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A more recent version of this article appeared on September 1, 2004
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Submitted on November 17, 2003
Accepted on June 30, 2004
, 
*Department of Life Sciences, Graduate School of Arts and Sciences, The University of Tokyo, Tokyo 153-8902, Japan; Cambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 2XY, United Kingdom; and PRESTO, Japan Science and Technology Corporation, Japan
Monitoring Editor: Benjamin Glick
We observed the disassembly of ER exit sites (ERES) by confocal microscopy during mitosis in CHO cells using Yip1A fused to GFP (green fluorescence protein) as a transmembrane marker of ERES. Photobleaching experiments revealed that Yip1A-GFP, which was restricted to the ERES during interphase, diffused throughout the ER network during mitosis. Next, we reconstituted mitotic disassembly of Yip1A-GFP labeled ERES in streptolysin O-permeabilized CHO cells using mitotic L5178Y cytosol. Using the ERES disassembly assay and the anterograde transport assay of GFP-tagged VSVGts045, we demonstrated that the phosphorylation of p47 by Cdc2 kinase regulates the disassembly of ERES and results in the specific inhibition of ER-to-Golgi transport during mitosis.
Corresponding author.
E-mail: mmurata{at}bio.c.u-tokyo.ac.jp
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