ArticleThe Journal of biological chemistry2015
Mechanistic Insights into Glucan Phosphatase Activity against Polyglucan Substrates.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 32 citations in OpenAlex.
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- Article
- Generation and characterization of a laforin nanobody inhibitor.Clinical biochemistry · 2021Article
- Central Nervous System Delivery and Biodistribution Analysis of an Antibody-Enzyme Fusion for the Treatment of Lafora Disease.Molecular pharmaceutics · 2019Article
- LIKE SEX4 1 Acts as a β-Amylase-Binding Scaffold on Starch Granules during Starch Degradation.The Plant cell · 2019Article
- Brain Glycogen Structure and Its Associated Proteins: Past, Present and Future.Advances in neurobiology · 2019Review
- Oligomerization and carbohydrate binding of glucan phosphatases.Analytical biochemistry · 2018Article
- A novel EPM2A mutation yields a slow progression form of Lafora disease.Epilepsy research · 2018Article
- Lafora disease offers a unique window into neuronal glycogen metabolism.The Journal of biological chemistry · 2018Review
- Repression ofFrontiers in plant science · 2018Article
- Protein Kinases and Phosphatases of the Plastid and Their Potential Role in Starch Metabolism.Frontiers in plant science · 2018Review
- Identification and analysis of OsttaDSP, a phosphoglucan phosphatase from Ostreococcus tauri.PloS one · 2018Article
- Structural biology of glucan phosphatases from humans to plants.Current opinion in structural biology · 2016Review
- Unique carbohydrate binding platforms employed by the glucan phosphatases.Cellular and molecular life sciences : CMLS · 2016Review
- Structural mechanisms of plant glucan phosphatases in starch metabolism.The FEBS journal · 2016Review
- The LIKE SEX FOUR2 regulates root development by modulating reactive oxygen species homeostasis in Arabidopsis.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Glucan phosphatases are central to the regulation of starch and glycogen metabolism. Plants contain two known glucan phosphatases, Starch EXcess4 (SEX4) and Like Sex Four2 (LSF2), which dephosphorylate starch. Starch is water-insoluble and reversible phosphorylation solubilizes its outer surface allowing processive degradation. Vertebrates contain a single known glucan phosphatase, laforin, that dephosphorylates glycogen. In the absence of laforin, water-soluble glycogen becomes insoluble, leading to the neurodegenerative disorder Lafora Disease. Because of their essential role in starch and glycogen metabolism glucan phosphatases are of significant interest, yet a comparative analysis of their activities against diverse glucan substrates has not been established. We identify active site residues required for specific glucan dephosphorylation, defining a glucan phosphatase signature motif (CζAGΨGR) in the active site loop. We further explore the basis for phosphate position-specific activity of these enzymes and determine that their diverse phosphate position-specific activity is governed by the phosphatase domain. In addition, we find key differences in glucan phosphatase activity toward soluble and insoluble polyglucan substrates, resulting from the participation of ancillary glucan-binding domains. Together, these data provide fundamental insights into the specific activity of glucan phosphatases against diverse polyglucan substrates.
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