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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 03 Jul 2015.

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, AGE, HAD, CAN, 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, 02 Aug 2015
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.
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, 20 Jul 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).
Clinical and genetic data on Lafora disease patients of Serbian/Montenegrin origin.
New
Romac et al., Belgrade, Serbia. In Clin Genet, Mar 2015
LD is caused by mutations either in the EPM2A or in NHLRC1 genes.
Oxidative stress, a new hallmark in the pathophysiology of Lafora progressive myoclonus epilepsy.
New
Pallardó et al., Valencia, Spain. In Free Radic Biol Med, Mar 2015
UNASSIGNED: Lafora Disease (LD, OMIM 254780, ORPHA501) is a devastating neurodegenerative disorder characterized by the presence of glycogen-like intracellular inclusions called Lafora bodies and caused, in most cases, by mutations in either EPM2A or EPM2B genes, encoding respectively laforin, a phosphatase with dual specificity that is involved in the dephosphorylation of glycogen, and malin, an E3-ubiquitin ligase involved in the polyubiquitination of proteins related with glycogen metabolism.
A recurrent de novo mutation in KCNC1 causes progressive myoclonus epilepsy.
New
Impact
Lehesjoki et al., Helsinki, Finland. In Nat Genet, Jan 2015
Ten cases had pathogenic mutations in known PME-associated genes (NEU1, NHLRC1, AFG3L2, EPM2A, CLN6 and SERPINI1).
Unclassified cardiomyopathies in neuromuscular disorders.
Review
Stöllberger et al., Vienna, Austria. In Wien Med Wochenschr, 2013
Takotsubo syndrome has been described in association with myasthenia gravis, amyotrophic lateral sclerosis, Guillain-Barre syndrome, rhabdomyolysis, mitochondrial disorder, hypokalemia-related myopathy, syndrome malin, hereditary sensorimotor neuropathy, Beals syndrome, polymyalgia rheumatica, and unclassified myopathy.
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.
Lafora disease: severe phenotype associated with homozygous deletion of the NHLRC1 gene.
Review
Romac et al., Belgrade, Serbia. In J Neurol Sci, 2013
It is due to either EPM2A or NHLRC1 mutations.
Progressive myoclonus epilepsy.
Review
Minassian et al., Toronto, Canada. In Handb Clin Neurol, 2012
It is caused by defects of two genes of yet unknown function, one encoding a glycogen phosphatase (laforin) and the other an ubiquitin E3 ligase (malin).
Deciphering the role of malin in the lafora progressive myoclonus epilepsy.
Review
Gentry et al., Valencia, Spain. In Iubmb Life, 2012
LD is caused by mutations in the gene encoding the E3 ubiquitin ligase malin or the glucan phosphatase laforin.
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.
Lafora progressive myoclonus epilepsy: recent insights into cell degeneration.
Review
Navarro et al., Vigo, Spain. In Recent Pat Endocr Metab Immune Drug Discov, 2012
The EPM2A gene encodes laforin, a dual-specificity protein phosphatase, and the NHLRC1 gene encodes malin, an E3-ubiquitin ligase.
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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