ArticleFEBS letters2018
The unique evolution of the carbohydrate-binding module CBM20 in laforin.
Article in FEBS letters, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Glycophagy is an ancient bilaterian pathway supporting metabolic adaptation through STBD1 structural evolution.Communications biology · 2026Article
- Impact of Starch Binding Domain Fusion on Activities and Starch Product Structure of 4-α-Glucanotransferase.Molecules (Basel, Switzerland) · 2023Article
- Laforin targets malin to glycogen in Lafora progressive myoclonus epilepsy.Disease models & mechanisms · 2023Article
- A Novel Subfamily GH13_46 of the α-Amylase Family GH13 Represented by the Cyclomaltodextrinase fromMolecules (Basel, Switzerland) · 2022Article
- Mining for novel cyclomaltodextrin glucanotransferases unravels the carbohydrate metabolism pathway via cyclodextrins in Thermoanaerobacterales.Scientific reports · 2022Article
- The rare rs769301934 variant in NHLRC1 is a common cause of Lafora disease in Turkey.Journal of human genetics · 2021Article
- Floridean Starch and Floridoside Metabolic Pathways ofMarine drugs · 2021Article
- Oligomerization and carbohydrate binding of glucan phosphatases.Analytical biochemistry · 2018Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
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Abstract
Laforin catalyses glycogen dephosphorylation. Mutations in its gene result in Lafora disease, a fatal progressive myoclonus epilepsy, the hallmark being water-insoluble, hyperphosphorylated carbohydrate inclusions called Lafora bodies. Human laforin consists of an N-terminal carbohydrate-binding module (CBM) from family CBM20 and a C-terminal dual-specificity phosphatase domain. Laforin is conserved in all vertebrates, some basal metazoans and a small group of protozoans. The present in silico study defines the evolutionary relationships among the CBM20s of laforin with an emphasis on newly identified laforin orthologues. The study reveals putative laforin orthologues in Trichinella, a parasitic nematode, and identifies two sequence inserts in the CBM20 of laforin from parasitic coccidia. Finally, we identify that the putative laforin orthologues from some protozoa and algae possess more than one CBM20.
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