Laforin

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epilepsy, progressive myoclonus type 2A, Lafora disease (laforin)
Identifiers
SymbolEPM2A
Entrez7957
HUGO3413
OMIM607566
PDB4RKK
RefSeqNM_001018041
UniProtO95278
Other data
LocusChr. 6 q24

Laforin, encoded by the EPM2A gene, is a phosphatase, with a carbohydate-binding domain, which is mutated in patients with Lafora disease.[1][2] It contains a dual specificity phosphatase domain (DSP) and a carbohydrate binding module subtype 20[3] (CBM20). Its physiological substrate has yet to be identified and the molecular mechanisms in which mutated laforin causes Lafora disease is unknown, though there has been progress made in the study by Ortolano et al.[1] Laforin regulates autophagy via Mammalian target of rapamycin, which is impaired in Lafora disease.[4]

References

  1. 1.0 1.1 Ortolano S, Vieitez I, Agis-Balboa RC, Spuch C (January 2014). "Loss of GABAergic cortical neurons underlies the neuropathology of Lafora disease". Molecular Brain. 7: 7. doi:10.1186/1756-6606-7-7. PMC 3917365. PMID 24472629.
  2. Ganesh S, Agarwala KL, Ueda K, Akagi T, Shoda K, Usui T, Hashikawa T, Osada H, Delgado-Escueta AV, Yamakawa K (September 2000). "Laforin, defective in the progressive myoclonus epilepsy of Lafora type, is a dual-specificity phosphatase associated with polyribosomes". Human Molecular Genetics. 9 (15): 2251–61. doi:10.1093/oxfordjournals.hmg.a018916. PMID 11001928.
  3. "CAZy - CBM".
  4. Aguado C, Sarkar S, Korolchuk VI, Criado O, Vernia S, Boya P, Sanz P, de Córdoba SR, Knecht E, Rubinsztein DC (July 2010). "Laforin, the most common protein mutated in Lafora disease, regulates autophagy". Human Molecular Genetics. 19 (14): 2867–76. doi:10.1093/hmg/ddq190. PMC 2893813. PMID 20453062.

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