University of Tasmania
Browse

File(s) under permanent embargo

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

journal contribution
posted on 2023-05-18, 11:22 authored by Niittyla, T, Comparot-Moss, S, Lue, W-L, Messerli, G, Trevisan, M, Seymour, MDJ, Gatehouse, JA, Villadsen, D, Steven SmithSteven Smith, Chen, J, Zeeman, SC, Smith, AM
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.

History

Publication title

Journal of Biological Chemistry

Volume

281

Issue

17

Pagination

11815-11818

ISSN

0021-9258

Department/School

School of Natural Sciences

Publisher

Amer Soc Biochemistry Molecular Biology Inc

Place of publication

9650 Rockville Pike, Bethesda, USA, Md, 20814-3996

Rights statement

© 2006 by The American Society for Biochemistry and Molecular Biology

Repository Status

  • Restricted

Socio-economic Objectives

Expanding knowledge in the biological sciences

Usage metrics

    University Of Tasmania

    Exports

    RefWorks
    BibTeX
    Ref. manager
    Endnote
    DataCite
    NLM
    DC