Structural highlights
Function
[CADF1_PLAF7] Not involved in actin polymerisation, instead functions to stimulate nucleotide exchange on monomeric actin and influence turnover of the small amount of cytosolic actin microfilaments. Essential for erythrocytic schizogony (By similarity).[UniProtKB:P86292]
Publication Abstract from PubMed
Apicomplexan 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.
Crystal structures explain functional differences in the two actin depolymerization factors of the malaria parasite.,Singh BK, Sattler JM, Chatterjee M, Huttu J, Schuler H, Kursula I J Biol Chem. 2011 Aug 12;286(32):28256-64. PMID:21832095[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Singh BK, Sattler JM, Chatterjee M, Huttu J, Schuler H, Kursula I. Crystal structures explain functional differences in the two actin depolymerization factors of the malaria parasite. J Biol Chem. 2011 Aug 12;286(32):28256-64. PMID:21832095 doi:10.1074/jbc.M111.211730
