Search results for "VILIP-1"

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Dimerization of visinin-like protein 1 is regulated by oxidative stress and calcium and is a pathological hallmark of amyotrophic lateral sclerosis

2014

AbstractRedox control of proteins that form disulfide bonds upon oxidative challenge is an emerging topic in the physiological and pathophysiological regulation of protein function. We have investigated the role of the neuronal calcium sensor protein visinin-like protein 1 (VILIP-1) as a novel redox sensor in a cellular system. We have found oxidative stress to trigger dimerization of VILIP-1 within a cellular environment and identified thioredoxin reductase as responsible for facilitating the remonomerization of the dimeric protein. Dimerization is modulated by calcium and not dependent on the myristoylation of VILIP-1. Furthermore, we show by site-directed mutagenesis that dimerization is…

Thioredoxin reductaseAmino Acid MotifsBlotting Westernchemistry.chemical_elementMice TransgenicFree radicalsOxidative phosphorylationCalciumProtein aggregationmedicine.disease_causeBiochemistryMass SpectrometryMicechemistry.chemical_compoundSuperoxide Dismutase-1BAPTAPhysiology (medical)VILIP-1medicineAnimalsHumansCysteineMyristoylationSuperoxide DismutaseChemistryHEK 293 cellsAmyotrophic lateral sclerosisRedox sensorImmunohistochemistryCell biologyDisease Models AnimalOxidative StressHEK293 CellsBiochemistryNeurocalcinMutagenesis Site-DirectedCalciumProtein MultimerizationOxidation-ReductionOxidative stressFree Radical Biology and Medicine
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