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
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