Cdc15

Cdc15 is a protein encoded by the cdc15 gene in the fission yeast Schizosaccharomyces pombe. It is an essential component of the cytokinetic contractile ring and functions as a scaffold that coordinates the assembly and constriction of the ring during cell division. Cdc15 localizes to the medial cortex during mitosis and helps organize the recruitment of other ring factors to the division site.

Structurally, Cdc15 is an F-BAR domain-containing protein with a modular architecture that typically includes an N-terminal F-BAR domain, a central coiled-coil region, and a C-terminal interaction module. This arrangement supports membrane association, self-assembly, and binding to a variety of partner proteins. Through these domains, Cdc15 serves as a platform for recruiting actin filaments, myosin II components, and other cytokinetic factors necessary for ring maturation and constriction.

Functionally, Cdc15 contributes to the formation and stabilization of the contractile ring and helps coordinate the transition from ring assembly to constriction. It interacts with multiple cytokinetic proteins and is regulated by cell-cycle–dependent signaling to ensure proper timing and localization at the division site.

Genetically, Cdc15 is essential for successful cytokinesis in S. pombe; loss or malfunction leads to defects in contractile ring formation and cell division. The protein is a representative member of the Cdc15 family of F-BAR–domain proteins found in fungi and serves as a model for understanding the molecular organization of cytokinetic machinery in eukaryotes.