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 language | English |
|---|---|
| Pages (from-to) | 586-598 |
| Number of pages | 13 |
| Journal | FEBS Letters |
| Volume | 592 |
| Issue number | 4 |
| DOIs | |
| State | Published - 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
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
