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

J. Biol. Chem., Vol. 280, Issue 24, 23048-23056, June 17, 2005

This Article Full Text Full Text (PDF) All Versions of this Article: 280/24/23048    most recent M502442200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Yoshimura, S.-i. Articles by Nakamura, N. Search for Related Content PubMed PubMed Citation Articles by Yoshimura, S.-i. Articles by Nakamura, N. Social Bookmarking                      What's this?

Convergence of Cell Cycle Regulation and Growth Factor Signals on GRASP65^*

Shin-ichiro Yoshimura, Katsuji Yoshioka¶, Francis A. Barr||**, Martin Lowe, Kazuhisa Nakayama, Shoji Ohkuma, and Nobuhiro Nakamura¶¶

From the Division of Life Sciences, Graduate School of Natural Science and Technology, Kanazawa University, Kakuma, Kanazawa 920-1192, Japan, the Japan Society for the Promotion of Science, 6 Ichiban-cho, Chiyoda, Tokyo 102-8471, Japan, the ^¶Division of Cell Cycle Regulation, Cancer Research Institute, Kanazawa University, 13-1 Takaramachi, Kanazawa 920-0934, Japan, the ^||Department of Cell Biology, Max-Planck-Institute of Biochemistry, Am Klopferspitz 18, Martinsried D-82152, Germany, the School of Biological Sciences, University of Manchester, The Michael Smith Building, Oxford Road, Manchester M13 9PT, United Kingdom, and the Department of Physiological Chemistry, Graduate School of Pharmaceutical Sciences, Kyoto University, Kyoto 606-8501, Japan

Together with other Golgi matrix components, GRASP65 contributes to the stacking of Golgi cisternae in interphase cells. During mitosis, GRASP65 is heavily phosphorylated, and in turn, cisternal stacking is inhibited leading to the breakdown of the Golgi apparatus. Here we show that GRASP65 is phosphorylated on serine 277 in interphase cells, and this is strongly enhanced in response to the addition of serum or epidermal growth factor. This is directly mediated by ERK suggesting that GRASP65 has some role in growth factor signal transduction. Phosphorylation of Ser-277 is also dramatically increased during mitosis, however this is mediated by Cdk1 and not by ERK. The microinjection of recombinant GRASP65 without N-terminal myristoylation or a peptide fragment containing Ser-277 into the cytosol of normal rat kidney cells inhibits passage through mitosis. This effect is abolished when Ser-277 is replaced with alanine suggesting the phosphorylation of Ser-277 plays an important role in cell cycle regulation. The convergence of cell cycle regulation and growth factor signals on GRASP65 Ser-277 suggests that GRASP65 may function as a signal integrator controlling the cell growth.

Received for publication, March 4, 2005 , and in revised form, April 13, 2005.

^* This work was supported in part by a Grant-in-Aid for Scientific Research (15570156), Grants-in-Aid for Scientific Research on Priority Areas (15032216 and 16044218) from the Ministry of Education, Culture, Sports, Science and Technology of Japan, and a special research project grant from Kanazawa University (2001, 2002, and 2003) (to N. N.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^** Supported by the Max-Planck Society.

^¶¶ To whom correspondence should be addressed: Tel./Fax: 81-76-234-4466; E-mail: osaru3{at}kenroku.kanazawa-u.ac.jp.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				D. Sengupta, S. Truschel, C. Bachert, and A. D. Linstedt Organelle tethering by a homotypic PDZ interaction underlies formation of the Golgi membrane network J. Cell Biol., July 6, 2009; (2009) jcb.200902110v1. [Abstract] [Full Text] [PDF]

				B. Bisel, Y. Wang, J.-H. Wei, Y. Xiang, D. Tang, M. Miron-Mendoza, S.-i. Yoshimura, N. Nakamura, and J. Seemann ERK regulates Golgi and centrosome orientation towards the leading edge through GRASP65 J. Cell Biol., September 8, 2008; 182(5): 837 - 843. [Abstract] [Full Text] [PDF]

				J. M. Duran, M. Kinseth, C. Bossard, D. W. Rose, R. Polishchuk, C. C. Wu, J. Yates, T. Zimmerman, and V. Malhotra The Role of GRASP55 in Golgi Fragmentation and Entry of Cells into Mitosis Mol. Biol. Cell, June 1, 2008; 19(6): 2579 - 2587. [Abstract] [Full Text] [PDF]

				T. N. Feinstein and A. D. Linstedt Mitogen-activated Protein Kinase Kinase 1-dependent Golgi Unlinking Occurs in G2 Phase and Promotes the G2/M Cell Cycle Transition Mol. Biol. Cell, February 1, 2007; 18(2): 594 - 604. [Abstract] [Full Text] [PDF]

				K. Arasaki, M. Taniguchi, K. Tani, and M. Tagaya RINT-1 Regulates the Localization and Entry of ZW10 to the Syntaxin 18 Complex Mol. Biol. Cell, June 1, 2006; 17(6): 2780 - 2788. [Abstract] [Full Text] [PDF]

				H. H. Ho, C. Y. He, C. L. de Graffenried, L. J. Murrells, and G. Warren Ordered assembly of the duplicating Golgi in Trypanosoma brucei PNAS, May 16, 2006; 103(20): 7676 - 7681. [Abstract] [Full Text] [PDF]

				V. Kondylis, K. M. Spoorendonk, and C. Rabouille dGRASP Localization and Function in the Early Exocytic Pathway in Drosophila S2 Cells Mol. Biol. Cell, September 1, 2005; 16(9): 4061 - 4072. [Abstract] [Full Text] [PDF]