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 1995
形態種別 研究論文
査読 査読あり
標題 Characterization of a cis-Golgi matrix protein, GM130
執筆形態 その他
掲載誌名 Journal of Cell Biology
出版社・発行元 ROCKEFELLER UNIV PRESS
巻・号・頁 131(6 II),pp.1715-1726
著者・共著者 Nakamura, N.,Rabouille, C.,Watson, R.,Nilsson, T.,Hui, N.,Slusarewicz, P.,Kreis, T.E.,Warren, G.
概要 Antisera raised to a detergent- and salt-resistant matrix fraction from rat liver Golgi stacks were used to screen an expression library from rat liver cDNA. A full-length clone was obtained encoding a protein of 130 kD (termed GM130), the COOH-terminal domain of which was highly homologous to a Golgi human auto-antigen, golgin-95 (Fritzler et al., 1993). Biochemical data showed that GM130 is a peripheral cytoplasmic protein that is tightly bound to Golgi membranes and part of a larger oligomeric complex. Predictions from the protein sequence suggest that GM130 is an extended rod-like protein with coiled-coil domains, Immunofluorescence microscopy showed partial over-lap with medial- and trans-Golgi markers but almost complete overlap with the cis-Golgi network (CGN) marker, syntaxin5, Immunoelectron microscopy confirmed this location showing that most of the GM130 was located in the CGN and in one or two cisternae on the cis-side of the Golgi stack. GM130 was not re-distributed to the ER in the presence of brefeldin A but maintained its overlap with syntaxin5 and a partial overlap with the ER-Golgi intermediate compartment marker, p53, Together these results suggest that GM130 is part of a cis-Golgi matrix and has a role in maintaining cis-Golgi structure.
DOI 10.1083/jcb.131.6.1715
ISSN 0021-9525/1540-8140
Put Code(ORCID) 19809428