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UAP56 is an important regulator of protein synthesis and growth in cardiomyocytes.

Authors: Sahni, A  Wang, N  Alexis, JD 
Citation: Sahni A, etal., Biochem Biophys Res Commun. 2010 Feb 26;393(1):106-10. doi: 10.1016/j.bbrc.2010.01.093. Epub 2010 Jan 29.
Pubmed: (View Article at PubMed) PMID:20116367
DOI: Full-text: DOI:10.1016/j.bbrc.2010.01.093

UAP56, an ATP dependent RNA helicase that also has ATPase activity, is a DExD/H box protein that is phylogenetically grouped with the eukaryotic initiation factor eIF4A, the prototypical member of the DExD/H box family of helicases. UAP56, also known as BAT1, is an essential RNA splicing factor required for spliceosome assembly and mRNA export but its role in protein synthesis is not known. Here we demonstrate that UAP56 regulates protein synthesis and growth in cardiomyocytes. We found that wild-type (WT) UAP56 increased serum induced protein synthesis in HeLa cells. UAP56 mutants lacking ATPase and/or helicase activity inhibited protein synthesis compared with WT UAP56, suggesting that the ATPase and RNA helicase activity of UAP56 is important for protein synthesis. UAP56 siRNA inhibited phenylephrine (PE) induced protein synthesis in cardiomyocytes and inhibited PE induced cardiomyocyte hypertrophy. Our data demonstrate that UAP56 is an important regulator of protein synthesis and plays an important role in the regulation of cardiomyocyte growth.


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CRRD Object Information
CRRD ID: 10401141
Created: 2015-09-29
Species: All species
Last Modified: 2015-09-29
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.