ArticleThe Journal of biological chemistry2015
Dimeric quaternary structure of human laforin.
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 11 papers.
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Who cites it
11 citing papers in PubMed.
- DUSP family phosphatases in cell signaling, inflammation, and chronic diseases.Journal of biomedical science · 2026Review
- Identification of Novel Inhibitors of Starch Excess 4 (SEX4).Life (Basel, Switzerland) · 2024Article
- Lafora progressive myoclonus epilepsy: Disease mechanism and therapeutic attempts.Journal of biosciences · 2024Review
- A Review of DUSP26: Structure, Regulation and Relevance in Human Disease.International journal of molecular sciences · 2021Review
- Molecular Architecture of the Inositol Phosphatase Siw14.Biochemistry · 2019Article
- Oligomerization and carbohydrate binding of glucan phosphatases.Analytical biochemistry · 2018Article
- Lafora disease: from genotype to phenotype.Journal of genetics · 2018Review
- Abnormal glycogen chain length pattern, not hyperphosphorylation, is critical in Lafora disease.EMBO molecular medicine · 2017Article
- Unique carbohydrate binding platforms employed by the glucan phosphatases.Cellular and molecular life sciences : CMLS · 2016Review
- Remarkable evolutionary relatedness among the enzymes and proteins from the α-amylase family.Cellular and molecular life sciences : CMLS · 2016Review
- Glycogen metabolism in humans.BBA clinical · 2016Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The phosphatase laforin removes phosphate groups from glycogen during biosynthetic activity. Loss-of-function mutations in the gene encoding laforin is the predominant cause of Lafora disease, a fatal form of progressive myoclonic epilepsy. Here, we used hybrid structural methods to determine the molecular architecture of human laforin. We found that laforin adopts a dimeric quaternary structure, topologically similar to the prototypical dual specificity phosphatase VH1. The interface between the laforin carbohydrate-binding module and the dual specificity phosphatase domain generates an intimate substrate-binding crevice that allows for recognition and dephosphorylation of phosphomonoesters of glucose. We identify novel molecular determinants in the laforin active site that help decipher the mechanism of glucan phosphatase activity.
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