The binding of eukaryotic translation elongation factor 1A (eEF1A) to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression. Using the yeast Saccharomyces cerevisiae, we have established an in vivo assay that directly identifies specific regions and residues of eEF1A responsible for actin interactions and bundling. Using a unique genetic screen, we isolated a series of eEF1A mutants with reduced actin bundling activity. These mutations alter actin cytoskeleton organization but not translation, indicating that these are separate functions of eEF1A. This demonstrates for the first time a direct consequence of eEF1A on cytoskeletal organization in vivo and the physiological significance of this interaction.
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The authors acknowledge the assistance of the Cancer Institute of New Jersey/Environmental and Occupational Health Sciences Institute Analytical Cytometry Image Analysis, the Robert Wood Johnson Medical School (RWJMS) DNA Core Facility sequencing laboratory and the fluorescence microscopy laboratory in the RWJMS Department of Pharmacology. This research was supported by a grant from the US National Institutes of Health (GM62789 to T.G.K.).
The authors declare no competing financial interests.
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Gross, S., Kinzy, T. Translation elongation factor 1A is essential for regulation of the actin cytoskeleton and cell morphology. Nat Struct Mol Biol 12, 772–778 (2005). https://doi.org/10.1038/nsmb979
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