Structural and biochemical basis of rapid actin dynamics in Leishmania parasites

Abstract

Actin polymerisation is a force-generating process that is utilized for various functions of cells throughout the eukaryotic kingdom. However, our understanding on the biochemical properties of evolutionary distant actin turnover systems is limited. Here we focus on the actin cytoskeleton of a flagellated unicellular parasite Leishmania major. This organism harbours only a very simple set of actin-regulatory proteins, and lacks for example Capping protein, which controls filament barbed end polymerization, as well as cofilin ‘cofactors', which accelerate filament severing and pointed end depolymerization.