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E3 ubiquitin ligase that recognizes sugar chains

Author

Listed:
  • Yukiko Yoshida

    (Tokyo Metropolitan Institute of Medical Science)

  • Tomoki Chiba

    (Tokyo Metropolitan Institute of Medical Science
    CREST, Japan Science and Technology Corporation (JST))

  • Fuminori Tokunaga

    (Graduate School of Medicine, Osaka City University)

  • Hiroshi Kawasaki

    (Kihara Institute for Biological Research, Graduate School of Integrated Science, Yokohama City University, Kanagawa)

  • Kazuhiro Iwai

    (Graduate School of Medicine, Osaka City University)

  • Toshiaki Suzuki

    (Tokyo Metropolitan Institute of Medical Science
    CREST, Japan Science and Technology Corporation (JST))

  • Yukishige Ito

    (Synthetic Cellular Chemistry Laboratory, RIKEN, Wako)

  • Koji Matsuoka

    (Saitama University)

  • Minoru Yoshida

    (CREST, Japan Science and Technology Corporation (JST)
    Chemical Genetics Laboratory, RIKEN, Wako)

  • Keiji Tanaka

    (Tokyo Metropolitan Institute of Medical Science
    CREST, Japan Science and Technology Corporation (JST))

  • Tadashi Tai

    (Tokyo Metropolitan Institute of Medical Science)

Abstract

N-glycosylation of proteins in the endoplasmic reticulum (ER) has a central role in protein quality control1,2,3. Here we report that N-glycan serves as a signal for degradation by the Skp1–Cullin1–Fbx2–Roc1 (SCFFbx2) ubiquitin ligase complex. The F-box protein Fbx2 (ref. 4) binds specifically to proteins attached to N-linked high-mannose oligosaccharides and subsequently contributes to ubiquitination of N-glycosylated proteins. Pre-integrin β1 is a target of Fbx2; these two proteins interact in the cytosol after inhibition of the proteasome. In addition, expression of the mutant Fbx2ΔF, which lacks the F-box domain that is essential for forming the SCF complex, appreciably blocks degradation of typical substrates of the ER-associated degradation pathway5,6. Our results indicate that SCFFbx2 ubiquitinates N-glycosylated proteins that are translocated from the ER to the cytosol by the quality control mechanism.

Suggested Citation

  • Yukiko Yoshida & Tomoki Chiba & Fuminori Tokunaga & Hiroshi Kawasaki & Kazuhiro Iwai & Toshiaki Suzuki & Yukishige Ito & Koji Matsuoka & Minoru Yoshida & Keiji Tanaka & Tadashi Tai, 2002. "E3 ubiquitin ligase that recognizes sugar chains," Nature, Nature, vol. 418(6896), pages 438-442, July.
    • Handle: RePEc:nat:nature:v:418:y:2002:i:6896:d:10.1038_nature00890
    DOI: 10.1038/nature00890
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