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The protein encoded by NHLRC1 is a single subunit E3 ubiquitin ligase. Additionally we are shipping NHLRC1 Antibodies (68) and NHLRC1 Kits (3) and many more products for this protein.
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Malin promotes its own degradation via auto-ubiquitination.Malin preferentially degrades the phosphatase-inactive laforin (show EPM2A Proteins) monomer.
laforin/malin complex is able to interact with and ubiquitinate both PKM1 and PKM2
Lafora disease proteins laforin (show EPM2A Proteins) and malin negatively regulate the HIPK2 (show HIPK2 Proteins)-p53 (show TP53 Proteins) cell death pathway.
This study demonistrated that NHLRC1 mutations were detected in some case of Mild Lafora disease patients.
Without functional laforin (show EPM2A Proteins)-malin complex assembled on polyglucosan bodies, polyglucosan is not degraded.
Malin regulates the recruitment of mRNA-decapping enzyme 1A (Dcp1a (show DCP1A Proteins)) to processing bodies.
Malin forms a functional complex with laforin (show EPM2A Proteins). This complex promotes the ubiquitination of proteins involved in glycogen (show GYS1 Proteins) metabolism and misregulation of pathways involved in this process results in Lafora body formation. (Review)
This study identified that NHLRC1 gene mutations leading to Lafora disease in six Turkish families.
Our results indicate that malin regulates Wnt (show WNT2 Proteins) signaling pathway through the degradation of dishevelled2 and suggest possible deregulation of Wnt (show WNT2 Proteins) signaling in Lafora disease.
Mutations in the NHL repeat containing 1 (NHLRC1) gene are described in association with a more benign clinical course and later age of death in an adolescent patient.
The authors conclude that laforin's principle function is to control glycogen (show GYS1 Proteins) chain lengths, in a malin-dependent fashion, and that loss of this control underlies Lafora disease.
The present study analyzes possible inflammatory responses in the mouse lines Epm2a (-/-) (laforin (show EPM2A Proteins) knock-out) and Epm2b (-/-) (malin knock-out) with disease progression.
that laforin and malin are novel regulators of mitochondrial quality control pathway and that the mitochondrial dysfunction resulting from the increased Drp1 levels could underlie neuropathology in Lafora disease
Loss of malin leads to reduced proteasomal activity in the heat-shocked cells.
This study also suggests a malin function independent of laforin (show EPM2A Proteins), possibly in lysosomal biogenesis and/or lysosomal glycogen (show GYS1 Proteins) disposal.
Results indicate that malin has no effect on whole-body glucose metabolism and insulin (show INS Proteins) sensitivity.
Dysfunction of autophagy is a common feature of both laforin (show EPM2A Proteins)- and malin-deficient mice.
malin functions to regulate laforin (show EPM2A Proteins) and that malin deficiency at least in part causes LB and LD through increased laforin (show EPM2A Proteins) binding to glycogen (show GYS1 Proteins).
Results show that a functional laforin (show EPM2A Proteins)-malin complex plays a critical role in disrupting Lafora bodies and relieving endoplasmic reticulum stres.
Motor coordination, activity impairment, and memory deficits progressively increase with age in Epm2b deficient mice.
The protein encoded by this gene is a single subunit E3 ubiquitin ligase. Laforin is polyubiquitinated by the encoded protein. Defects in this intronless gene lead to an accumulation of laforin and onset of Lafora disease, also known as progressive myoclonic epilepsy type 2 (EPM2).
E3 ubiquitin-protein ligase NHLRC1
, NHL repeat-containing protein 1
, NHL repeat containing 1
, NHL repeat-containing protein 1-like