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- W2738580038 abstract "The role of signaling in regulating cholesterol homeostasis is gradually becoming more widely recognized. Here, we explored how kinases and phosphorylation sites regulate the activity of the enzyme involved in the final step of cholesterol synthesis (3β-hydroxysterol Δ24-reductase; DHCR24). Many factors are known to regulate DHCR24 transcriptionally, but little is known about its post-translational regulation. We developed a system to specifically test human ectopic DHCR24 activity in a model cell-line (Chinese hamster ovary-7) using siRNA targeted only to hamster DHCR24, thus ensuring that all activity could be attributed to the human enzyme. We determined the effect of known phosphorylation sites and found that mutating certain residues (T110, Y299, and Y507) inhibited DHCR24 activity. In addition, inhibitors of protein kinase C ablated DHCR24 activity, although not through a known phosphorylation site. Our data indicate a novel mechanism whereby DHCR24 activity is regulated by signaling. Moreover, we propose that post-translational modifications such as phosphorylation are a valuable resource for mapping the topology of membrane-associated proteins such as DHCR24. The Brown lab is funded by grants from the National Health and Medical Research Council." @default.
- W2738580038 created "2017-07-31" @default.
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- W2738580038 date "2015-04-01" @default.
- W2738580038 modified "2023-09-23" @default.
- W2738580038 title "Signaling Regulates Activity of DHCR24, the Final Enzyme in Cholesterol Synthesis" @default.
- W2738580038 doi "https://doi.org/10.1096/fasebj.29.1_supplement.568.7" @default.
- W2738580038 hasPublicationYear "2015" @default.
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