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

Authors :
Totte Niittylä
Steven M. Smith
Samuel C. Zeeman
John A. Gatehouse
Michael D.J. Seymour
Sylviane Comparot-Moss
Jychian Chen
Alison M. Smith
Gaëlle Messerli
Dorthe Villadsen
Martine Trevisan
Wei-Ling Lue
Source :
The Journal of biological chemistry. 281(17)
Publication Year :
2006

Abstract

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.

Details

ISSN :
00219258
Volume :
281
Issue :
17
Database :
OpenAIRE
Journal :
The Journal of biological chemistry
Accession number :
edsair.doi.dedup.....4bd11f55a55b4797ec1bedf3d2f0fa34