# Microtubule dependent sorting of actin-binding proteins in mitosis

## TL;DR

The paper explores how actin-binding proteins are sorted during cell division in a specific Dictyostelium mutant, revealing their localization patterns and interactions with microtubules.

## Contribution

The study identifies a novel mechanism of actin-binding protein sorting during mitosis, specifically involving Formin B and Arp2/3 complex localization.

## Key findings

- Formin B and Arp2/3 localize to microtubule asters around centrosomes during anaphase.
- These regions are depleted of myosin II and cortexillin, and avoided by cleavage furrows.
- The sorting of actin-binding proteins correlates with planar patterns in multinucleate cells.

## Abstract

The patterns of Formin B and of the Arp2/3 complex formed during mitosis were studied in a mutant of Dictyostelium discoideum that produces multinucleate cells, which divide by the ingression of unilateral cleavage furrows. During cytokinesis the cells of this mutant remain spread on a glass surface where they generate a planar pattern based on the sorting-out of actin-binding proteins. During anaphase, Formin B and Arp2/3 became localized to the regions of microtubule asters around the centrosomes; Formin B in particular in the form of round, quite uniformly covered areas. These areas have been shown to be depleted of myosin II and the actin-filament crosslinker cortexillin, and to be avoided by cleavage furrows on their path into the cell.