Nuclear protein FNBP4: A novel inhibitor of non-diaphanous formin FMN1-mediated actin cytoskeleton dynamics.

ABSTRACT: Formin1 (FMN1), a member of the non-diaphanous formin family, is essential for development and neuronal function. Unlike diaphanous-related formins, FMN1 is not subject to canonical autoinhibition through the DID and DAD domains, nor is it activated by Rho GTPase binding. Recent studies suggest that formins also play roles in the nucleus, influencing DNA damage response and transcriptional regulation. However, the mechanisms regulating formins particularly non-diaphanous ones like FMN1 remain poorly understood. Our previous research identified the interaction between FMN1 and formin-binding protein 4 (FNBP4), prompting further investigation into its functional role in regulating actin dynamics. Results reveal that FNBP4 inhibits FMN1-mediated actin assembly in vitro. It is shown that FNBP4

SUBMITTER: Das S 

PROVIDER: S-EPMC12159680 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature