메뉴 건너뛰기




Volumn 360, Issue 2, 2007, Pages 357-362

Analysis of ER-associated glycoprotein degradation using synthetic glycopeptide probes

Author keywords

ER associated degradation; F box protein; Fluorescent correlation spectroscopy; Peptide:N glycanase; Proteasome

Indexed keywords

CHITOBIOSE; F BOX PROTEIN; GLYCOPEPTIDASE; GLYCOPEPTIDE; GLYCOPROTEIN; MANNOSE; PROTEASOME;

EID: 34447098303     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.06.053     Document Type: Article
Times cited : (15)

References (34)
  • 1
    • 0032904470 scopus 로고    scopus 로고
    • The dolichol pathway of N-linked glycosylation
    • Burda P., and Aebi M. The dolichol pathway of N-linked glycosylation. Biochim. Biophys. Acta 1426 (1999) 239-257
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 239-257
    • Burda, P.1    Aebi, M.2
  • 2
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • Helenius A., and Aebi M. Roles of N-linked glycans in the endoplasmic reticulum. Annu. Rev. Biochem. 73 (2004) 1019-1049
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 3
    • 2442505584 scopus 로고    scopus 로고
    • Role of N-linked polymannose oligosaccharides in targeting glycoproteins for endoplasmic reticulum-associated degradation
    • Spiro R.G. Role of N-linked polymannose oligosaccharides in targeting glycoproteins for endoplasmic reticulum-associated degradation. Cell. Mol. Life Sci. 61 (2004) 1025-1041
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 1025-1041
    • Spiro, R.G.1
  • 4
    • 0346096508 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum protein factory
    • Sitia R., and Braakman I. Quality control in the endoplasmic reticulum protein factory. Nature 426 (2003) 891-894
    • (2003) Nature , vol.426 , pp. 891-894
    • Sitia, R.1    Braakman, I.2
  • 5
    • 15944408403 scopus 로고    scopus 로고
    • In vitro and in vivo assays to assess the functions of calnexin and calreticulin in ER protein folding and quality control
    • Paquet M.E., Leach M.R., and Williams D.B. In vitro and in vivo assays to assess the functions of calnexin and calreticulin in ER protein folding and quality control. Methods 35 (2005) 338-347
    • (2005) Methods , vol.35 , pp. 338-347
    • Paquet, M.E.1    Leach, M.R.2    Williams, D.B.3
  • 6
    • 25844454688 scopus 로고    scopus 로고
    • Structural approaches to the study of oligosaccharides in glycoprotein quality control
    • Ito Y., Hagihara S., Matsuo I., and Totani K. Structural approaches to the study of oligosaccharides in glycoprotein quality control. Curr. Opin. Struct. Biol. 15 (2005) 481-489
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 481-489
    • Ito, Y.1    Hagihara, S.2    Matsuo, I.3    Totani, K.4
  • 8
    • 3042818270 scopus 로고    scopus 로고
    • ER-60 domains responsible for interaction with calnexin and calreticulin
    • Urade R., Okudo H., Kato H., Moriyama T., and Arakaki Y. ER-60 domains responsible for interaction with calnexin and calreticulin. Biochemistry 43 (2004) 8858-8868
    • (2004) Biochemistry , vol.43 , pp. 8858-8868
    • Urade, R.1    Okudo, H.2    Kato, H.3    Moriyama, T.4    Arakaki, Y.5
  • 9
    • 0037470515 scopus 로고    scopus 로고
    • EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin
    • Oda Y., Hosokawa N., Wada I., and Nagata K. EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin. Science 299 (2003) 1394-1397
    • (2003) Science , vol.299 , pp. 1394-1397
    • Oda, Y.1    Hosokawa, N.2    Wada, I.3    Nagata, K.4
  • 10
    • 0037470410 scopus 로고    scopus 로고
    • Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle
    • Molinari M., Calance V., Galli C., Lucca P., and Paganetti P. Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle. Science 299 (2003) 1397-1400
    • (2003) Science , vol.299 , pp. 1397-1400
    • Molinari, M.1    Calance, V.2    Galli, C.3    Lucca, P.4    Paganetti, P.5
  • 11
    • 0037566901 scopus 로고    scopus 로고
    • For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection
    • Kostova Z., and Wolf D.H. For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection. EMBO J. 22 (2003) 2309-2317
    • (2003) EMBO J. , vol.22 , pp. 2309-2317
    • Kostova, Z.1    Wolf, D.H.2
  • 12
    • 0030695025 scopus 로고    scopus 로고
    • A complex of Cdc4p, Skp1p, and Cdc53p/Cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p
    • Feldman R.M., Correll C.C., Kaplan K.B., and Deshaies R.J. A complex of Cdc4p, Skp1p, and Cdc53p/Cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p. Cell 91 (1997) 221-230
    • (1997) Cell , vol.91 , pp. 221-230
    • Feldman, R.M.1    Correll, C.C.2    Kaplan, K.B.3    Deshaies, R.J.4
  • 13
    • 0030662523 scopus 로고    scopus 로고
    • F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex
    • Skowyra D., Craig K.L., Tyers M., Elledge S.J., and Harper J.W. F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex. Cell 91 (1997) 209-219
    • (1997) Cell , vol.91 , pp. 209-219
    • Skowyra, D.1    Craig, K.L.2    Tyers, M.3    Elledge, S.J.4    Harper, J.W.5
  • 15
    • 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., and Tai T. Fbs2 is a new member of the E3 ubiquitin ligase family that recognizes sugar chains. J. Biol. Chem. 278 (2003) 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
  • 16
    • 0032867676 scopus 로고    scopus 로고
    • THE 26S PROTEASOME: a molecular machine designed for controlled proteolysis
    • Voges D., Zwickl P., and Baumeister W. THE 26S PROTEASOME: a molecular machine designed for controlled proteolysis. Annu. Rev. Biochem. 68 (1999) 1015-1068
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 17
    • 0036239939 scopus 로고    scopus 로고
    • Cytoplasmic peptide:N-glycanase (PNGase) in eukaryotic cells: occurrence, primary structure, and potential functions
    • Suzuki T., Park H., and Lennarz W.J. Cytoplasmic peptide:N-glycanase (PNGase) in eukaryotic cells: occurrence, primary structure, and potential functions. FASEB J. 16 (2002) 635-641
    • (2002) FASEB J. , vol.16 , pp. 635-641
    • Suzuki, T.1    Park, H.2    Lennarz, W.J.3
  • 18
    • 0028362217 scopus 로고
    • Purification and enzymatic properties of peptide:N-glycanase from C3H mouse-derived L-929 fibroblast cells. Possible widespread occurrence of post-translational remodification of proteins by N-deglycosylation
    • Suzuki T., Seko A., Kitajima K., Inoue Y., and Inoue S. Purification and enzymatic properties of peptide:N-glycanase from C3H mouse-derived L-929 fibroblast cells. Possible widespread occurrence of post-translational remodification of proteins by N-deglycosylation. J. Biol. Chem. 269 (1994) 17611-17618
    • (1994) J. Biol. Chem. , vol.269 , pp. 17611-17618
    • Suzuki, T.1    Seko, A.2    Kitajima, K.3    Inoue, Y.4    Inoue, S.5
  • 20
    • 0037416196 scopus 로고    scopus 로고
    • A role for N-glycanase in the cytosolic turnover of glycoproteins
    • Hirsch C., Blom D., and Ploegh H.L. A role for N-glycanase in the cytosolic turnover of glycoproteins. EMBO J. 22 (2003) 1036-1046
    • (2003) EMBO J. , vol.22 , pp. 1036-1046
    • Hirsch, C.1    Blom, D.2    Ploegh, H.L.3
  • 21
    • 0036216613 scopus 로고    scopus 로고
    • Synthesis of N-linked glycosyl asparagine derivatives with unprotected sugar components
    • Ishiwata A., Takatani M., Nakahara Y., and Ito Y. Synthesis of N-linked glycosyl asparagine derivatives with unprotected sugar components. Synlett (2002) 634-636
    • (2002) Synlett , pp. 634-636
    • Ishiwata, A.1    Takatani, M.2    Nakahara, Y.3    Ito, Y.4
  • 24
    • 0033613196 scopus 로고    scopus 로고
    • The catalytic sites of 20S proteasomes and their role in subunit maturation: a mutational and crystallographic study
    • Groll M., Heinemeyer W., Jager S., Ullrich T., Bochtler M., Wolf D.H., and Huber R. The catalytic sites of 20S proteasomes and their role in subunit maturation: a mutational and crystallographic study. Proc. Natl. Acad. Sci. USA 96 (1999) 10976-10983
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10976-10983
    • Groll, M.1    Heinemeyer, W.2    Jager, S.3    Ullrich, T.4    Bochtler, M.5    Wolf, D.H.6    Huber, R.7
  • 25
    • 0027421430 scopus 로고
    • Purification and characterization of a Z-Leu-Leu-Leu-MCA degrading protease expected to regulate nitrite formation: a novel catalytic activity in proteasome
    • Tsubuki S., Kawasaki H., Saito Y., Miyashita N., Inomata M., and Kawashima S. Purification and characterization of a Z-Leu-Leu-Leu-MCA degrading protease expected to regulate nitrite formation: a novel catalytic activity in proteasome. Biochem. Biophys. Res. Commun. 196 (1993) 1195-1201
    • (1993) Biochem. Biophys. Res. Commun. , vol.196 , pp. 1195-1201
    • Tsubuki, S.1    Kawasaki, H.2    Saito, Y.3    Miyashita, N.4    Inomata, M.5    Kawashima, S.6
  • 26
    • 0037452979 scopus 로고    scopus 로고
    • Proteasome-dependent, ubiquitin-independent degradation of the Rb family of tumor suppressors by the human cytomegalovirus pp71 protein
    • Kalejta R.F., and Shenk T. Proteasome-dependent, ubiquitin-independent degradation of the Rb family of tumor suppressors by the human cytomegalovirus pp71 protein. Proc. Natl. Acad. Sci. USA 100 (2003) 3263-3268
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 3263-3268
    • Kalejta, R.F.1    Shenk, T.2
  • 28
    • 18244371937 scopus 로고    scopus 로고
    • Thermodynamic analysis of interactions between N-linked sugar chains and F-box protein Fbs1
    • Hagihara S., Totani K., Matsuo I., and Ito Y. Thermodynamic analysis of interactions between N-linked sugar chains and F-box protein Fbs1. J. Med. Chem. 48 (2005) 3126-3129
    • (2005) J. Med. Chem. , vol.48 , pp. 3126-3129
    • Hagihara, S.1    Totani, K.2    Matsuo, I.3    Ito, Y.4
  • 29
    • 0028998706 scopus 로고
    • Carbohydrate-binding property of peptide:N-glycanase from mouse fibroblast L-929 cells as evaluated by inhibition and binding experiments using various oligosaccharides
    • Suzuki T., Seko A., Kitajima K., Inoue Y., and Inoue S. Carbohydrate-binding property of peptide:N-glycanase from mouse fibroblast L-929 cells as evaluated by inhibition and binding experiments using various oligosaccharides. J. Biol. Chem. 270 (1995) 15181-15186
    • (1995) J. Biol. Chem. , vol.270 , pp. 15181-15186
    • Suzuki, T.1    Seko, A.2    Kitajima, K.3    Inoue, Y.4    Inoue, S.5
  • 30
    • 12744281810 scopus 로고    scopus 로고
    • Misfolding of glycoproteins is a prerequisite for peptide:N-glycanase mediated deglycosylation
    • Joshi S., Katiyar S., and Lennarz W.J. Misfolding of glycoproteins is a prerequisite for peptide:N-glycanase mediated deglycosylation. FEBS Lett. 579 (2005) 823-826
    • (2005) FEBS Lett. , vol.579 , pp. 823-826
    • Joshi, S.1    Katiyar, S.2    Lennarz, W.J.3
  • 31
    • 21544450264 scopus 로고    scopus 로고
    • Structure of a peptide:N-glycanase-Rad23 complex: insight into the deglycosylation for denatured glycoproteins
    • Lee J.H., Choi J.M., Lee C., Yi K.J., and Cho Y. Structure of a peptide:N-glycanase-Rad23 complex: insight into the deglycosylation for denatured glycoproteins. Proc. Natl. Acad. Sci. USA 102 (2005) 9144-9149
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 9144-9149
    • Lee, J.H.1    Choi, J.M.2    Lee, C.3    Yi, K.J.4    Cho, Y.5
  • 32
    • 0037162548 scopus 로고    scopus 로고
    • Endo-β-N-acetylglucosaminidase, an enzyme involved in processing of free oligosaccharide in the cytosol
    • Suzuki T., Yano K., Sugimoto S., Kitajima K., Lennarz W.J., Inoue S., and Inoue Y. Endo-β-N-acetylglucosaminidase, an enzyme involved in processing of free oligosaccharide in the cytosol. Proc. Natl. Acad. Sci. 99 (2002) 9691-9696
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 9691-9696
    • Suzuki, T.1    Yano, K.2    Sugimoto, S.3    Kitajima, K.4    Lennarz, W.J.5    Inoue, S.6    Inoue, Y.7
  • 34
    • 34147130645 scopus 로고    scopus 로고
    • A neural-specific F-box protein Fbs1 functions as a chaperone suppressing glycoprotein aggregation
    • Yoshida Y., Murakami A., Iwai K., and Tanaka K. A neural-specific F-box protein Fbs1 functions as a chaperone suppressing glycoprotein aggregation. J. Biol. Chem. 282 (2007) 7137-7144
    • (2007) J. Biol. Chem. , vol.282 , pp. 7137-7144
    • Yoshida, Y.1    Murakami, A.2    Iwai, K.3    Tanaka, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.