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

• Type: Article in International Scientific Journal
• Date: 2013

Authors

JG Ferreira (Author) FMUP

Journal

Title: Journal of Cell Biology

Vol. 201 No. 5

Pages: 709-724

ISSN: 0021-9525

Publisher: Rockefeller University Press

Indexing

ISI Web of Knowledge - 36 Citations

ISI Web of Science

Scopus - 38 Citations

Scientific classification

CORDIS: Natural sciences > Biological sciences > Biology > Human biology

FOS: Natural sciences > Biological sciences

Other information

Authenticus ID: P-005-0NE

DOI: 10.1083/jcb.201301131

Abstract (EN): 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 micro-tubule 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 spatially regulated by distinct states of EB3 phosphorylation on serine 176 by Aurora B. This EB3 phosphorylation was enriched at the midbody and shown to control cortical microtubule growth. These findings uncover differential roles of EB proteins and explain the importance of an Aurora B phosphorylation gradient for the spatiotemporal regulation of microtubule function during mitotic exit and cytokinesis.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 16