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

被引：119

作者：

Niittylä, T

Comparot-Moss, S

Lue, WL

Messerli, G

Trevisan, M

Seymour, MDJ

Gatehouse, JA

Villadsen, D

Smith, SM

Chen, JC

Zeeman, SC ^{[1
]}

Alison, MS

机构：

[1] ETH, Inst Plant Sci, CH-8092 Zurich, Switzerland

[2] John Innes Ctr Plant Sci Res, Dept Metab Biol, Norwich NR4 7UH, Norfolk, England

[3] Acad Sinica, Inst Mol Biol, Taipei 115, Taiwan

[4] Univ Bern, Inst Plant Sci, CH-3013 Bern, Switzerland

[5] Univ Durham, Sch Biol & Biomed Sci, Durham DH1 3LE, England

[6] Univ Edinburgh, Inst Mol Plant Sci, Edinburgh EH9 3JH, Midlothian, Scotland

[7] Univ Western Australia, Australian Res Council Ctr Excellence Plant Energ, Crawley, WA 6009, Australia

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2006年 / 281卷 / 17期

基金：

英国生物技术与生命科学研究理事会;

关键词：

D O I：

10.1074/jbc.M600519200

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：11815 / 11818

页数：4

共 37 条

[1] A novel isoform of glucan, water dikinase phosphorylates pre-phosphorylated α-glucans and is involved in starch degradation in Arabidopsis [J].