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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 | 2001 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | Identification and Characterization of a Novel Golgi Protein, GCP60, that Interacts with the Integral Membrane Protein Giantin |
| 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 | 276(48),pp.45298-45306 |
| 著者・共著者 | Sohda, M.,Misumi, Y.,Yamamoto, A.,Yano, A.,Nakamura, N.,Ikehara, Y. |
| 概要 | We demonstrated previously that the integral membrane protein giantin has the Golgi localization signal at the COOH-terminal cytoplasmic domain (Misumi, Y., Sohda, M., Tashiro, A., Sato, H., and Ikehara, Y. (2001) J Biol. Chem. 276, 6867-6873). In the present study, using this domain as bait in the yeast two-hybrid screening system, we identified a novel protein interacting with giantin. The 3.6-kilobase mRNA encoding a 528-amino acid protein of 60 kDa designated GCP60 was ubiquitously expressed and was especially abundant in the testis and ovary. Immunofluorescence and immunoelectron microscopy confirmed that GCP60 was co-localized with giantin in the Golgi complex. GCP60 was found to be a peripheral protein associated with the Golgi membrane, where a COOH-terminal domain of GCP60 interacts with the COOH-terminal cytoplasmic domain of giantin. Overexpression of the COON-terminal domain of GCP60 caused disassembly of the Golgi structure and blocked protein transport from the endoplasmic reticulum to the Golgi. Taken together, these results suggest that GCP60 is involved in the maintenance of the Golgi structure by interacting with giantin, affecting protein transport between the endoplasmic reticulum and the Golgi. |
| DOI | 10.1074/jbc.M108961200 |
| ISSN | 0021-9258 |
| Put Code(ORCID) | 19809418 |