Journal article

Minimal requirements for actin filament disassembly revealed by structural analysis of malaria parasite actin-depolymerizing factor 1

Wilson Wong, Colleen T Skau, Danushka S Marapana, Eric Hanssen, Nicole L Taylor, David T Riglar, Elizabeth S Zuccala, Fiona Angrisano, Heather Lewis, Bruno Catimel, Oliver B Clarke, Nadia J Kershaw, Matthew A Perugini, David R Kovar, Jacqueline M Gulbis, Jake Baum

Proceedings of the National Academy of Sciences of the United States of America | NATL ACAD SCIENCES | Published : 2011

Abstract

Malaria parasite cell motility is a process that is dependent on the dynamic turnover of parasite-derived actin filaments. Despite its central role, actin's polymerization state is controlled by a set of identifiable regulators that is markedly reduced compared with those of other eukaryotic cells. In Plasmodium falciparum, the most virulent species that affects humans, this minimal repertoire includes two members of the actin-depolymerizing factor/cofilin (AC) family of proteins, P. falciparum actin-depolymerizing factor 1 (PfADF1) and P. falciparum actin-depolymerizing factor 2. This essential class of actin regulator is involved in the control of filament dynamics at multiple levels, from..

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Grants

Awarded by National Health and Medical Research Council


Awarded by Australian Research Council


Funding Acknowledgements

We thank Andrew Holmes, Dejan Bursac, Trevor Lithgow, Tony Hodder, and Wai-Hong Tham for experimental help and reagents and the staff of the CSIRO Bio21 Collaborative Crystallization Centre and Australian Synchrotron for invaluable assistance. Human erythrocytes were kindly provided by the Red Cross Blood Bank (Melbourne). This work was supported by National Health and Medical Research Council Project Grant 516747 (to J.B.). J.B. is supported through a Future Fellowship (FT100100112) from the Australian Research Council.