Phosphorylation regulates activity of 7-dehydrocholesterol reductase (DHCR7), a terminal enzyme of cholesterol synthesis

• Published in: The Journal of steroid biochemistry and molecular biology Vol. 165; no. Pt B; pp. 363 - 368
• Main Authors: Prabhu, Anika V., Luu, Winnie, Sharpe, Laura J., Brown, Andrew J.
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 01.01.2017
• Subjects: 7-Dehydrocholesterol; 7-Dehydrocholesterol reductase; AMP-Activated Protein Kinases - metabolism; Animals; CHO Cells; Cholesterol; Cholesterol - biosynthesis; Cricetinae; Cricetulus; Cyclic AMP-Dependent Protein Kinases - metabolism; Gas Chromatography-Mass Spectrometry; Gene Expression Regulation, Enzymologic; Humans; Mutagenesis, Site-Directed; Mutation; Oxidoreductases Acting on CH-CH Group Donors - metabolism; Phosphorylation; RNA, Small Interfering - metabolism; Signaling; Smith-Lemli-Opitz Syndrome - metabolism; Vitamin D; Vitamin D - metabolism; CKI; Phosphorylation; PKA; 7-Dehydrocholesterol reductase; PBGD; CHO; HMGCR; Cholesterol; Signaling; 7DHC; CaMKII; Vitamin D; 7-Dehydrocholesterol; AMPK; DHCR7; SLOS

•Inhibition of AMPK or PKA decreases DHCR7 activity.•Mutation of S14 in DHCR7 decreases activity independently of AMPK and PKA.•In the skin, phosphorylation of DHCR7 may divert flux from cholesterol to vitamin D synthesis. Cholesterol is essential for survival, but too much or too little can cause d...