Novosylna, O, Doyle, A, Murphy, MF, Vlasenko, D, Negrutskii, B and El'skaya, A (2016) Comparison of the ability of mammalian eEF1A1 and its oncogenic variant eEF1A2 to interact with actin and calmodulin. Biological Chemistry, 398 (1). ISSN 1431-6730

Preview

Text 2017 Biol.Chem.pdf - Accepted Version Download (994kB) | Preview

Abstract

The question as to why a protein exerts oncogenic properties is answered mainly by well-established ideas that these proteins interfere with cellular signaling pathways. However, the knowledge about structural and functional peculiarities of the oncoproteins causing these effects is far from comprehensive. The 97.5% homologous tissue-specific A1 and A2 isoforms of mammalian translation elongation factor eEF1A represent an interesting model to study a difference between protein variants of a family that differ in oncogenic potential. We propose that the different oncogenic impact of A1 and A2 might be explained by differences in their ability to communicate with their respective cellular partners. Here we probed this hypothesis by studying the interaction of eEF1A with two known partners – calmodulin and actin. Indeed, an inability of the A2 isoform to interact with calmodulin is shown, while calmodulin is capable of binding A1 and interferes with its tRNA-binding and actin-bundling activities in vitro. Both A1 and A2 variants revealed actin-bundling activity; however, the form of bundles formed in the presence of A1 or A2 was distinctly different. Thus, a potential inability of A2 to be controlled by Ca2+-mediated regulatory systems is revealed.

Item Type:	Article
Uncontrolled Keywords:	0601 Biochemistry And Cell Biology
Subjects:	Q Science > QD Chemistry
Divisions:	Engineering
Publisher:	De Gruyter
Date Deposited:	19 Sep 2018 09:50
Last Modified:	04 Sep 2021 02:29
DOI or ID number:	10.1515/hsz-2016-0172
URI:	https://researchonline.ljmu.ac.uk/id/eprint/9259

View Item