Loss of Ufsp1 does not cause major changes at the neuromuscular junction.

ABSTRACT: UFMylation is a Ubiquitin-like post-translational modification involved in myriad of cellular processes. Enzymes involved in this pathway, including ligases and UFM1-specific proteases, are essential for development and homeostasis. Our previous transcriptomic analyses identified an enrichment of Ufsp1 at the neuromuscular junction of skeletal muscle cells. Ufsp1, one of the two UFM1 proteases, had been considered a pseudogene due to truncation of its catalytic domain in several species, including humans. However, recent findings revealed that Ufsp1 is translated from a non-canonical start codon in humans, yielding a catalytically active enzyme. This discovery has revived interest in studying Ufsp1's role in vivo. We generated two mutant mouse models, one with a point mutation abolishing c

SUBMITTER: Calvo C 

PROVIDER: S-EPMC12316231 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature