SUMO-mediated regulation of integrins during C. elegans embryogenesis

Integrins are transmembrane proteins that mediate cell-matrix adhesion and are crucial for the development of organisms. Interacting proteins, cellular environmental conditions and post-translation modifications regulate the activation state, clustering, and mobility of integrins, thus orchestrating the dynamics of integrin-mediated adhesions. SUMOylation is a type of post-translation modification that attaches a peptide - SUMO - to proteins altering their binding partners, localization and/or function. The participation of SUMOylation in integrin-adhesion complexes hasn’t been addressed. Here, we uncovered a possible role of SUMO modifications in regulating integrin functions in vivo. Using CRISPR-Cas9 in the C. elegans model system, we generated an endogenous integrin mutant, in which the predicted SUMO-receiving lysine was replaced with arginine. The absence of this lysine caused severe phenotypes from embryonic lethality to L1 larval arrest, indicating that SUMO may have a role in regulating integrin function.