The unique evolution of the carbohydrate-binding module CBM20 in laforin

Andrea Kuchtová, Matthew S. Gentry, Štefan Janeček

Research output: Contribution to journalArticlepeer-review

12 Scopus citations


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.

Original languageEnglish
Pages (from-to)586-598
Number of pages13
JournalFEBS Letters
Issue number4
StatePublished - Feb 2018

Bibliographical note

Funding Information:
This work was supported by the grant No. 2/0146/17 from the Slovak Grant Agency VEGA to SJ and the grant No. R01NS070899 from the National Institutes of Health to MSG. AK thanks for the short-term fellowship from the Slovak Academic Information Agency SAIA.

Publisher Copyright:
© 2018 Federation of European Biochemical Societies


  • Lafora disease
  • carbohydrate-binding module
  • domain arrangement
  • evolutionary relatedness
  • family CBM20
  • laforin

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology


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