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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 18 Mar 2014.

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, HAD, AGE, ACID
Papers on EPM2A
The phosphatase activity of laforin is dispensable to rescue Epm2a-/- mice from Lafora disease.
New
Rodríguez de Córdoba et al., Madrid, Spain. In Brain, 31 Mar 2014
The vast majority of patients carry mutations in either the EPM2A or EPM2B genes, encoding laforin, a glucan phosphatase, and malin, an E3 ubiquitin ligase, respectively.
Glycogen accumulation underlies neurodegeneration and autophagy impairment in Lafora Disease.
New
Guinovart et al., Barcelona, Spain. In Hum Mol Genet, 22 Feb 2014
It is an autosomal recessive disorder caused by mutations in either the laforin or malin gene.
PTG depletion rescues malin-deficient Lafora disease in mouse.
New
Minassian et al., Toronto, Canada. In Ann Neurol, 13 Feb 2014
The malin ubiquitin E3 ligase is reported to regulate autophagy, the misfolded protein response, microRNA silencing, Wnt signaling, neuronatin-mediated endoplasmic reticulum stress, and the laforin glycogen phosphatase.
Loss of GABAergic cortical neurons underlies the neuropathology of Lafora disease.
New
Spuch et al., Pontevedra, Spain. In Mol Brain, Dec 2013
Lafora disease can be caused by defects in the EPM2A gene, which encodes the laforin protein phosphatase, or in the NHLRC1 gene (also called EPM2B) codifying the malin E3 ubiquitin ligase.
Hyperphosphorylation of glucosyl C6 carbons and altered structure of glycogen in the neurodegenerative epilepsy Lafora disease.
New
Impact
Minassian et al., Potsdam, Germany. In Cell Metab, Jun 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
New
Romac et al., Belgrade, Serbia. In J Neurol Sci, Mar 2013
It is due to either EPM2A or NHLRC1 mutations.
Laforin, a protein with many faces: glucan phosphatase, adapter protein, et alii.
Review
Sanz et al., Lexington, United States. In Febs J, 2013
The main cause of the disease is related to the activity of two proteins, the dual-specificity phosphatase laforin and the E3-ubiquitin ligase malin, which form a functional complex.
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 knockout mice support a primary role of autophagy in the pathogenesis of Lafora disease.
Review
Rodríguez de Córdoba et al., Valencia, Spain. In Autophagy, 2012
Lafora disease (LD), a fatal neurodegenerative disorder characterized by intracellular inclusions called Lafora bodies (LBs), is caused by recessive loss-of-function mutations in the genes encoding either laforin or malin.
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
Mutations in a gene encoding a novel protein tyrosine phosphatase cause progressive myoclonus epilepsy.
Impact
Scherer et al., Toronto, Canada. In Nat Genet, 1998
Using a positional cloning approach, we have identified at chromosome 6q24 a novel gene, EPM2A, that encodes a protein with consensus amino acid sequence indicative of a protein tyrosine phosphatase (PTP).
Relationship of cyst nematode gene frequencies to soybean resistance.
Luedders, Columbia, United States. In Theor Appl Genet, 1989
The acronym "alins" was proposed for these alleles for incompatibility, with "xalin" representing the interaction X of one microsymbiont malin with its host h-alin.
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