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PMID:16513634
| Citation |
Niittylä, T, Comparot-Moss, S, Lue, WL, Messerli, G, Trevisan, M, Seymour, MD, Gatehouse, JA, Villadsen, D, Smith, SM, Chen, J, Zeeman, SC and Smith, AM (2006) Similar protein phosphatases control starch metabolism in plants and glycogen metabolism in mammals. J. Biol. Chem. 281:11815-8 |
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| 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. |
| Links |
PubMed Online version:10.1074/jbc.M600519200 |
| Keywords |
Animals; Arabidopsis/growth & development; Arabidopsis/metabolism; Arabidopsis Proteins/metabolism; Chloroplasts/chemistry; Glucans/metabolism; Glycogen/metabolism; Humans; Mammals/metabolism; Phosphoprotein Phosphatases/metabolism; Phosphorylation; Plant Leaves/chemistry; Plant Leaves/cytology; Starch/metabolism |
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Significance
Annotations
| Gene product | Qualifier | GO ID | GO term name | Evidence Code | with/from | Aspect | Notes | Status |
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See also
References
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