JBC Ideal method for primary cell transfection

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J Biol Chem, Vol. 274, Issue 27, 18932-18941, July 2, 1999

Hyperphosphorylation of the Retinoid X Receptor alpha  by Activated c-Jun NH2-terminal Kinases

Sylvie Adam-Stitah, Lucia Penna, Pierre Chambon, and Cécile Rochette-Egly

From the Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS/INSERM/ULP/Collège de France, BP 163, 67404 Illkirch Cedex, CU de Strasbourg, France

The nuclear receptor mouse retinoid X receptor alpha  (mRXRalpha ) was shown to be constitutively phosphorylated in its NH2-terminal A/B region, which contains potential phosphorylation sites for proline-directed Ser/Thr kinases. Mutants for each putative site were generated and overexpressed in transfected COS-1 cells. Constitutively phosphorylated residues identified by tryptic phosphopeptide mapping included serine 22 located in the A1 region that is specific to the RXRalpha 1 isoform. Overexpression and UV activation of the stress-activated kinases, c-Jun NH2-terminal kinases 1 and 2 (JNK1 and JNK2), hyperphosphorylated RXRalpha , resulting in a marked decrease in its electrophoretic mobility. This inducible hyperphosphorylation involved three residues (serines 61 and 75 and threonine 87) in the B region of RXRalpha and one residue (serine 265) in the ligand binding domain (E region). Binding assays performed in vitro with purified recombinant proteins demonstrated that JNKs did not interact with RXRalpha but bound to its heterodimeric partners, retinoic acid receptors alpha  and gamma  (RARalpha and RARgamma ). Hyperphosphorylation by JNKs did not affect the transactivation properties of either RXRalpha homodimers or RXRalpha /RARalpha heterodimers in transfected cultured cells.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.


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