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The targeting of mRNA and local protein synthesis is important for the generation and maintenance of cell polarity. As part of the translational machinery as well as an actin/microtubule-binding protein, elongation factor 1α (EF1α) is a candidate linker between the protein translation apparatus and the cytoskeleton. We demonstrate in this work that EF1α colocalizes with β-actin mRNA and F-actin in protrusions of chicken embryo fibroblasts and binds directly to F-actin and β-actin mRNA simultaneously in vitro in actin cosedimentation and enzyme-linked immunosorbent assays. To investigate the role of EF1α in mRNA targeting, we mapped the two actin-binding sites on EF1α at high resolution and defined one site at the N-terminal 49 residues of domain I and the other at the C-terminal 54 residues of domain III. In vitro actin-binding assays and localization in vivo of recombinant full-length EF1α and its various …