HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE ADVANCED SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kano, F. Articles by Murata, M. Search for Related Content PubMed PubMed Citation Articles by Kano, F. Articles by Murata, M.

¹ Department of Life Sciences, Graduate School of Arts and Sciences, University of Tokyo, Tokyo 153-8902, Japan
² Cambridge Institute for Medical Research, University of Cambridge, Cambridge CB2 2XY, UK
³ PRESTO, Japan Science and Technology Corporation, Japan
⁴ Department of Cell Biology, Nagahama Institute of Bio-Science and Technology, Nagahama, Shiga 526-0829, Japan
⁵ Department of Molecular and Cellular Biology, Institute for Frontier Medical Sciences, Kyoto University, Kyoto 606-8507, Japan

The endoplasmic reticulum (ER) has a characteristic complex polygonal structure with hallmark three-way junctions in many types of cells. To investigate the mechanisms responsible for maintaining the ER network, we established ER disassembly and reassembly assays in semi-intact Chinese hamster ovary (CHO) cells that constitutively expressed heat shock protein-47 fused to the green fluorescent protein (GFP-HSP47) as an ER marker (the cells are referred to as CHO-HSP cells). Using these assays, we found that maintenance of the ER network required cytosol and adenosine triphosphate/guanosine 5'-triphosphate (ATP/GTP) hydrolysis, but not actin filaments or microtubules. We also showed that the ER network was disrupted upon addition of either N-ethylmaleimide-treated cytosol after washing semi-intact cells with high salt solution or mitotic cytosol in nocodazole-treated semi-intact CHO-HSP cells. The disrupted ER network induced by mitotic cytosol was reformed by the addition of interphase cytosol. In addition, we found that p47, a cofactor of p97, was essential for the maintenance of the ER network, and that phosphorylation of p47 by cdc2 kinase resulted in ER network disruption by mitotic cytosol. Taken together, these results imply that the maintenance of the ER network requires a membrane fusion process mediated by p97/p47, and that cell cycle-dependent morphological changes of the ER network are regulated through phosphorylation/dephosphorylation of p47.

^* Correspondence: E-mail: mmurata{at}bio.c.u-tokyo.ac.jp

This article has been cited by other articles:

				H. Nakajima, S. Yonemura, M. Murata, N. Nakamura, H. Piwnica-Worms, and E. Nishida Myt1 protein kinase is essential for Golgi and ER assembly during mitotic exit J. Cell Biol., April 3, 2008; 181(1): 89 - 103. [Abstract] [Full Text] [PDF]

				J. G. Goetz, H. Genty, P. St-Pierre, T. Dang, B. Joshi, R. Sauve, W. Vogl, and I. R. Nabi Reversible interactions between smooth domains of the endoplasmic reticulum and mitochondria are regulated by physiological cytosolic Ca2+ levels J. Cell Sci., October 15, 2007; 120(20): 3553 - 3564. [Abstract] [Full Text] [PDF]

				M. A. Davis, D. Hinerfeld, S. Joseph, Y.-H. Hui, N. H. Huang, J. Leszyk, J. Rutherford-Bethard, and S. W. Tam Proteomic Analysis of Rat Liver Phosphoproteins after Treatment with Protein Kinase Inhibitor H89 (N-(2-[p-Bromocinnamylamino-]ethyl)-5-isoquinolinesulfonamide) J. Pharmacol. Exp. Ther., August 1, 2006; 318(2): 589 - 595. [Abstract] [Full Text] [PDF]

				F. Kano, H. Kondo, A. Yamamoto, Y. Kaneko, K. Uchiyama, N. Hosokawa, K. Nagata, and M. Murata NSF/SNAPs and p97/p47/VCIP135 are sequentially required for cell cycle-dependent reformation of the ER network Genes Cells, October 1, 2005; 10(10): 989 - 999. [Abstract] [Full Text] [PDF]