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A more recent version of this article appeared on February 1, 2002
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Submitted on March 28, 2001
Revised on October 26, 2001
Accepted on November 14, 2001
1 Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, NY 10461 (Present address: Center for Cell Biology and Cancer Research, Albany Medical College, 47 New Scotland Avenue, Albany, NY 12208)
2 Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, NY 10461
3 Analytical Imaging Facility, Albert Einstein College of Medicine, 1300 Morris Park Avenue, NY 10461
* Corresponding author. E-mail address: liug{at}mail.amc.edu.
The targeting of messenger RNA 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 1 alpha (EF1alpha) is a candidate linker between the protein translation apparatus and the cytoskeleton. We demonstrate in this work that EF1alpha colocalizes with beta-actin mRNA and F-actin in protrusions of chicken embryo fibroblasts (CEFs) and binds directly to F-actin and beta-actin mRNA simultaneously in vitro in actin co-sedimentation and ELISA assays. To investigate the role of EF1alpha in mRNA targeting we mapped the two actin binding sites on EF1alpha 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 EF1alpha and its various truncates demonstrated that the C-terminus of domain III was the dominant actin binding site both in vitro and in vivo. We propose that EF1alpha-F-actin complex is the scaffold that is important for beta-actin mRNA anchoring. Disruption of this complex would lead to delocalization of the mRNA. This hypothesis was tested by using two dominant negative polypeptides: the actin binding domain III of EF1alpha and the EF1alpha binding site of yeast Bni1p, a protein that inhibits EF1alpha binding to F-actin and also is required for yeast mRNA localization. We demonstrate that either Domain III of EF1alpha or the EF1alpha binding site of Bni1p inhibits EF1alpha binding to beta-actin mRNA in vitro and causes delocalization of beta-actin mRNA in CEFs. Taken together, these results implicate EF1alpha in the anchoring of beta-actin mRNA to the protrusion in crawling cells.
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