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 | 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 |