From Wikipedia, the free encyclopedia
Laforin, encoded by the EPM2A
gene, is a
phosphatase, with a
carbohydrate-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]
- ^
a
b 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.
-
^ 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.
-
^
"CAZy - CBM". Archived from
the original on 2007-02-25. Retrieved 2007-03-28.
-
^ 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.