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In steroidogenic tissues, upon hormone stimulation, there is a rapid transfer of cholesterol to the mitochondria, which is the site of the initial step in steroidogenesis. In the current study, we examined PM cholesterol trafficking for steroidogenesis. In a mitochondrial reconstitution assay, adrenal PMs supported steroidogenesis in the absence of additional transport proteins. Depletion of cholesterol in PMs by 50% eliminated the membranes' ability to support steroidogenesis\n                    <jats:italic>in vitro<\/jats:italic>\n                    and reduced steroid production in intact Y1 adrenocortical cells. Syntaxin (STX)\u20105 and \u03b1\u2010soluble\n                    <jats:italic>N<\/jats:italic>\n                    \u2010emylmaleimide\u2010sensitive factor attachment protein (\u03b1\u2010SNAP) are enriched in adrenal PMs, and adrenocorticotropic hormone treatment of rats recruited STX5 and \u03b1\u2010SNAP to adrenal PMs and mitochondria. Immunodepletion of STX5 and \u03b1\u2010SNAP from PMs decreased steroidogenesis supported by PMs\n                    <jats:italic>in vitro<\/jats:italic>\n                    . Protease digestion of PMs decreased, whereas recombinant STX5 or \u03b1\u2010SNAP restored, the PMs' ability to support steroidogenesis. Knockdown of either STX5 or \u03b1\u2010SNAP in Y1 cells decreased stimulated steroidogenesis. These results indicate that STX5 and \u03b1\u2010SNAP facilitate cholesterol trafficking from PMs to mitochondria for adrenal steroid synthesis and underscore the importance of vesicular trafficking of PM cholesterol for steroidogenesis.\u2014Deng, B., Shen, W.\u2010J., Dong, D., Azhar, S., Kraemer, F. B. Plasma membrane cholesterol trafficking in steroidogenesis. 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