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Serine 27, a Human Retinoid X Receptor \alpha Residue, Phosphorylated by Protein Kinase A Is Essential for CyclicAMP-Mediated Downregulation of $RXR\alpha$ Function

Harish, S and Ashok, MS and Khanam, Tasneem and Rangarajan, PN (2000) Serine 27, a Human Retinoid X Receptor \alpha Residue, Phosphorylated by Protein Kinase A Is Essential for CyclicAMP-Mediated Downregulation of $RXR\alpha$ Function. In: Biochemical and Biophysical Research Communications, 279 (3). pp. 853-857.

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Abstract

Retinoid X Receptor \alpha $(RXR \alpha$), a member of the steroid-thyroid hormone receptor super family, is phosphorylated in vitro by protein kinase A (PKA) and this phosphorylation is inhibited in presence of PKA inhibitory peptide. Analysis of various deletion mutants of $RXR \alpha$ indicate that the amino-terminal A/B domain is the target for PKA phosphorylation. An $RXR \alpha$ mutant in which serine residue 27 is mutated to alanine is no longer phosphorylated by PKA. In vivo transfection experiments in COS cells indicate that cyclicAMP represses retinoic acid-mediated transcriptional activation of $RXR\alpha$ and this repression is mediated by serine 27. These results indicate that serine 27 of $RXR\alpha$ is an unique target for phosphorylation by PKA in vitro and it has an important role in the crosstalk between $RXR\alpha$ and cyclicAMP signalling pathways.

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Academic Press.
Keywords: RXRα;Protein kinaseA;Phosphorylation;CyclicAMP;Transcription
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 16 Oct 2007
Last Modified: 19 Sep 2010 04:40
URI: http://eprints.iisc.ernet.in/id/eprint/12171

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