Aberrant association of promyelocytic leukemia protein-retinoic acid receptor-alpha with coactivators contributes to its ability to regulate gene expression.
The aberrant association of promyelocytic leukemia protein-retinoic acid receptor-alpha (PML-RARalpha) with corepressor complexes is generally thought to contribute to the ability of PML-RARalpha to regulate transcription. We report here that PML-RARalpha acquires aberrant association with coactivators. We show that endogenous PML-RARalpha interacts with the histone acetyltransferases CBP, p300, and SRC-1 ... in a hormoneindependent manner, an association not seen for RARalpha. This hormone-independent coactivator binding activity requires an intact ligand-binding domain and the NR box of the coactivators. Confocal microscopy studies demonstrate that exogenous PML-RARalpha sequesters and colocalizes with coactivators. These observations correlate with the ability of PML-RARalpha to attenuate the transcription activation of the Notch signaling downstream effector, CBF1, and of the glucocorticoid receptor. This includes attenuation of the glucocorticoid-induced leucine zipper (GILZ) and FLJ25390 target genes of the endogenous glucocorticoid receptor. Furthermore, treatment of NB4 cells with all-trans-retinoic acid, which promotes PML-RARalpha degradation, resulted in increased activation of GILZ. On the basis of these findings, we propose a model in which the hormone-independent association between PML-RARalpha and coactivators contributes to its ability to regulate gene expression.
Mesh Terms:
Animals, Cell Line, Gene Expression Regulation, Neoplastic, Glutathione Transferase, HL-60 Cells, Humans, Microscopy, Fluorescence, Models, Biological, Neoplasm Proteins, Nuclear Proteins, Plasmids, Protein Binding, Protein Structure, Tertiary, Receptors, Notch, Receptors, Retinoic Acid, Signal Transduction, Transcription Factors, Tumor Suppressor Proteins
Animals, Cell Line, Gene Expression Regulation, Neoplastic, Glutathione Transferase, HL-60 Cells, Humans, Microscopy, Fluorescence, Models, Biological, Neoplasm Proteins, Nuclear Proteins, Plasmids, Protein Binding, Protein Structure, Tertiary, Receptors, Notch, Receptors, Retinoic Acid, Signal Transduction, Transcription Factors, Tumor Suppressor Proteins
J. Biol. Chem.
Date: Jun. 22, 2007
PubMed ID: 17475621
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