Structural basis of rapid actin dynamics in the evolutionarily divergent Leishmania parasite

Tommi Kotila, Hugo Wioland, Muniyandi Selvaraj, Konstantin Kogan, Lina Antenucci, Antoine Jégou, Juha T. Huiskonen, Guillaume Romet-Lemonne and Pekka Lappalainen ()
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Tommi Kotila: University of Helsinki
Hugo Wioland: Université Paris Cité, CNRS, Institut Jacques Monod
Muniyandi Selvaraj: University of Helsinki
Konstantin Kogan: University of Helsinki
Lina Antenucci: University of Helsinki
Antoine Jégou: Université Paris Cité, CNRS, Institut Jacques Monod
Juha T. Huiskonen: University of Helsinki
Guillaume Romet-Lemonne: Université Paris Cité, CNRS, Institut Jacques Monod
Pekka Lappalainen: University of Helsinki

Nature Communications, 2022, vol. 13, issue 1, 1-18

Abstract: Abstract Actin polymerization generates forces for cellular processes throughout the eukaryotic kingdom, but our understanding of the ‘ancient’ actin turnover machineries is limited. We show that, despite > 1 billion years of evolution, pathogenic Leishmania major parasite and mammalian actins share the same overall fold and co-polymerize with each other. Interestingly, Leishmania harbors a simple actin-regulatory machinery that lacks cofilin ‘cofactors’, which accelerate filament disassembly in higher eukaryotes. By applying single-filament biochemistry we discovered that, compared to mammalian proteins, Leishmania actin filaments depolymerize more rapidly from both ends, and are severed > 100-fold more efficiently by cofilin. Our high-resolution cryo-EM structures of Leishmania ADP-, ADP-Pi- and cofilin-actin filaments identify specific features at actin subunit interfaces and cofilin-actin interactions that explain the unusually rapid dynamics of parasite actin filaments. Our findings reveal how divergent parasites achieve rapid actin dynamics using a remarkably simple set of actin-binding proteins, and elucidate evolution of the actin cytoskeleton.

Date: 2022
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DOI: 10.1038/s41467-022-31068-y

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