Journal
TRENDS IN BIOCHEMICAL SCIENCES
Volume 47, Issue 4, Pages 289-300Publisher
CELL PRESS
DOI: 10.1016/j.tibs.2021.12.005
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This article summarizes recent structural and mechanistic investigations of sterol-sensing domain (SSD)-containing proteins and proposes to divide them into moderators and transporters.
The sterol-sensing domain (SSD) is present in several membrane proteins that function in cholesterol metabolism, transport, and signaling. Recent progress in structural studies of SSD-containing proteins, such as sterol regulatory Niemann-Pick disease type C1 (NPC1), and related proteins, reveals a conserved core that is essential for their sterol-dependent functions. This domain, by its name, 'senses' the presence of sterol substrates through interactions and may modulate protein behaviors with changing sterol levels. We summarize recent advances in structural and mechanistic investigations of these proteins and propose to divide them to two classes: M for 'moderator' proteins that regulate sterol metabolism in response to membrane sterol levels, and T for 'transporter' proteins that harbor inner tunnels for cargo trafficking across cellular membranes.
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