The MO25 protein Pmo25 functions in contractile ring stability and Sid2 localization during cytokinesis.

ABSTRACT: Mouse protein-25 (MO25) family proteins are crucial in development and morphogenesis from plants to humans. The fission yeast MO25 protein Pmo25 is essential for cell polarity and division. However, how Pmo25 regulates cytokinesis remains largely unknown. Here, we found that the actomyosin contractile ring and septum formation were defective during cytokinesis in pmo25 mutants. Pmo25 physically and genetically interacted with the myosin-II light chain Cdc4, which is essential for the contractile-ring assembly and function. Additionally, pmo25 mutations had synthetic genetic interactions with all other tested mutations in contractile-ring proteins. Moreover, Pmo25 colocalized with the NDR kinase Sid2 and participated in its recruitment to the division plane. Furthermore, Pmo25

SUBMITTER: Ye Y 

PROVIDER: S-EPMC12803953 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature