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Epilepsy, progressive myoclonus type 2A, Lafora disease

EPM2A, malin, EPM2B, Laforin, NHLRC1
This gene encodes a dual-specificity phosphatase that associates with polyribosomes. The encoded protein may be involved in the regulation of glycogen metabolism. Mutations in this gene have been associated with myoclonic epilepsy of Lafora. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Ubiquitin, CAN, AGE, HAD, ACID
Papers on EPM2A
Non-invasive gene targeting to the fetal brain after intravenous administration and transplacental transfer of plasmid DNA using PEGylated immunoliposomes.
New
Pardridge et al., Los Angeles, United States. In J Drug Target, 31 Jan 2016
In addition to studies of normal wild-type mice, we similarly injected pregnant Lafora Knockout (EPM2a null-mutant) and demonstrated luciferase activity days later in the maternal and newborn pup brains of both types.
Interdependence of laforin and malin proteins for their stability and functions could underlie the molecular basis of locus heterogeneity in Lafora disease.
New
Ganesh et al., Kānpur, India. In J Biosci, 31 Dec 2015
LD can be caused by defects either in the EPM2A gene coding for the laforin protein phosphatase or the NHLRC1 gene coding for the malin ubiquitin ligase.
Ubiquitin conjugating enzyme E2-N and sequestosome-1 (p62) are components of the ubiquitination process mediated by the malin-laforin E3-ubiquitin ligase complex.
New
Sanz et al., Valencia, Spain. In Int J Biochem Cell Biol, 31 Dec 2015
Lafora disease (LD, OMIM254780, ORPHA501) is a rare neurodegenerative form of epilepsy related to mutations in two proteins: laforin, a dual specificity phosphatase, and malin, an E3-ubiquitin ligase.
Brain glycogen in health and disease.
New
Guinovart et al., Barcelona, Spain. In Mol Aspects Med, 31 Dec 2015
Loss-of-function mutations in laforin and malin cause Lafora disease.
Polyglucosan storage myopathies.
New
Oldfors et al., Göteborg, Sweden. In Mol Aspects Med, 31 Dec 2015
Mutations in eight human genes are known to be associated with polyglucosan storage involving muscle, namely GYG1, GBE1, RBCK1 (HOIL-1), PFKM, EPM2A, EPM2B (NHLRC1), PRDM8, and PRKAG2.
Biophysical characterization of laforin-carbohydrate interaction.
New
Castanheira et al., Cambridge, United Kingdom. In Biochem J, 17 Dec 2015
UNASSIGNED: Laforin is a human dual-specificity phosphatase involved in glycogen metabolism regulation containing a carbohydrate binding module (CBM).
Lafora disease proteins laforin and malin negatively regulate the HIPK2-p53 cell death pathway.
New
Ganesh et al., Kānpur, India. In Biochem Biophys Res Commun, Sep 2015
LD is caused by defects in either the laforin protein phosphatase or the malin E3 ubiquitin ligase.
Burden analysis of rare microdeletions suggests a strong impact of neurodevelopmental genes in genetic generalised epilepsies.
New
Sander et al., Köln, Germany. In Plos Genet, May 2015
Microdeletions found only in GGE patients harboured a high proportion of genes previously associated with epilepsy and neuropsychiatric disorders (NRXN1, RBFOX1, PCDH7, KCNA2, EPM2A, RORB, PLCB1).
A recurrent de novo mutation in KCNC1 causes progressive myoclonus epilepsy.
Impact
Lehesjoki et al., Helsinki, Finland. In Nat Genet, 2015
Ten cases had pathogenic mutations in known PME-associated genes (NEU1, NHLRC1, AFG3L2, EPM2A, CLN6 and SERPINI1).
The laforin/malin E3-ubiquitin ligase complex ubiquitinates pyruvate kinase M1/M2.
Sanz et al., Valencia, Spain. In Bmc Biochem, 2014
BACKGROUND: Lafora disease (LD, OMIM 254780) is a fatal neurodegenerative disorder produced mainly by mutations in two genes: EPM2A, encoding the dual specificity phosphatase laforin, and EPM2B, encoding the E3-ubiquitin ligase malin.
Increased oxidative stress and impaired antioxidant response in Lafora disease.
Sanz et al., Valencia, Spain. In Free Radic Biol Med, 2014
Lafora Disease (LD, OMIM 254780, ORPHA501) is a fatal neurodegenerative disorder characterized by the presence of glycogen-like intracellular inclusions called Lafora bodies and caused, in the vast majority of cases, by mutations in either EPM2A or EPM2B genes, encoding respectively laforin and malin.
Hyperphosphorylation of glucosyl C6 carbons and altered structure of glycogen in the neurodegenerative epilepsy Lafora disease.
Impact
Minassian et al., Potsdam, Germany. In Cell Metab, 2013
Laforin or malin deficiency causes Lafora disease, characterized by altered glycogen metabolism and teenage-onset neurodegeneration with intractable and invariably fatal epilepsy.
Increased laforin and laforin binding to glycogen underlie Lafora body formation in malin-deficient Lafora disease.
GeneRIF
Minassian et al., Toronto, Canada. In J Biol Chem, 2012
malin functions to regulate laforin and that malin deficiency at least in part causes LB and LD through increased laforin binding to glycogen.
Ontogeny of Lafora bodies and neurocytoskeleton changes in Laforin-deficient mice.
GeneRIF
Delgado-Escueta et al., Los Angeles, United States. In Exp Neurol, 2012
A detailed microscopic analysis of the neuropil of a Laforin-deficient (epm2a-/-) mouse model shows neurofibrillary degeneration and senile-like plaques prominent in the hippocampus and ventral pons.
Laforin is required for the functional activation of malin in endoplasmic reticulum stress resistance in neuronal cells.
GeneRIF
Liu et al., Ann Arbor, United States. In Febs J, 2012
Results show that a functional laforin-malin complex plays a critical role in disrupting Lafora bodies and relieving endoplasmic reticulum stres.
Laforin and malin deletions in mice produce similar neurologic impairments.
GeneRIF
Sánchez et al., Madrid, Spain. In J Neuropathol Exp Neurol, 2012
Motor coordination, activity impairment, and memory deficits progressively increase with age in Epm2a deficient mice.
Malin regulates Wnt signaling pathway through degradation of dishevelled2.
GeneRIF
Jana et al., Gurgaon, India. In J Biol Chem, 2012
Our results indicate that malin regulates Wnt signaling pathway through the degradation of dishevelled2 and suggest possible deregulation of Wnt signaling in Lafora disease.
Epm2a suppresses tumor growth in an immunocompromised host by inhibiting Wnt signaling.
Impact
GeneRIF
Zheng et al., Columbus, United States. In Cancer Cell, 2006
Inactivation of Epm2a resulted in increased Wnt signaling and tumorigenesis
Expanded repeat in canine epilepsy.
Impact
Minassian et al., Toronto, Canada. In Science, 2005
A canid-specific unstable dodecamer repeat in the Epm2b (Nhlrc1) gene recurrently expands, causing a fatal epilepsy and contributing to the high incidence of canine epilepsy.
Mutations in NHLRC1 cause progressive myoclonus epilepsy.
Impact
GeneRIF
Scherer et al., Toronto, Canada. In Nat Genet, 2003
Laforin and malin colocalize to the ER, suggesting they operate in a related pathway protecting against polyglucosan accumulation and epilepsy
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