Medical Journals

Similar Protein Phosphatases Control Starch Metabolism in Plants and Glycogen Metabolism in Mammals.

Authors:
  • Niittylä Totte
  • Comparot-Moss Sylviane
  • Lue Wei-Ling
  • Messerli Gaëlle
  • Trevisan Martine
  • Seymour Michael D J
  • Gatehouse John A
  • Villadsen Dorthe
  • Smith Steven M
  • Chen Jychian
  • Zeeman Samuel C
  • Smith Alison M

From: Department of Metabolic Biology, John Innes Centre, Norwich NR4 7UH, United Kingdom.

The Journal of biological chemistry

  • Publish Date: Apr 2006
  • ISSN: 0021-9258
  • Volume: 281
  • Issue: 17
  • Pages: 11815-8
  • Medium: Print
  • Language: English
  • Citation (JAMA): Niittylä Totte, Comparot-Moss Sylviane, Lue Wei-Ling, et al. Similar Protein Phosphatases Control Starch Metabolism in Plants and Glycogen Metabolism in Mammals.. J. Biol. Chem. Apr 2006;281:11815-8

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.

Mesh Headings (Keywords): Animals, Arabidopsis, Arabidopsis Proteins, Chloroplasts, Glucans, Glycogen, Humans, Mammals, Phosphoprotein Phosphatases, Phosphorylation, Plant Leaves, Starch


Check for Full Text / PubMed Unique Identifier (PMID): 16513634


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