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Originally published In Press as doi:10.1074/jbc.M600519200 on March 2, 2006

J. Biol. Chem., Vol. 281, Issue 17, 11815-11818, April 28, 2006
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Similar Protein Phosphatases Control Starch Metabolism in Plants and Glycogen Metabolism in Mammals*Formula

Totte Niittylä{ddagger}12, Sylviane Comparot-Moss{ddagger}1, Wei-Ling Lue§, Gaëlle Messerli, Martine Trevisan||3, Michael D. J. Seymour**, John A. Gatehouse**, Dorthe Villadsen{ddagger}{ddagger}, Steven M. Smith§§, Jychian Chen§, Samuel C. Zeeman4, and Alison M. Smith{ddagger}

From the {ddagger}Department of Metabolic Biology, John Innes Centre, Norwich NR4 7UH, United Kingdom, §Institute of Molecular Biology, Academia Sinica, Taipei 115, Taiwan, Institute of Plant Sciences, ETH Zurich, CH-8092 Zurich, Switzerland, ||Institute of Plant Sciences, University of Bern, Altenbergrain 21, CH-3013 Bern, Switzerland, **School of Biological and Biomedical Sciences, Durham University, Durham DH1 3LE, United Kingdom, {ddagger}{ddagger}Institute of Molecular Plant Sciences, University of Edinburgh, Edinburgh EH9 3JH, United Kingdom, and §§Australian Research Council Centre of Excellence in Plant Energy Biology, University of Western Australia, Crawley WA 6009, Australia

We report that protein phosphorylation is involved in the control of starch metabolism in Arabidopsis leaves at night. sex4 (starch excess 4) mutants, which have strongly reduced rates of starch metabolism, lack a protein predicted to be a dual specificity protein phosphatase. We have shown that this protein is chloroplastic and can bind to glucans and have presented evidence that it acts to regulate the initial steps of starch degradation at the granule surface. Remarkably, the most closely related protein to SEX4 outside the plant kingdom is laforin, a glucan-binding protein phosphatase required for the metabolism of the mammalian storage carbohydrate glycogen and implicated in a severe form of epilepsy (Lafora disease) in humans.

Received for publication, January 18, 2006 , and in revised form, February 27, 2006.

* This work was supported by funding from the Biotechnology and Biological Sciences Research Council of the United Kingdom (to A. M. S. and J. A. G.), from the Swiss National Science Foundation (National Centre of Competence in Research-Plant Survival) and the Roche Research Foundation (to S. C. Z.), and from the National Science Council, Taiwan (to J. C.). 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.

Formula The on-line version of this article (available at http://www.jbc.org) contains supplemental material.

1 These authors contributed equally to this work.

2 Present address: Carnegie Institution, Stanford, CA 94305-1297.

3 Present address: Ctr. for Integrative Genomics, University of Lausanne, CH-1015, Lausanne, Switzerland.

4 To whom correspondence should be addressed: Institute of Plant Sciences, ETH Zurich, CH-8092 Zurich, Switzerland. Tel.: 41-44-632-8275; Fax: 41-44-632-1044; E-mail szeeman{at}ethz.ch.


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