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Volumn 6, Issue 3, 2005, Pages 239-244

Glycoprotein-specific ubiquitin ligases recognize N-glycans in unfolded substrates

Author keywords

Glycoprotein; N glycan; Ubiquitin ligase; Unfold

Indexed keywords

ADENOSINE TRIPHOSPHATASE; BETA1 INTEGRIN; GLYCAN DERIVATIVE; GLYCOPROTEIN; MANNOSE; OLIGOSACCHARIDE; PROTEIN P97; UBIQUITIN PROTEIN LIGASE;

EID: 16844369621     PISSN: 1469221X     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.embor.7400351     Document Type: Article
Times cited : (80)

References (24)
  • 1
    • 0035144199 scopus 로고    scopus 로고
    • Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation
    • Bays NW, Gardner RG, Seelig LP, Joazeiro CA, Hampton RY (2001) Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation. Nat Cell Biol 3: 24-29
    • (2001) Nat. Cell Biol. , vol.3 , pp. 24-29
    • Bays, N.W.1    Gardner, R.G.2    Seelig, L.P.3    Joazeiro, C.A.4    Hampton, R.Y.5
  • 2
    • 1442313919 scopus 로고    scopus 로고
    • A glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromised
    • Blom D, Hirsch C, Stern P, Tortorella D, Ploegh HL (2004) A glycosylated type I membrane protein becomes cytosolic when peptide: N glycanase is compromised. EMBO J 23: 650-658
    • (2004) EMBO J. , vol.23 , pp. 650-658
    • Blom, D.1    Hirsch, C.2    Stern, P.3    Tortorella, D.4    Ploegh, H.L.5
  • 3
    • 0037422614 scopus 로고    scopus 로고
    • UDP-Glc: Glycoprotein glucosyltransferase recognizes structured and solvent accessible hydrophobic patches in molten globule-like folding intermediates
    • Caramelo JJ, Castro OA, Alonso LG, De Prat-Gay G, Parodi AJ (2003) UDP-Glc:glycoprotein glucosyltransferase recognizes structured and solvent accessible hydrophobic patches in molten globule-like folding intermediates. Proc Natl Acad Sci USA 100: 86-91
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 86-91
    • Caramelo, J.J.1    Castro, O.A.2    Alonso, L.G.3    De Prat-Gay, G.4    Parodi, A.J.5
  • 4
    • 0034608370 scopus 로고    scopus 로고
    • Receptor-mediated uptake of antigen/heat shock protein complexes results in major histocompatibility complex class I antigen presentation via two distinct processing pathways
    • Castellino F et al (2000) Receptor-mediated uptake of antigen/heat shock protein complexes results in major histocompatibility complex class I antigen presentation via two distinct processing pathways. J Exp Med 191: 1957-1964
    • (2000) J. Exp. Med. , vol.191 , pp. 1957-1964
    • Castellino, F.1
  • 5
    • 0033279836 scopus 로고    scopus 로고
    • SCF and Cullin/Ring H2-based ubiquitin ligases
    • Deshaies RJ (1999) SCF and Cullin/Ring H2-based ubiquitin ligases. Annu Rev Cell Dev Biol 15: 435-467
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 435-467
    • Deshaies, R.J.1
  • 6
    • 1042278180 scopus 로고    scopus 로고
    • Distinct steps in dislocation of luminal endoplasmic reticulum-associated degradation substrates: Roles of endoplamic reticulum-bound p97/Cdc48p and proteasome
    • Elkabetz Y, Shapira I, Rabinovich E, Bar-Nun S (2004) Distinct steps in dislocation of luminal endoplasmic reticulum-associated degradation substrates: roles of endoplamic reticulum-bound p97/Cdc48p and proteasome. J Biol Chem 279: 3980-3989
    • (2004) J. Biol. Chem. , vol.279 , pp. 3980-3989
    • Elkabetz, Y.1    Shapira, I.2    Rabinovich, E.3    Bar-Nun, S.4
  • 8
    • 0035807839 scopus 로고    scopus 로고
    • The tumour autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum
    • Fang S, Ferrone M, Yang C, Jensen JP, Tiwari S, Weissman AM (2001) The tumour autocrine motility factor receptor, gp78, is a ubiquitin protein ligase implicated in degradation from the endoplasmic reticulum. Proc Natl Acad Sci USA 98: 14422-14427
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14422-14427
    • Fang, S.1    Ferrone, M.2    Yang, C.3    Jensen, J.P.4    Tiwari, S.5    Weissman, A.M.6
  • 9
    • 1442331636 scopus 로고    scopus 로고
    • Yeast N-glycanase distinguishes between native and non-native glycoproteins
    • Hirsch C, Misaghi S, Blom D, Pacold ME, Ploegh HL (2004) Yeast N-glycanase distinguishes between native and non-native glycoproteins. EMBO Rep 5: 201-206
    • (2004) EMBO Rep. , vol.5 , pp. 201-206
    • Hirsch, C.1    Misaghi, S.2    Blom, D.3    Pacold, M.E.4    Ploegh, H.L.5
  • 10
    • 0035967883 scopus 로고    scopus 로고
    • An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin
    • Imai Y, Soda M, Inoue H, Hattori N, Mizuno Y, Takahashi R (2001) An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin. Cell 105: 891-902
    • (2001) Cell , vol.105 , pp. 891-902
    • Imai, Y.1    Soda, M.2    Inoue, H.3    Hattori, N.4    Mizuno, Y.5    Takahashi, R.6
  • 11
    • 0028910938 scopus 로고
    • A phagosome-to-cytosol pathway for exogenous antigens presented on MHC class I molecules
    • Kovacsovics-Bankowski M, Rock KL (1995) A phagosome-to-cytosol pathway for exogenous antigens presented on MHC class I molecules. Science 267: 243-246
    • (1995) Science , vol.267 , pp. 243-246
    • Kovacsovics-Bankowski, M.1    Rock, K.L.2
  • 12
    • 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
  • 13
  • 14
    • 12144289596 scopus 로고    scopus 로고
    • Structural basis of sugar-recognizing ubiquitin ligase
    • Mizushima T et al (2004) Structural basis of sugar-recognizing ubiquitin ligase. Nat Struct Mol Biol 11: 365-370
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 365-370
    • Mizushima, T.1
  • 15
    • 0033782777 scopus 로고    scopus 로고
    • Protein glucosylation and its role in protein folding
    • Parodi AJ (2000) Protein glucosylation and its role in protein folding. Annu Rev Biochem 69: 69-93
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 69-93
    • Parodi, A.J.1
  • 16
    • 0029126624 scopus 로고
    • The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc: Glycoprotein glucosyltransferase
    • Sousa M, Parodi AJ (1995) The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. EMBO J 14: 4196-4203
    • (1995) EMBO J. , vol.14 , pp. 4196-4203
    • Sousa, M.1    Parodi, A.J.2
  • 17
    • 0035887277 scopus 로고    scopus 로고
    • A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matα2 repressor degradation
    • Swanson R, Locher M, Hochstrasser M (2001) A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matα2 repressor degradation. Genes Dev 15: 2660-2674
    • (2001) Genes Dev. , vol.15 , pp. 2660-2674
    • Swanson, R.1    Locher, M.2    Hochstrasser, M.3
  • 18
    • 0036270698 scopus 로고    scopus 로고
    • Retro-translocation of proteins from the endoplasmic reticulum into the cytosol
    • Tsai B, Ye Y, Rapoport TA (2002) Retro-translocation of proteins from the endoplasmic reticulum into the cytosol. Nat Rev Mol Cell Biol 3: 246-255
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 246-255
    • Tsai, B.1    Ye, Y.2    Rapoport, T.A.3
  • 19
    • 0023665255 scopus 로고
    • The crystal structure of ribonuclease B at 2.5-Å resolution
    • Williams RL, Greene SM, McPherson A (1987) The crystal structure of ribonuclease B at 2.5-Å resolution. J Biol Chem 262: 16020-16031
    • (1987) J. Biol. Chem. , vol.262 , pp. 16020-16031
    • Williams, R.L.1    Greene, S.M.2    McPherson, A.3
  • 20
    • 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
  • 21
    • 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
  • 22
    • 0141814712 scopus 로고    scopus 로고
    • A novel role for N-glycans in the ERAD system
    • Yoshida Y (2003) A novel role for N-glycans in the ERAD system. J Biochem, (Tokyo) 134: 183-190
    • (2003) J. Biochem. (Tokyo) , vol.134 , pp. 183-190
    • Yoshida, Y.1
  • 23
    • 18444413218 scopus 로고    scopus 로고
    • E3 ubiquitin ligase that recognizes sugar chains
    • Yoshida Y et al (2002) E3 ubiquitin ligase that recognizes sugar chains. Nature 418: 438-442
    • (2002) Nature , vol.418 , pp. 438-442
    • Yoshida, Y.1
  • 24
    • 0242321836 scopus 로고    scopus 로고
    • Fbs2 is a new member of the E3 ubiquitin ligase family that recognizes sugar chains
    • Yoshida Y, Tokunaga F, Chiba T, Iwai K, Tanaka K, Tai T (2003) Fbs2 is a new member of the E3 ubiquitin ligase family that recognizes sugar chains. J Biol Chem 278: 43877-43884
    • (2003) J. Biol. Chem. , vol.278 , pp. 43877-43884
    • Yoshida, Y.1    Tokunaga, F.2    Chiba, T.3    Iwai, K.4    Tanaka, K.5    Tai, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.