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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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.|
|Department/Centre:||Division of Biological Sciences > Biochemistry|
|Date Deposited:||16 Oct 2007|
|Last Modified:||19 Sep 2010 04:40|
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