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 | 2004 |
形態種別 | 研究論文 |
査読 | 査読あり |
標題 | Dynamics of Golgi Matrix Proteins after the Blockage of ER to Golgi Transport |
執筆形態 | その他 |
掲載誌名 | Journal of Biochemistry |
出版社・発行元 | JAPANESE BIOCHEMICAL SOC |
巻・号・頁 | 135(2),pp.201-216 |
著者・共著者 | Yoshimura, S.-I.,Yamamoto, A.,Misumi, Y.,Sohda, M.,Barr, F.A.,Fujii, G.,Shakoori, A.,Ohno, H.,Mihara, K.,Nakamura, N. |
概要 | When the ER to Golgi transport is blocked by a GTP-restricted mutant of Sar1p (H79G) in NRK-52E cells, most Golgi resident proteins are transported back into the ER. In contrast, the cis-Golgi matrix proteins GM130 and GRASP65 are retained in punctate cytoplasmic structures, namely Golgi remnants. Significant amounts of the medial-Golgi matrix proteins golgin-45, GRASP55 and giantin are retained in the Golgi remnants, but a fraction of these proteins relocates to the ER. Golgin-97, a candidate trans-Golgi net-work matrix protein, is retained in Golgi remnant-like structures, but mostly separated from GM130 and GRASP65. Interestingly, most Sec13p, a COPII component, congregates into larger cytoplasmic clusters soon after the microinjection of Sar1p(H79G), and these move to accumulate around the Golgi apparatus. Sec13p clusters remain associated with Golgi remnants after prolonged incubation. Electron microscopic analysis revealed that Golgi remnants are clusters of larger vesicles with smaller vesicles, many of which are coated. GM130 is mainly associated with larger vesicles and Sec13p with smaller coated vesicles. The Sec13p clusters disperse when p115 binding to the Golgi apparatus is inhibited. These results suggest that cis-Golgi matrix proteins resist retrograde transport flow and stay as true residents in Golgi remnants after the inhibition of ER to Golgi transport. |
DOI | 10.1093/jb/mvh024 |
ISSN | 0021-924X |
Put Code(ORCID) | 19809412 |