Crystal structures explain functional differences in the two actin depolymerization factors of the malaria parasite.
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AbstractApicomplexan parasites, such as the malaria-causing Plasmodium, utilize an actin-based motor for motility and host cell invasion. The actin filaments of these parasites are unusually short, and actin polymerization is under strict control of a small set of regulatory proteins, which are poorly conserved with their mammalian orthologs. Actin depolymerization factors (ADFs) are among the most important actin regulators, affecting the rates of filament turnover in a multifaceted manner. Plasmodium has two ADFs that display low sequence homology with each other and with the higher eukaryotic family members. Here, we show that ADF2, like canonical ADF proteins but unlike ADF1, binds to both globular and filamentous actin, severing filaments and inducing nucleotide exchange on the actin monomer. The crystal structure of Plasmodium ADF1 shows major differences from the ADF consensus, explaining the lack of F-actin binding. Plasmodium ADF2 structurally resembles the canonical members of the ADF/cofilin family.
CitationCrystal structures explain functional differences in the two actin depolymerization factors of the malaria parasite. 2011, 286 (32):28256-64 J. Biol. Chem.
The following license files are associated with this item:
- A mechanism for actin filament severing by malaria parasite actin depolymerizing factor 1 via a low affinity binding interface.
- Authors: Wong W, Webb AI, Olshina MA, Infusini G, Tan YH, Hanssen E, Catimel B, Suarez C, Condron M, Angrisano F, Nebi T, Kovar DR, Baum J
- Issue date: 2014 Feb 14
- Crystallization and preliminary structural characterization of the two actin-depolymerization factors of the malaria parasite.
- Authors: Huttu J, Singh BK, Bhargav SP, Sattler JM, Schüler H, Kursula I
- Issue date: 2010 May 1
- Structural differences explain diverse functions of Plasmodium actins.
- Authors: Vahokoski J, Bhargav SP, Desfosses A, Andreadaki M, Kumpula EP, Martinez SM, Ignatev A, Lepper S, Frischknecht F, Sidén-Kiamos I, Sachse C, Kursula I
- Issue date: 2014 Apr
- Minimal requirements for actin filament disassembly revealed by structural analysis of malaria parasite actin-depolymerizing factor 1.
- Authors: Wong W, Skau CT, Marapana DS, Hanssen E, Taylor NL, Riglar DT, Zuccala ES, Angrisano F, Lewis H, Catimel B, Clarke OB, Kershaw NJ, Perugini MA, Kovar DR, Gulbis JM, Baum J
- Issue date: 2011 Jun 14
- Disassembly activity of actin-depolymerizing factor (ADF) is associated with distinct cellular processes in apicomplexan parasites.
- Authors: Haase S, Zimmermann D, Olshina MA, Wilkinson M, Fisher F, Tan YH, Stewart RJ, Tonkin CJ, Wong W, Kovar DR, Baum J
- Issue date: 2015 Sep 1