Structural advances in sterol-sensing domain-containing proteins.
Trends Biochem Sci
; 47(4): 289-300, 2022 04.
Article
en En
| MEDLINE
| ID: mdl-35012873
ABSTRACT
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 element-binding protein (SREBP)-cleavage activating protein (Scap), Patched, 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.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Péptidos y Proteínas de Señalización Intracelular
/
Proteína Niemann-Pick C1
Idioma:
En
Revista:
Trends Biochem Sci
Año:
2022
Tipo del documento:
Article
País de afiliación:
Estados Unidos