Video Experimental Relacionado

Updated: Jan 20, 2026

Cell Division: Mitosis and Cytokinesis

Cell Division: Mitosis and Cytokinesis

La proteína Pmo25 de MO25 funciona en la estabilidad del anillo contráctil y la localización de Sid2 durante la

Yanfang Ye^1,2, Sha Zhang¹, Jack R Gregory^1,3,4

¹Department of Molecular Genetics, The Ohio State University, Columbus, OH 43210, USA.

|January 19, 2026

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 directly bound the Munc13/UNC-13 protein Ync13 and modulated the secretion of glucanase Eng1 to the division site for daughter-cell separation. Our data provide insight into how Pmo25 regulates cytokinesis and suggest that the conserved MO25 proteins can link various steps of cytokinesis.

Palabras clave:

aspectos organizativos de la biología celular Proteína aspectos estructurales de las proteínas

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