Journal
TRENDS IN PLANT SCIENCE
Volume 19, Issue 7, Pages 471-478Publisher
CELL PRESS
DOI: 10.1016/j.tplants.2014.01.008
Keywords
starch degradation; phosphoglucan phosphatase; phosphorylation; redox; dual-specificity phosphatase
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Funding
- Natural Sciences and Engineering Research Council of Canada
- Alberta Innovates Technology Futures
- ETH Zurich
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Phosphoglucan phosphatases are novel enzymes that remove phosphates from complex carbohydrates. In plants, these proteins are vital components in the remobilization of leaf starch at night. Breakdown of starch is initiated through reversible glucan phosphorylation to disrupt the semi-crystalline starch structure at the granule surface. The phosphoglucan phosphatases starch excess 4 (SEX4) and like-SEX4 2 (LSF2) dephosphorylate glucans to provide access for amylases that release maltose and glucose from starch. Another phosphatase, LSF1, is a putative inactive scaffold protein that may act as regulator of starch degradative enzymes at the granule surface. Absence of these phosphatases disrupts starch breakdown, resulting in plants accumulating excess starch. Here, we describe recent advances in understanding the biochemical and structural properties of each of these starch phosphatases.
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