2002年7月
E3 ubiquitin ligase that recognizes sugar chains
NATURE
- 巻
- 418
- 号
- 6896
- 開始ページ
- 438
- 終了ページ
- 442
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1038/nature00890
- 出版者・発行元
- NATURE PUBLISHING GROUP
N-glycosylation of proteins in the endoplasmic reticulum (ER) has a central role in protein quality control(1-3). Here we report that N-glycan serves as a signal for degradation by the Skp1-Cullin1-Fbx2-Roc1 (SCF(Fbx2)) 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 beta1 is a target of Fbx2; these two proteins interact in the cytosol after inhibition of the proteasome. In addition, expression of the mutant Fbx2DeltaF, 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 pathway(5,6). Our results indicate that SCF(Fbx2) ubiquitinates N-glycosylated proteins that are translocated from the ER to the cytosol by the quality control mechanism.
- リンク情報
- ID情報
-
- DOI : 10.1038/nature00890
- ISSN : 0028-0836
- PubMed ID : 12140560
- Web of Science ID : WOS:000177009700043