The utrophin-beta 2 syntrophin complex regulates adipocyte lipid droplet size independent of adipogenesis
Abstract
Utrophin is a widely expressed cytoskeleton protein and is associated with lipid droplets (LDs) in adipocytes. The scaffold protein beta 2 syntrophin (SNTB2) controls signaling events by recruiting distinct membrane and cytoskeletal proteins, and binds to utrophin. Here we show that SNTB2 forms a complex with utrophin in adipocytes. SNTB2 protein is strongly diminished when utrophin is low. Of note, knock-down of utrophin or SNTB2 enhances LD growth during adipogenesis. SNTB2 reduction has no effect on basal and induced lipolysis, and insulin-stimulated phosphorylation of Akt is normal. The antilipolytic activity of insulin is enhanced in adipocytes with low SNTB2, while knock-down of utrophin has no effect. Uptake of exogenously supplied oleate and linoleate is comparable in scrambled and SNTB2 siRNA-treated cells. In the fibroblasts, diminished SNTB2 is associated with lower proliferation. CCAAT/enhancer-binding protein alpha and sterol regulatory element-binding proteins which are critical transcription factors for adipogenesis are normally expressed. Consequently, maturation of cells with SNTB2 knock-down is not grossly impaired. In fibroblasts, SNTB2 is localized to filamentous and vesicular structures which are distinct f...Continue Reading
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