Oxidative stress elicits the remodeling of vimentin filaments into biomolecular condensates.

ABSTRACT: The intermediate filament protein vimentin performs an essential role in cytoskeletal interplay and dynamics, mechanosensing and cellular stress responses. In pathology, vimentin is a key player in tumorigenesis, fibrosis and infection. Vimentin filaments undergo distinct and versatile reorganizations, and behave as redox sensors. The vimentin monomer possesses a central α-helical rod domain flanked by N- and C-terminal low complexity domains. Interactions between this type of domains play an important function in the formation of phase-separated biomolecular condensates, which in turn are critical for the organization of cellular components. Here we show that several oxidants, including hydrogen peroxide and diamide, elicit the remodeling of vimentin filaments into small particles. Oxidat

SUBMITTER: Martinez-Cenalmor P 

PROVIDER: S-EPMC11338992 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature