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First published online 9 June 2009
doi: 10.1242/jcs.043414
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Research Article |

1 Department of Life Sciences, Graduate School of Arts and Sciences, The University of Tokyo, Komaba 3-8-1, Meguro-ku, Tokyo 153-8902, Japan
2 PRESTO, Japan Science and Technology Agent, 4-1-8 Honcho Kawaguchi, Saitama, Japan
3 Division of Life Sciences, Graduate School of Natural Science and Technology and Faculty of Pharmaceutical Sciences, Kanazawa University, Kakuma, Kanazawa 920-1192, Japan
4 Faculty of Life and Medical Science, Doshisha University, Kyoto 610-0394, Japan
Author for correspondence (e-mail: mmurata{at}bio.c.u-tokyo.ac.jp)
Accepted 19 March 2009
Yip1A, a mammalian homologue of yeast Yip1p, is a multi-spanning 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.
Key words: Retrograde transport, Yip1A, Golgi complex, Endoplasmic reticulum
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