Ontology highlight
ABSTRACT:
SUBMITTER: Millrine D
PROVIDER: S-EPMC9638016 | biostudies-literature | 2022 Aug
REPOSITORIES: biostudies-literature
Millrine David D Cummings Thomas T Matthews Stephen P SP Peter Joshua J JJ Magnussen Helge M HM Lange Sven M SM Macartney Thomas T Lamoliatte Frederic F Knebel Axel A Kulathu Yogesh Y
Cell reports 20220801 5
An essential first step in the post-translational modification of proteins with UFM1, UFMylation, is the proteolytic cleavage of pro-UFM1 to expose a C-terminal glycine. Of the two UFM1-specific proteases (UFSPs) identified in humans, only UFSP2 is reported to be active, since the annotated sequence of UFSP1 lacks critical catalytic residues. Nonetheless, efficient UFM1 maturation occurs in cells lacking UFSP2, suggesting the presence of another active protease. We herein identify UFSP1 translat ...[more]