ABSTRACT
Cytokinetic abscission is the terminal step of cell division, leading to the physical separation of the two daughter cells. The exact mechanism mediating the final scission of the intercellular bridge connecting the dividing cells is not fully understood, but requires the local constriction of endosomal sorting complex required for transport (ESCRT)-III-dependent helices, as well as remodelling of lipids and the cytoskeleton at the site of abscission. In particular, microtubules and actin filaments must be locally disassembled for successful abscission. However, the mechanism that actively removes actin during abscission is poorly understood. In this Commentary, we will focus on the latest findings regarding the emerging role of the MICAL family of oxidoreductases in F-actin disassembly and describe how Rab GTPases regulate their enzymatic activity. We will also discuss the recently reported role of MICAL1 in controlling F-actin clearance in the ESCRT-III-mediated step of cytokinetic abscission. In addition, we will highlight how two other members of the MICAL family (MICAL3 and MICAL-L1) contribute to cytokinesis by regulating membrane trafficking. Taken together, these findings establish the MICAL family as a key regulator of actin cytoskeleton dynamics and membrane trafficking during cell division.
Footnotes
Funding
This work of our laboratories been supported by Institut Pasteur, Centre National de la Recherche Scientifique (CNRS), Fondation pour la Recherche Médicale (FRM) (Equipe FRM DEQ20120323707), Institut National Du Cancer (INCa) (2014-1-PL BIO-04-IP1), Agence Nationale de la Recherche (ANR) (AbCyStem, CytoSign) and the IXCORE Foundation to A.E.; by grants from the CNRS and INCa (2014-1-PL BIO-04-ICR-1) to A.H. The A.H. team is part of by the Labex CelTisPhyBio 11-LBX-0038, which is part of the Initiative d'Excellence at PSL Research University (ANR-10-IDEX-0001-02 PSL).
