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ナカムラ ノブヒロ
NAKAMURA NOBUHIRO
中村 暢宏 所属 京都産業大学 生命科学部 先端生命科学科 職種 教授 |
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| 言語種別 | 英語 |
| 発行・発表の年月 | 2000 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | A di-leucine signal in the ubiquitin moiety: Possible involvement in ubiqutination-mediated endocytosis |
| 執筆形態 | その他 |
| 掲載誌名 | Journal of Biological Chemistry |
| 出版社・発行元 | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC |
| 巻・号・頁 | 275(34),pp.26213-26219 |
| 著者・共著者 | Nakatsu, F.,Sakuma, M.,Matsuo, Y.,Arase, H.,Yamasaki, S.,Nakamura, N.,Saito, T.,Ohno, H. |
| 概要 | Some plasma membrane receptors in yeast are known to be internalized and degraded in lysosomes up on ligand-dependent ubiquitination. However, the role of ubiquitination in endocytosis and lysosomal degradation in higher eukaryotes has been controversial. In order to directly assess this question, we investigated the fate of chimeric molecules in which ubiquitin moiety was fused in-frame to the cytoplasmic region of membrane proteins, The chimeric proteins with the wild-type ubiquitin were endocytosed and delivered to lysosomes efficiently. Mutant ubiquitin with lysine-to-arginine substitution could still mediate endocytosis, suggesting that polyubiquitination is not required for the endocytosis. We next searched for the existence of an endocytosis signal(s) in the ubiquitin moiety, and identified a di-leucine signal, Leu(43)-Ile(44). The Leu(43)-Ile(44) sequence mediated endocytosis and lysosomal sorting in a Leu(43)-dependent manner. These results suggest that the di-leucine signal in ubiquitin can be involved in ubiquitination-mediated endocytosis and lysosomal targeting of membrane proteins. |
| DOI | 10.1074/jbc.M907720199 |
| ISSN | 0021-9258 |
| Put Code(ORCID) | 19809419 |