The mammalian cholesterol synthesis enzyme squalene monooxygenase is proteasomally truncated to a constitutively active form

• Published in: The Journal of biological chemistry Vol. 296; p. 100731
• Main Authors: Coates, Hudson W., Capell-Hattam, Isabelle M., Brown, Andrew J.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.01.2021; American Society for Biochemistry and Molecular Biology
• Subjects: cholesterol; endoplasmic reticulum–associated protein degradation; proteasome; protein degradation; squalene monooxygenase; ubiquitylation (ubiquitination); proteasome; VCP; [HA]3–SM–V5; DMSO; RIPA; ubiquitylation (ubiquitination); BSA; GSK-3β; HEK293; FCLPDS; cholesterol; cDNA; SM; UNSW; MARCHF6; SM-N100; trunSM; DMEM-HG; squalene monooxygenase; endoplasmic reticulum–associated protein degradation; DOS; ER; ERAD; MOS; SQLE; PBST; FCS; HA; protein degradation; endoplasmic reticulum-associated protein degradation (ERAD)

Squalene monooxygenase (SM, also known as squalene epoxidase) is a rate-limiting enzyme of cholesterol synthesis that converts squalene to monooxidosqualene and is oncogenic in numerous cancer types. SM is subject to feedback regulation via cholesterol-induced proteasomal degradation, which depends...