Translation elongation factor eEF1A binds to a novel myosin binding protein-C-like protein

• Published in: Journal of cellular biochemistry 2008-10, Vol.105 (3), p.847-858
• Main Authors: Mansilla, Francisco, Dominguez, Carlota A.G., Yeadon, James E., Corydon, Thomas J., Burden, Steven J., Knudsen, Charlotte R.
• Format: Article
• Language: English
• Subjects: Adaptor Proteins, Signal Transducing; Amino Acid Sequence; Animals; Binding Sites; Carrier Proteins - chemistry; Carrier Proteins - genetics; Carrier Proteins - metabolism; Cells, Cultured; denervation; Humans; Mice; Microscopy, Confocal; Molecular Sequence Data; myosin-binding protein-C; Peptide Elongation Factor 1 - genetics; Peptide Elongation Factor 1 - metabolism; Protein Biosynthesis - genetics; protein synthesis; Saccharomyces cerevisiae - genetics; Saccharomyces cerevisiae - metabolism; sarcomeric protein; Sequence Alignment; skeletal muscle; translation elongation factor eEF1A; yeast two-hybrid system
• ISSN: 0730-2312; 1097-4644
• DOI: 10.1002/jcb.21880

Eukaryotic translation elongation factor 1A (eEF1A) is a guanine‐nucleotide binding protein, which transports aminoacylated tRNA to the ribosomal A site during protein synthesis. In a yeast two‐hybrid screening of a human skeletal muscle cDNA library, a novel eEF1A binding protein, immunoglobulin‐like and fibronectin type III domain containing 1 (IGFN1), was discovered, and its interaction with eEF1A was confirmed in vitro. IGFN1 is specifically expressed in skeletal muscle and presents immunoglobulin I and fibronectin III sets of domains characteristic of sarcomeric proteins. IGFN1 shows sequence and structural homology to myosin binding protein‐C fast and slow‐type skeletal muscle isoforms. IGFN1 is substantially upregulated during muscle denervation. We propose a model in which this increased expression of IGFN1 serves to down‐regulate protein synthesis via interaction with eEF1A during denervation. J. Cell. Biochem. 105: 847–858, 2008. © 2008 Wiley‐Liss, Inc.