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

Andrea Kuchtová, Matthew S. Gentry, Štefan Janeček

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

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.

Original languageEnglish
Pages (from-to)586-598
Number of pages13
JournalFEBS Letters
Volume592
Issue number4
DOIs
StatePublished - Feb 2018

Bibliographical note

Publisher Copyright:
© 2018 Federation of European Biochemical Societies

Keywords

  • 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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