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• W2340423587 abstract "Abstract Dematin is a relatively low abundance actin binding and bundling protein associated with the spectrin–actin junctions of mature erythrocytes. Primary structure of dematin includes a loosely folded core domain and a compact headpiece domain that was originally identified in villin. Dematin’s actin binding properties are regulated by phosphorylation of its headpiece domain by cyclic adenosine monophosphate–dependent protein kinase. Here, we used a novel gene disruption strategy to generate the whole body dematin gene knockout mouse model (FLKO). FLKO mice, while born at a normal Mendelian ratio, developed severe anemia and exhibited profound aberrations of erythrocyte morphology and membrane stability. Having no apparent effect on primitive erythropoiesis, FLKO mice show significant enhancement of erythroblast enucleation during definitive erythropoiesis. Using membrane protein analysis, domain mapping, electron microscopy, and dynamic deformability measurements, we investigated the mechanism of membrane instability in FLKO erythrocytes. Although many membrane and cytoskeletal proteins remained at their normal levels, the major peripheral membrane proteins spectrin, adducin, and actin were greatly reduced in FLKO erythrocytes. Our results demonstrate that dematin plays a critical role in maintaining the fundamental properties of the membrane cytoskeleton complex." @default.
• W2340423587 created "2016-06-24" @default.
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• W2340423587 date "2016-07-07" @default.
• W2340423587 modified "2023-10-05" @default.
• W2340423587 title "Gene disruption of dematin causes precipitous loss of erythrocyte membrane stability and severe hemolytic anemia" @default.
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• W2340423587 doi "https://doi.org/10.1182/blood-2016-01-692251" @default.
• W2340423587 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4937361" @default.
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