Molecular basis of functional exchangeability between ezrin and other actin-membrane associated proteins during cytokinesis

The mechanism that mediates the interaction between contractile ring and plasma membrane during cytokinesis remains elusive. We previously found ERM (Ezrin/Radixin/Moesin) proteins, which usually mediate cellular pole contraction, become over-accumulated at cell equator support furrow ingression upon loss of other actin-membrane associated anillin supervillin. In this study, we addressed molecular basis exchangeability ezrin proteins in mediating cortical contraction cytokinesis. depletion supervillin caused over-accumulation membrane-associated FERM domain actin-binding C-terminal (C-term) cleavage furrow, respectively. This finding suggests differentially shares its binding sites with these on actin cytoskeleton or inner surface. Using chimeric mutants, C-term, but not domain, can substitute for corresponding domains proliferation. On hand, either actin/myosin-binding could controlling blebbing poles. Our results highlight specific designs actin- moieties different limited exchangeability, enables them to diverse activities shared interface