Twinfilin modulates tissue contractility through uncapping of capping protein in C. elegans.

ABSTRACT: The actin cytoskeleton is dynamically remodeled by conserved regulators to control cell and tissue mechanics. Although many of these proteins are well studied, their roles in driving tissue-specific contractility remains unclear. Twinfilin, an actin uncapper and depolymerase, has not previously been linked to tissue contractility. Here, we show that the sole twinfilin ortholog in C. elegans, TWF-2, modulates actomyosin contractility in the spermatheca. TWF-2 localizes to the spermathecal cortex through interactions with α-spectrin (SPC-1) and β-spectrin (UNC-70). In vitro, TWF-2 inhibits depolymerization of ADP-actin filaments and modestly promotes depolymerization of ADP-Pi-actin filaments, while also rapidly displacing capping protein (CAP-1 and CAP-2) from filament barbed ends. In vivo,

SUBMITTER: Saini A 

PROVIDER: S-EPMC12746075 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature