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

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• 作者：Anika V. Prabhu¹ ; Winnie Luu¹ ; Laura J. Sharpe ; Andrew J. Brown ; ^{aj.brown@unsw.edu.au}
• 关键词：7DHC ; 7-dehydrocholesterol ; AMPK ; AMP-activated protein kinase ; CaMKII ; calmodulin-dependent kinase II ; CHO ; Chinese hamster ovary ; CKI ; casein kinase I ; DHCR7 ; 7-dehydrocholesterol reductase ; HMGCR ; 3-hydroxy-3-methylglutaryl-CoA reductase ; PBGD ; porphobilinogen deaminase ; PKA ; protein kinase A ; SLOS ; Smith-Lemli-Opitz syndrome
• 刊名：The Journal of Steroid Biochemistry and Molecular Biology
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：165
• 期：part_PB
• 页码：363-368
• 全文大小：642 K
• 卷排序：165

文摘

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.