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 2009
形態種別 研究論文
査読 査読あり
標題 Yip1A regulates the COPI-independent retrograde transport from the Golgi complex to the ER
執筆形態 その他
掲載誌名 Journal of Cell Science
出版社・発行元 COMPANY OF BIOLOGISTS LTD
巻・号・頁 122(13),pp.2218-2227
著者・共著者 Kano, F.,Yamauchi, S.,Yoshida, Y.,Watanabe-Takahashi, M.,Nishikawa, K.,Nakamura, N.,Murata, M.
概要 Yip1A, a mammalian homologue of yeast Yip1p, is a multispanning membrane protein that is considered to be involved in transport between the endoplasmic reticulum (ER) and the Golgi. However, the precise role of Yip1A in mammalian cells remains unclear. We show here that endogenous Yip1A is localized to the ER-Golgi intermediate compartment (ERGIC). Knockdown of Yip1A by RNAi did not induce morphological changes in the Golgi, ER, or ERGIC. By analyzing a number of intracellular transport pathways, we found that Yip1A knockdown delayed the transport of Shiga toxin from the Golgi to the ER, but did not affect the anterograde transport of VSVGts045. We also found that a recombinant protein that corresponded to the N-terminal domain of Yip1A inhibited the COPI-independent retrograde transport of GFP-tagged galactosyltransferase, GT-GFP, but not the COPI-dependent retrograde transport of p58/ERGIC53. Furthermore, we found that Yip1A knockdown resulted in the dissociation of Rab6 from the membranes. These results suggested that Yip1A has a role in COPI-independent retrograde transport from the Golgi to the ER and regulates the membrane recruitment of Rab6.
DOI 10.1242/jcs.043414
ISSN 0021-9533
Put Code(ORCID) 19809394