Journal
JOURNAL OF CELLULAR BIOCHEMISTRY
Volume 105, Issue 3, Pages 847-858Publisher
WILEY
DOI: 10.1002/jcb.21880
Keywords
TRANSLATION ELONGATION FACTOR EEF1A; PROTEIN SYNTHESIS; YEAST TWO-HYBRID SYSTEM; SARCOMERIC PROTEIN; MYOSINBINDING PROTEIN-C; SKELETAL MUSCLE; DENERVATION
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Funding
- The Novo Nordic Foundation
- NIH [NS36193]
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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: 847858, 2008. (c) 2008 Wiley-Liss, Inc.
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