Aurora B spatially regulates EB3 phosphorylation to coordinate daughter cell adhesion with cytokinesis.

ABSTRACT: During mitosis, human cells round up, decreasing their adhesion to extracellular substrates. This must be quickly reestablished by poorly understood cytoskeleton remodeling mechanisms that prevent detachment from epithelia, while ensuring the successful completion of cytokinesis. Here we show that the microtubule end-binding (EB) proteins EB1 and EB3 play temporally distinct roles throughout cell division. Whereas EB1 was involved in spindle orientation before anaphase, EB3 was required for stabilization of focal adhesions and coordinated daughter cell spreading during mitotic exit. Additionally, EB3 promoted midbody microtubule stability and, consequently, midbody stabilization necessary for efficient cytokinesis. Importantly, daughter cell adhesion and cytokinesis completion were spatial

SUBMITTER: Ferreira JG 

PROVIDER: S-EPMC3664705 | biostudies-literature | 2013 May

REPOSITORIES: biostudies-literature