Aim44p regulates phosphorylation of Hof1p to promote contractile ring closure during cytokinesis in budding yeast.

ABSTRACT: Whereas actomyosin and septin ring organization and function in cytokinesis are thoroughly described, little is known regarding the mechanisms by which the actomyosin ring interacts with septins and associated proteins to coordinate cell division. Here we show that the protein product of YPL158C, Aim44p, undergoes septin-dependent recruitment to the site of cell division. Aim44p colocalizes with Myo1p, the type II myosin of the contractile ring, throughout most of the cell cycle. The Aim44p ring does not contract when the actomyosin ring closes. Instead, it forms a double ring that associates with septin rings on mother and daughter cells after cell separation. Deletion of AIM44 results in defects in contractile ring closure. Aim44p coimmunoprecipitates with Hof1p, a conserved F-BAR protei

SUBMITTER: Wolken DM 

PROVIDER: S-EPMC3952846 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature