiol , vol.188 , Issue.2 , pp. 223-235
    • Bernasconi, R.1    Galli, C.2    Calanca, V.3    Nakajima, T.4    Molinari, M.5
  • 25
    • 79952133558 scopus 로고    scopus 로고
    • HRD1 and UBE2J1 target misfolded MHC class i heavy chains for endoplasmic reticulum-associated degradation
    • Burr ML, et al. (2011) HRD1 and UBE2J1 target misfolded MHC class I heavy chains for endoplasmic reticulum-associated degradation. Proc Natl Acad Sci USA 108(5): 2034-2039.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.5 , pp. 2034-2039
    • Burr, M.L.1
  • 26
    • 42949115445 scopus 로고    scopus 로고
    • SEL1L and HRD1 are involved in the degradation of unassembled secretory Ig-mu chains
    • Cattaneo M, et al. (2008) SEL1L and HRD1 are involved in the degradation of unassembled secretory Ig-mu chains. J Cell Physiol 215(3): 794-802.
    • (2008) J Cell Physiol , vol.215 , Issue.3 , pp. 794-802
    • Cattaneo, M.1
  • 27
    • 9144239817 scopus 로고    scopus 로고
    • Human HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum
    • Kikkert M, et al. (2004) Human HRD1 is an E3 ubiquitin ligase involved in degradation of proteins from the endoplasmic reticulum. J Biol Chem 279(5): 3525-3534.
    • (2004) J Biol Chem , vol.279 , Issue.5 , pp. 3525-3534
    • Kikkert, M.1
  • 28
    • 33845536214 scopus 로고    scopus 로고
    • A ubiquitin ligase HRD1 promotes the degradation of Pael receptor, a substrate of Parkin
    • Omura T, et al. (2006) A ubiquitin ligase HRD1 promotes the degradation of Pael receptor, a substrate of Parkin. J Neurochem 99(6): 1456-1469.
    • (2006) J Neurochem , vol.99 , Issue.6 , pp. 1456-1469
    • Omura, T.1
  • 29
    • 0023907965 scopus 로고
    • A frameshift mutation results in a truncated alpha 1-antitrypsin that is retained within the rough endoplasmic reticulum
    • Sifers RN, Brashears-Macatee S, Kidd VJ, Muensch H, Woo SL (1988) A frameshift mutation results in a truncated alpha 1-antitrypsin that is retained within the rough endoplasmic reticulum. J Biol Chem 263(15): 7330-7335.
    • (1988) J Biol Chem , vol.263 , Issue.15 , pp. 7330-7335
    • Sifers, R.N.1    Brashears-Macatee, S.2    Kidd, V.J.3    Muensch, H.4    Woo, S.L.5
  • 30
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • Johnston JA, Ward CL, Kopito RR (1998) Aggresomes: A cellular response to misfolded proteins. J Cell Biol 143(7): 1883-1898.
    • (1998) J Cell Biol , vol.143 , Issue.7 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 31
    • 68349112682 scopus 로고    scopus 로고
    • Statistical methods for analysis of high-throughput RNA interference screens
    • Birmingham A, et al. (2009) Statistical methods for analysis of high-throughput RNA interference screens. Nat Methods 6(8): 569-575.
    • (2009) Nat Methods , vol.6 , Issue.8 , pp. 569-575
    • Birmingham, A.1
  • 32
    • 26444621357 scopus 로고    scopus 로고
    • Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane
    • Ye Y, et al. (2005) Recruitment of the p97 ATPase and ubiquitin ligases to the site of retrotranslocation at the endoplasmic reticulum membrane. Proc Natl Acad Sci USA 102(40): 14132-14138.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.40 , pp. 14132-14138
    • Ye, Y.1
  • 33
    • 67650535999 scopus 로고    scopus 로고
    • Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans
    • Hosokawa N, Kamiya Y, Kamiya D, Kato K, Nagata K (2009) Human OS-9, a lectin required for glycoprotein endoplasmic reticulum-associated degradation, recognizes mannose-trimmed N-glycans. J Biol Chem 284(25): 17061-17068.
    • (2009) J Biol Chem , vol.284 , Issue.25 , pp. 17061-17068
    • Hosokawa, N.1    Kamiya, Y.2    Kamiya, D.3    Kato, K.4    Nagata, K.5
  • 34
    • 84864976096 scopus 로고    scopus 로고
    • Live cell imaging of protein dislocation from the endoplasmic reticulum
    • Zhong Y, Fang S (2012) Live cell imaging of protein dislocation from the endoplasmic reticulum. J Biol Chem 287(33): 28057-28066.
    • (2012) J Biol Chem , vol.287 , Issue.33 , pp. 28057-28066
    • Zhong, Y.1    Fang, S.2
  • 35
    • 66349084131 scopus 로고    scopus 로고
    • Oligosaccharyltransferase directly binds to ribosome at a location near the translocon-binding site
    • Harada Y, Li H, Li H, LennarzWJ (2009)Oligosaccharyltransferase directly binds to ribosome at a location near the translocon-binding site. Proc Natl Acad Sci USA 106(17): 6945-6949.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.17 , pp. 6945-6949
    • Harada, Y.1    Li, H.2    Li, H.3    Lennarz, W.J.4
  • 36
    • 79953745092 scopus 로고    scopus 로고
    • Superfolder GFP is fluorescent in oxidizing environments when targeted via the Sec translocon
    • Aronson DE, Costantini LM, Snapp EL (2011) Superfolder GFP is fluorescent in oxidizing environments when targeted via the Sec translocon. Traffic 12(5): 543-548.
    • (2011) Traffic , vol.12 , Issue.5 , pp. 543-548
    • Aronson, D.E.1    Costantini, L.M.2    Snapp, E.L.3
  • 37
    • 0035893753 scopus 로고    scopus 로고
    • Oligomerization of green fluorescent protein in the secretory pathway of endocrine cells
    • Jain RK, Joyce PB, Molinete M, Halban PA, Gorr SU (2001) Oligomerization of green fluorescent protein in the secretory pathway of endocrine cells. Biochem J 360(Pt 3): 645-649.
    • (2001) Biochem J , vol.360 , Issue.PART 3 , pp. 645-649
    • Jain, R.K.1    Joyce, P.B.2    Molinete, M.3    Halban, P.A.4    Gorr, S.U.5
  • 38
    • 22144472527 scopus 로고    scopus 로고
    • Proton pathways in green fluorescence protein
    • Agmon N (2005) Proton pathways in green fluorescence protein. Biophys J 88(4): 2452-2461.
    • (2005) Biophys J , vol.88 , Issue.4 , pp. 2452-2461
    • Agmon, N.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.