Cryo electron structure of the ectodomain of SPRING bound to the ectodomain of Site-one protease
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ABSTRACT:
SUBMITTER: Daniel L Kober
PROVIDER: EMPIAR-11928 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
SPRING licenses S1P-mediated cleavage of SREBP2 by displacing an inhibitory pro-domain.
Hendrix Sebastian S Dartigue Vincent V Hall Hailee H Bawaria Shrankhla S Kingma Jenina J Bajaj Bilkish B Zelcer Noam N Kober Daniel L DL
Nature communications 20240709 1
Site-one protease (S1P) conducts the first of two cleavage events in the Golgi to activate Sterol regulatory element binding proteins (SREBPs) and upregulate lipogenic transcription. S1P is also required for a wide array of additional signaling pathways. A zymogen serine protease, S1P matures through autoproteolysis of two pro-domains, with one cleavage event in the endoplasmic reticulum (ER) and the other in the Golgi. We recently identified the SREBP regulating gene, (SPRING), which enhances S ...[more]
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