Research ExplorerPublicationsCharacterization of calmodulin binding to the orphan nuclear...

Characterization of calmodulin binding to the orphan nuclear receptor Errgamma.

Standard

Characterization of calmodulin binding to the orphan nuclear receptor Errgamma. / Hentschke, Moritz; Schulze, Christian; Süsens, Ute; Borgmeyer, Uwe.

In: BIOL CHEM, Vol. 384, No. 3, 3, 2003, p. 473-482.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Hentschke, M, Schulze, C, Süsens, U & Borgmeyer, U 2003, 'Characterization of calmodulin binding to the orphan nuclear receptor Errgamma.', BIOL CHEM, vol. 384, no. 3, 3, pp. 473-482. <http://www.ncbi.nlm.nih.gov/pubmed/12715898?dopt=Citation>

APA

Hentschke, M., Schulze, C., Süsens, U., & Borgmeyer, U. (2003). Characterization of calmodulin binding to the orphan nuclear receptor Errgamma. BIOL CHEM, 384(3), 473-482. [3]. http://www.ncbi.nlm.nih.gov/pubmed/12715898?dopt=Citation

Vancouver

Hentschke M, Schulze C, Süsens U, Borgmeyer U. Characterization of calmodulin binding to the orphan nuclear receptor Errgamma. BIOL CHEM. 2003;384(3):473-482. 3.

Bibtex

@article{4875e2b368ec403aa1e75ecca9680bc6,
title = "Characterization of calmodulin binding to the orphan nuclear receptor Errgamma.",
abstract = "The estrogen receptor-related receptor gamma (ERRgamma/ 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 ERRgamma. In vitro pull-down experiments with calmodulin-Sepharose demonstrated a Ca2+-dependent interaction with cellularly expressed ERRgamma. 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 ERR-gamma 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 calmodulin-independent, transient transfection analysis revealed a Ca2+-influx-dependent ERRgamma-mediated transcriptional activation of a luciferase reporter gene. Thus, we propose that CaM acts as a mediator in the Ca2+-dependent modulation of ERRgamma.",
author = "Moritz Hentschke and Christian Schulze and Ute S{\"u}sens and Uwe Borgmeyer",
year = "2003",
language = "Deutsch",
volume = "384",
pages = "473--482",
journal = "BIOL CHEM",
issn = "1431-6730",
publisher = "Walter de Gruyter GmbH & Co. KG",
number = "3",

}

RIS

TY - JOUR

T1 - Characterization of calmodulin binding to the orphan nuclear receptor Errgamma.

AU - Hentschke, Moritz

AU - Schulze, Christian

AU - Süsens, Ute

AU - Borgmeyer, Uwe

PY - 2003

Y1 - 2003

N2 - The estrogen receptor-related receptor gamma (ERRgamma/ 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 ERRgamma. In vitro pull-down experiments with calmodulin-Sepharose demonstrated a Ca2+-dependent interaction with cellularly expressed ERRgamma. 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 ERR-gamma 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 calmodulin-independent, transient transfection analysis revealed a Ca2+-influx-dependent ERRgamma-mediated transcriptional activation of a luciferase reporter gene. Thus, we propose that CaM acts as a mediator in the Ca2+-dependent modulation of ERRgamma.

AB - The estrogen receptor-related receptor gamma (ERRgamma/ 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 ERRgamma. In vitro pull-down experiments with calmodulin-Sepharose demonstrated a Ca2+-dependent interaction with cellularly expressed ERRgamma. 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 ERR-gamma 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 calmodulin-independent, transient transfection analysis revealed a Ca2+-influx-dependent ERRgamma-mediated transcriptional activation of a luciferase reporter gene. Thus, we propose that CaM acts as a mediator in the Ca2+-dependent modulation of ERRgamma.

M3 - SCORING: Zeitschriftenaufsatz

VL - 384

SP - 473

EP - 482

JO - BIOL CHEM

JF - BIOL CHEM

SN - 1431-6730

IS - 3

M1 - 3

ER -