E3 ubiquitin ligase that recognizes sugar chains

Yukiko Yoshida, Tomoki Chiba, Fuminori Tokunaga, Hiroshi Kawasaki, Kazuhiro Iwai, Toshiaki Suzuki, Yukishige Ito, Koji Matsuoka, Minoru Yoshida, Keiji Tanaka () and Tadashi Tai ()
Additional contact information
Yukiko Yoshida: Tokyo Metropolitan Institute of Medical Science
Tomoki Chiba: Tokyo Metropolitan Institute of Medical Science
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
Yukishige Ito: Synthetic Cellular Chemistry Laboratory, RIKEN, Wako
Koji Matsuoka: Saitama University
Minoru Yoshida: CREST, Japan Science and Technology Corporation (JST)
Keiji Tanaka: Tokyo Metropolitan Institute of Medical Science
Tadashi Tai: Tokyo Metropolitan Institute of Medical Science

Nature, 2002, vol. 418, issue 6896, 438-442

Abstract: 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.

Date: 2002
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DOI: 10.1038/nature00890

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