The Ski protein can inhibit ligand induced RARalpha and HDAC3 degradation in the retinoic acid signaling pathway

Recent data has implicated the Ski protein as being a physiologically relevant negative regulator of signaling by retinoic acid (RA). The mechanism by which Ski represses RA signaling is unknown. Co-immunoprecipitation and immunofluorescence assay showed that Ski and RARalpha are in the same complex...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2009-05, Vol.383 (1), p.119-124
Main Authors: Zhao, Hong-Ling, Ueki, Nobuhide, Marcelain, Katherine, Hayman, Michael J
Format: Article
Language:English
Subjects:
Animals
Cell Line
DNA-Binding Proteins - genetics
DNA-Binding Proteins - metabolism
Histone Deacetylases - metabolism
Humans
Immunoprecipitation
Ligands
Protein Stability
Proto-Oncogene Proteins - genetics
Proto-Oncogene Proteins - metabolism
Receptors, Retinoic Acid - metabolism
Retinoic Acid Receptor alpha
Signal Transduction
Tretinoin - metabolism
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Summary:Recent data has implicated the Ski protein as being a physiologically relevant negative regulator of signaling by retinoic acid (RA). The mechanism by which Ski represses RA signaling is unknown. Co-immunoprecipitation and immunofluorescence assay showed that Ski and RARalpha are in the same complex in both the absence and presence of RA, which makes Ski different from other corepressors. We determined that Ski can stabilize RARalpha and HDAC3. These results suggest that Ski represses RA signaling by stabilizing corepressor complex.
ISSN:1090-2104
DOI:10.1016/j.bbrc.2009.03.141