ArticleThe Plant cell2011
The phosphoglucan phosphatase like sex Four2 dephosphorylates starch at the C3-position in Arabidopsis.
Article in The Plant cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.
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Who cites it
66 citing papers in PubMed, 132 citations in OpenAlex.
- Solving the Insoluble: Regulation of α-Polyglucan Solubility and Functionality in Nature.Molecules (Basel, Switzerland) · 2026Review
- A structural perspective on α-glucan catabolism in oxygenic phototrophs.The Plant journal : for cell and molecular biology · 2026Review
- Covalently linked phosphate monoesters on alpha-polyglucans reduce substrate affinity of branching enzymes.Carbohydrate polymers · 2025Article
- Genome-wide identification of the AcBAM family in kiwifruit (Actinidia chinensis cv. Hongyang) and the expression profiling analysis of AcBAMs reveal their role in starch metabolism.BMC plant biology · 2025Article
- Target of rapamycin signaling regulates starch degradation via α-glucan water dikinase in a unicellular red alga.Plant physiology · 2025Article
- Branched oligosaccharides cause atypical starch granule initiation in Arabidopsis chloroplasts.Plant physiology · 2025Article
- Identification of Novel Inhibitors of Starch Excess 4 (SEX4).Life (Basel, Switzerland) · 2024Article
- Emerging Functions of Protein Tyrosine Phosphatases in Plants.International journal of molecular sciences · 2024Review
- Starch phosphorylation regulates starch granule morphological homogeneity in Arabidopsis thaliana.Plant physiology · 2024Article
- The LIKE SEX FOUR 1-malate dehydrogenase complex functions as a scaffold to recruit β-amylase to promote starch degradation.The Plant cell · 2023Article
- Gradual Analytics of Starch-Interacting Proteins Revealed the Involvement of Starch-Phosphorylating Enzymes during Synthesis of Storage Starch in Potato (Molecules (Basel, Switzerland) · 2023Article
- Starch degradation in the bean fruit pericarp is characterized by an increase in maltose metabolism.Physiologia plantarum · 2022Article
- A dominant mutation in β-AMYLASE1 disrupts nighttime control of starch degradation in Arabidopsis leaves.Plant physiology · 2022Article
- BETA-AMYLASE9 is a plastidial nonenzymatic regulator of leaf starch degradation.Plant physiology · 2022Article
- Article
- Proteomics and Post-Translational Modifications of Starch Biosynthesis-Related Proteins in Developing Seeds of Rice.International journal of molecular sciences · 2021Review
- ALTERED MERISTEM PROGRAM 1 promotes growth and biomass accumulation influencing guard cell aperture and photosynthetic efficiency in Arabidopsis.Protoplasma · 2020Article
- Accurate and sensitive quantitation of glucose and glucose phosphates derived from storage carbohydrates by mass spectrometry.Carbohydrate polymers · 2020Article
- Involvement of five catalytically active Arabidopsis β-amylases in leaf starch metabolism and plant growth.Plant direct · 2020Article
- Mutations in Glucan, Water Dikinase Affect Starch Degradation and Gametophore Development in the Moss Physcomitrella patens.Scientific reports · 2019Article
6 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 3 countries.
Funding
Abstract
Starch contains phosphate covalently bound to the C6-position (70 to 80% of total bound phosphate) and the C3-position (20 to 30%) of the glucosyl residues of the amylopectin fraction. In plants, the transient phosphorylation of starch renders the granule surface more accessible to glucan hydrolyzing enzymes and is required for proper starch degradation. Phosphate also confers desired properties to starch-derived pastes for industrial applications. In Arabidopsis thaliana, the removal of phosphate by the glucan phosphatase Starch Excess4 (SEX4) is essential for starch breakdown. We identified a homolog of SEX4, LSF2 (Like Sex Four2), as a novel enzyme involved in starch metabolism in Arabidopsis chloroplasts. Unlike SEX4, LSF2 does not have a carbohydrate binding module. Nevertheless, it binds to starch and specifically hydrolyzes phosphate from the C3-position. As a consequence, lsf2 mutant starch has elevated levels of C3-bound phosphate. SEX4 can release phosphate from both the C6- and the C3-positions, resulting in partial functional overlap with LSF2. However, compared with sex4 single mutants, the lsf2 sex4 double mutants have a more severe starch-excess phenotype, impaired growth, and a further change in the proportion of C3- and C6-bound phosphate. These findings significantly advance our understanding of the metabolism of phosphate in starch and provide innovative options for tailoring novel starches with improved functionality for industry.
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