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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 | 2015 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | GM130 is a parallel tetramer with a flexible rod-like structure and N-terminally open (Y-shaped) and closed (I-shaped) conformations |
| 執筆形態 | その他 |
| 掲載誌名 | FEBS Journal |
| 出版社・発行元 | WILEY-BLACKWELL |
| 巻・号・頁 | 282(11),pp.2232-2244 |
| 著者・共著者 | Ishida, R.,Yamamoto, A.,Nakayama, K.,Sohda, M.,Misumi, Y.,Yasunaga, T.,Nakamura, N. |
| 概要 | GM130 is a cytoplasmic peripheral membrane protein localized on the cis side of the Golgi apparatus. GM130 is proposed to function as a membrane skeleton, maintaining the structure of the Golgi apparatus, and as a vesicle tether that facilitates vesicle fusion to the Golgi membrane. More than 60% of the GM130 molecule is believed to exist as coiled-coil structures with a probability above 90%, based on its primary amino acid sequence. The predicted coiled-coil region was similar to that of yeast Uso1p and its mammalian homolog, p115, both of which form coiled-coil homodimers. Therefore, GM130 has long been thought to form a homodimer with a rod-like shape. However, our biochemical and electron microscopical analyses revealed that GM130 is a parallel homotetramer with a flexible rod-like structure with I- and Y-shaped conformations. The structure of the N-terminal region may interchange between an open conformation (branched or Y-shaped) and a closed conformation (non-branched or I-shaped), possibly with the help of interacting molecules. This conformational change may alter the oligomeric state of the GM130 molecules and the function of GM130 in the vesicle tethering and the maintenance of the Golgi structure. |
| DOI | 10.1111/febs.13271 |
| ISSN | 1742-464X/1742-4658 |
| Put Code(ORCID) | 19809384 |