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E3 ubiquitin ligase that recognizes sugar chains
https://sucra.repo.nii.ac.jp/records/13316
https://sucra.repo.nii.ac.jp/records/133169a43f03e-e4cf-4a65-9029-c33074647fbf
名前 / ファイル | ライセンス | アクション |
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A1002757.pdf (1.6 MB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2008-08-19 | |||||
タイトル | ||||||
タイトル | E3 ubiquitin ligase that recognizes sugar chains | |||||
言語 | ||||||
言語 | eng | |||||
資源タイプ | ||||||
資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
資源タイプ | journal article | |||||
著者 |
Yoshida, Y
× Yoshida, Y× Chiba, T× Tokunaga, F× Kawasaki, H× Iwai, K× Suzuki, T× Ito, Y× Matsuoka, K× 吉田, 稔 |
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著者 ローマ字 | ||||||
Yoshida, Y | ||||||
著者 ローマ字 | ||||||
Chiba, T | ||||||
著者 ローマ字 | ||||||
Tokunaga, F | ||||||
著者 ローマ字 | ||||||
Kawasaki, H | ||||||
著者 ローマ字 | ||||||
Iwai, K | ||||||
著者 ローマ字 | ||||||
Suzuki, T | ||||||
著者 ローマ字 | ||||||
Ito, Y | ||||||
著者 ローマ字 | ||||||
Matsuoka, K | ||||||
著者 ローマ字 | ||||||
Yoshida, Minoru | ||||||
著者 所属 | ||||||
著者 所属 | ||||||
著者 所属 | ||||||
著者 所属 | ||||||
著者 所属 | ||||||
著者 所属 | ||||||
著者 所属 | ||||||
著者 所属 | ||||||
著者 所属 | ||||||
埼玉大学大学院理工学研究科生命科学部門 | ||||||
著者 所属(別言語) | ||||||
著者 所属(別言語) | ||||||
著者 所属(別言語) | ||||||
著者 所属(別言語) | ||||||
著者 所属(別言語) | ||||||
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著者 所属(別言語) | ||||||
著者 所属(別言語) | ||||||
著者 所属(別言語) | ||||||
Graduate School of Science and Engineering, Saitama University | ||||||
書誌情報 |
NATURE 巻 418, 号 6896, p. 438-442, 発行日 2002 |
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年月次 | ||||||
2002-7 | ||||||
出版者名 | ||||||
出版者 | Nature Publishing Group | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 00280836 | |||||
DOI | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | DOI | |||||
関連識別子 | info:doi/10.1038/nature00890 | |||||
抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | 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 (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 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 SCFFbx2 ubiquitinates N-glycosylated proteins that are translocated from the ER to the cytosol by the quality control mechanism. | |||||
版 | ||||||
[著者版] | ||||||
著者版フラグ | ||||||
出版タイプ | AM | |||||
出版タイプResource | http://purl.org/coar/version/c_ab4af688f83e57aa | |||||
資源タイプ | ||||||
内容記述タイプ | Other | |||||
内容記述 | text | |||||
フォーマット | ||||||
内容記述タイプ | Other | |||||
内容記述 | application/pdf | |||||
作成日 | ||||||
日付 | 2008-08-20 | |||||
日付タイプ | Created | |||||
アイテムID | ||||||
A1002757 |