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Cryo electron structure of the ectodomain of SPRING bound to the ectodomain of Site-one protease


ABSTRACT:

SUBMITTER: Daniel L Kober 

PROVIDER: EMPIAR-11928 | biostudies-other |

REPOSITORIES: biostudies-other

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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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