Twinfilin is a potent uncapper of actin capping protein and modulates actomyosin contractility in the <i>C. elegans</i> spermatheca.

ABSTRACT: The actin cytoskeleton is dynamically remodelled by conserved regulators to control cellular and tissue mechanics. While the functions of these proteins are well studied, how they drive 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, regulates actomyosin contractility in the spermatheca. TWF-2 localizes to the spermathecal cortex via interactions with α-spectrin (SPC-1) and β-spectrin (UNC-70). In vitro, TWF-2 promotes barbed-end depolymerization and rapidly removes CAP-1 from actin filaments. In vivo, embryonic lethality caused by CAP-1 depletion is partially rescued by simultaneous loss of TWF-2. Si

SUBMITTER: Saini A 

PROVIDER: S-EPMC12262733 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature