The Dictyostelium discoideum FimA protein, unlike yeast and plant fimbrins, is regulated by calcium similar to mammalian plastins.

Autor: Ishida H; Biochemistry Research Group, Department of Biological Sciences, University of Calgary, Calgary, AB, T2N 1N4, Canada., Woodman AG; Biochemistry Research Group, Department of Biological Sciences, University of Calgary, Calgary, AB, T2N 1N4, Canada., Kitada N; Faculty of Advanced Life Science, Hokkaido University, Sapporo, 060-0810, Japan., Aizawa T; Faculty of Advanced Life Science, Hokkaido University, Sapporo, 060-0810, Japan., Vogel HJ; Biochemistry Research Group, Department of Biological Sciences, University of Calgary, Calgary, AB, T2N 1N4, Canada. vogel@ucalgary.ca.
Jazyk: angličtina
Zdroj: Scientific reports [Sci Rep] 2023 Sep 27; Vol. 13 (1), pp. 16208. Date of Electronic Publication: 2023 Sep 27.
DOI: 10.1038/s41598-023-42682-1
Abstrakt: Plastins, also known as fimbrins, are highly conserved eukaryotic multidomain proteins that are involved in actin-bundling. They all contain four independently folded Calponin Homology-domains and an N-terminal headpiece that is comprised of two calcium-binding EF-hand motifs. Since calcium-binding has been shown to be integral to regulating the activity of the three mammalian plastin proteins, we decided to study the properties of the headpiece regions of fimbrins from the model plant Arabidopsis thaliana, the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe and the amoeba Dictyostelium discoideum. Of these protein domains only the FimA headpiece from the amoeba protein possesses calcium binding properties. Structural characterization of this protein domain by multidimensional NMR and site-directed mutagenesis studies indicates that this EF-hand region of FimA also contains a regulatory 'switch helix' that is essential to regulating the activity of the human L-plastin protein. Interestingly this regulatory helical region seems to be lacking in the plant and yeast proteins and in fimbrins from all other nonmotile systems. Typical calmodulin antagonists can displace the switch-helix from the FimA headpiece, suggesting that such drugs can deregulate the Ca 2+ -regulation of the actin-bunding in the amoeba, thereby making it a useful organism for drug screening against mammalian plastins.
(© 2023. Springer Nature Limited.)
Databáze: MEDLINE
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