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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 | 2011 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | Characterization of YIPF3 and YIPF4, cis-golgi localizing yip domain family proteins |
| 執筆形態 | その他 |
| 掲載誌名 | Cell Structure and Function |
| 出版社・発行元 | JAPAN SOC CELL BIOLOGY |
| 巻・号・頁 | 36(2),pp.171-185 |
| 著者・共著者 | Tanimoto, K.,Suzuki, K.,Jokitalo, E.,Sakai, N.,Sakaguchi, T.,Tamura, D.,Fujii, G.,Aoki, K.,Takada, S.,Ishida, R.,Tanabe, M.,Itoh, H.,Yoneda, Y.,Sohda, M.,Misumi, Y.,Nakamura, N. |
| 概要 | The Yip1 domain family (YIPF) proteins are homologues of yeast Yip1p and Yif1p, which are proposed to function in ER to Golgi transport. Here, we report the characterization of YIPF3 and YIPF4, homologues of human Yif1p and Yip1p, respectively. Immunofluorescence and immuno-electron microscopy showed that both YIPF3 and YIPF4 are clearly concentrated in the cis-Golgi. While YIPF4 was detected as a single mobility form consistent with its predicted molecular weight, three different mobility forms of YIPF3 were detected by western blotting. Biochemical and immunofluorescence experiments strongly indicated that YIPF3 is synthesized in the ER as a N-glycosylated form (40 kDa), is then O-glycosylated in the Golgi apparatus to become a lower mobility form (46 kDa) and finally becomes a higher mobility form cleaved at its C-terminal luminal domain (36 kDa). YIPF3 and YIPF4 form a complex in the Golgi apparatus, and this was suggested to be important for their proper localization and function. The knockdown of YIPF3 or YIPF4 in HeLa cells induced fragmentation of the Golgi apparatus, suggesting their involvement in the maintenance of the Golgi structure. |
| DOI | 10.1247/csf.11002 |
| ISSN | 0386-7196/1347-3700 |
| Put Code(ORCID) | 19809389 |