EPM2A Antibody

1. rs702304 and rs2235481 within the EPM2A gene were associated with schizophrenia liability. PMID: 27092952
2. Laforin prevents the auto-degradation of malin by presenting itself as a substrate. Malin preferentially degrades the phosphatase-inactive laforin monomer. PMID: 26648032
3. Laforin-glycan interactions occur with a favourable enthalpic contribution counter-balanced by an unfavourable entropic contribution. PMID: 26578817
4. laforin is responsible for glycogen dephosphorylation during exercise and acts during the cytosolic degradation of glycogen PMID: 26216881
5. Lafora disease proteins laforin and malin negatively regulate the HIPK2-p53 cell death pathway. PMID: 26102034
6. This study suggest that variations in phenotypes of EPM2A-deficient Lafora disease. PMID: 25246353
7. novel molecular determinants in the laforin active site that help decipher the mechanism of glucan phosphatase activity. PMID: 25538239
8. The crystal structure of laforin bound to phosphoglucan product, reveals its unique integrated tertiary and quaternary structure. PMID: 25544560
9. This study identified some Mild Lafora disease have EPM2A mutation. PMID: 25270369
10. Studied the role of conformational changes in human laforin structure due to existing single mutation W32G and prepared double mutation W32G/K87A related to loss of glycogen binding. PMID: 24770803
11. Polyglucosan body degradation requires a protein assembly that includes laforin and malin. PMID: 24068615
12. This study identified the flexibility of K87A mutated laforin structure, with replacement of acidic amino acid to aliphatic amino acid in functional carbohydrate binding module domain, have more impact in abolishing glycogen binding that favors Lafora disease. PMID: 23904258
13. These results suggest that cysteine 329 is specifically involved in the dimerization process of laforin. PMID: 23922729
14. A new novel mutation of the EPM2A gene is identified that causes Lafora disease. PMID: 23313408
15. Studies indicate that laforin directly dephosphorylates glycogen. PMID: 22364389
16. Malin forms a functional complex with laforin. This complex promotes the ubiquitination of proteins involved in glycogen metabolism and misregulation of pathways involved in this process results in Lafora body formation. (Review) PMID: 22815132
17. This study identified that EPM2 gene mutations leading to Lafora disease in six Turkish families. PMID: 22047982
18. alternative splicing could possibly be one of the mechanisms by which EPM2A may regulate the cellular functions of the proteins it codes for PMID: 22036712
19. Genetic analysis showed a novel c.659 T>A mutation on exon 3 of the EPM2A gene, in a patient with Lafora's disease. PMID: 21371719
20. laforin monomer is the dominant form of the protein and that it contains phosphatase activity. PMID: 21887368
21. Laforin and malin are defective in Lafora disease (LD), a neurodegenerative disorder associated with epileptic seizures PMID: 21652633
22. glycogen phosphorylation can be considered a catalytic error and laforin a repair enzyme. PMID: 21930129
23. results of the present study suggest that phosphorylation of laforin-Ser(25) by AMPK provides a mechanism to modulate the interaction between laforin and malin PMID: 21728993
24. study described several novel mutations of EPM2A and NHLRC1 and brought additional data to genetic epidemiology of Lafora disease (LD); emphasized the high mutation rate in patients with classical LD as well as the high negativity rate of skin biopsy PMID: 20738377
25. These results suggest that the modification introduced by the laforin-malin complex could affect the subcellular distribution of AMPK beta subunits. PMID: 20534808
26. Laforin regulates autophagy. PMID: 20453062
27. Laforin is an active phosphatase; therefore, isoforms targeted to different cellular compartments might dephosphorylate and regulate distinct cellular substrates. PMID: 11883934
28. identification of mutations in EPM2A with phenotypes of 22 patients (14 families) and identification of two subsyndromes PMID: 12019207
29. The EPM2AIP1 gene was identified and characterized in a screen for laforin-interacting proteins with a human brain cDNA library; the specificity of the interaction was confirmed; subcellular colocalization of laforin and EPM2AIP1 protein was demonstrated PMID: 12782127
30. Laforin interacts with HIRPI5. PMID: 12915448
31. Up to 20% cases of LD are not genetically linked to chromosome 6. We report two sisters affected from bioptically diagnosed LD but without evidence of EPM2A mutation PMID: 14643920
32. encodes a 331 amino acid protein that contains an N-terminal carbohydrate-binding domain (CBD) and a C-terminal dual-specificity phosphatase domain. The CBD of laforin targets the protein to Lafora inclusion bodies. PMID: 14706656
33. Six novel mutations were identified, one of which is the first mutation specific to the cytoplasmic laforin isoform, implicating this isoform in disease pathogenesis. PMID: 14722920
34. Laforin is a Glycogen-Synthase-Kinase-3 Ser 9 phosphatase, and therefore capable of inactivating GS through GSK3. PMID: 16115820
35. Laforin does not dephosphorylate GSK3B (beta) in vitro, but possesses the unique ability to utilize a phosphorylated complex carbohydrate as a substrate and this function may be necessary for the maintenance of normal cellular glycogen. PMID: 16901901
36. Inactivation of Epm2a resulted in increased Wnt signaling and tumorigenesis PMID: 16959610
37. results demonstrate a critical role of dimerization in Laforin function and suggest an important new dimension in protein phosphatase function and in molecular pathogenesis of Lafora's disease PMID: 16971387
38. Defects in laforin may lead to increased levels of misfolded and/or target proteins, which may eventually affect the physiological processes of the neuron, and likely to be the primary trigger in the physiopathology of lafora disease. PMID: 17337485
39. study concludse that considerable variability in the age at onset of Lafora disease can occur within families; identical mutations can be associated with the classic adolescent presentation, as well as late-onset cases PMID: 17509003
40. Regulation of glycogen synthesis by the laforin-malin complex is modulated by the AMP-activated protein kinase pathway. PMID: 18029386
41. Results suggest that the altered subcellular localization of mutant proteins of the EPM2A and NHLRC1 genes could be one of the molecular bases of the Lafora disease phenotype. PMID: 18311786
42. EPM2A regulated by alternative splicing plays roles in Lafora progressive myoclonus epilepsy. PMID: 18617530
43. Laforin and malin interact with misfolded proteins and promote their degradation through the ubiquitin-proteasome system. PMID: 19036738
44. phosphorylation of R5/PTG at Ser-8 by AMPK accelerates its laforin/malin-dependent ubiquitination and subsequent proteasomal degradation, which results in a decrease of its glycogenic activity. PMID: 19171932
45. Mutations of EPM2A formed aggregates and elicited endoplasm reticulum stress in neuronal cell. PMID: 19403557
46. laforin and malin play a role protecting cells from ER-stress, likely contributing to the elimination of unfolded proteins PMID: 19529779
47. Laforin is conserved in all vertebrates and a small class of protists; it is not found in other organisms. Additionally, laforin is a functional equivalent of the plant phosphatase SEX4, and it may function to dephosphorylate complex carbohydrates. PMID: 17646401
48. Laforin acts as a scaffold that allows the E3 ubiquitin ligase malin to ubiquitinate protein targeting to glycogen (PTG). These results suggest an additional mechanism, involving laforin and malin, in regulating glycogen metabolism. PMID: 18070875

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HGNC: 3413

OMIM: 254780

KEGG: hsa:7957

STRING: 9606.ENSP00000356489

UniGene: Hs.486696