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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

12 Issues per year


IMPACT FACTOR 2015: 2.710
Rank 142 out of 289 in category Biochemistry & Molecular Biology in the 2015 Thomson Reuters Journal Citation Report/Science Edition

SCImago Journal Rank (SJR) 2015: 1.607
Source Normalized Impact per Paper (SNIP) 2015: 0.751
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Online
ISSN
1437-4315
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Volume 384, Issue 3 (Mar 2003)

Issues

Characterization of Calmodulin Binding to the Orphan Nuclear Receptor ERRγ

M. Hentschke / C. Schulze / U. Süsens / U. Borgmeyer
Published Online: 2005-06-01 | DOI: https://doi.org/10.1515/BC.2003.053

Abstract

The estrogen receptorrelated receptor γ (ERγ/ERR3/NR3B3), a member of the nuclear receptor superfamily, activates transcription in the absence of ligands. In order to identify ligand-independent mechanisms of activation, we tested whether calmodulin (CaM), a key regulator of numerous cellular processes and a predominant intracellular receptor for Ca2+-signals, interacts with ERRγ. In vitro pulldown experiments with calmodulin-Sepharose demonstrated a Ca2+-dependent interaction with cellularly expressed ERRγ. As shown by truncation analysis, the CaM binding site is highly unusual in that it is composed of two discontinuous elements. Moreover, by surface plasmon resonance (SPR) biosensor technology, we detected a direct interaction of immobilized bacterially expressed ERRγ fusion protein with Ca2+-calmodulin. This is best described by a model which assumes a conformational change of the initially formed complex to a more stable form. Whereas in vitro DNA binding was calmodulinindependent, transient transfection analysis revealed a Ca2+-influxdependent ERRγmediated transcriptional activation of a luciferase reporter gene. Thus, we propose that CaM acts as a mediator in the Ca2+-dependent modulation of ERRγ.

About the article

Published Online: 2005-06-01

Published in Print: 2003-03-14


Citation Information: Biological Chemistry, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2003.053. Export Citation

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