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Similar protein phosphatases control starch metabolism in plant and glycogen metabolism in mammals

Citation

Niittyla, T and Comparot-Moss, S and Lue, W-L and Messerli, G and Trevisan, M and Seymour, MDJ and Gatehouse, JA and Villadsen, D and Smith, SM and Chen, J and Zeeman, SC and Smith, AM, Similar protein phosphatases control starch metabolism in plant and glycogen metabolism in mammals, Journal of Biological Chemistry, 281, (17) pp. 11815-11818. ISSN 0021-9258 (2006) [Refereed Article]

Copyright Statement

2006 by The American Society for Biochemistry and Molecular Biology

DOI: doi:10.1074/jbc.M600519200

Abstract

Wereport 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, themostclosely related protein to SEX4 outside the plant kingdom is laforin, a glucanbinding protein phosphatase required for the metabolism of the mammalian storage carbohydrate glycogen and implicated in a severe form of epilepsy (Lafora disease) in humans.

Item Details

Item Type:Refereed Article
Keywords:starch metabolism, protein phosphorylation, arabidopsis thaliana
Research Division:Biological Sciences
Research Group:Plant Biology
Research Field:Plant Physiology
Objective Division:Expanding Knowledge
Objective Group:Expanding Knowledge
Objective Field:Expanding Knowledge in the Biological Sciences
Author:Smith, SM (Professor Steven Smith)
ID Code:101517
Year Published:2006
Web of Science® Times Cited:104
Deposited By:Plant Science
Deposited On:2015-06-25
Last Modified:2015-09-25
Downloads:0

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