Modification of the retinoic acid signaling pathway by the catalytic subunit of protein kinase-A
Autor: | Yang-Won Kim, J. I. Huggenvik, Raghubir P. Sharma, Michael W. Collard |
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Rok vydání: | 1993 |
Předmět: |
Chloramphenicol O-Acetyltransferase
Receptors Retinoic Acid Recombinant Fusion Proteins Molecular Sequence Data Retinoic acid Tretinoin Biology Transfection Cell Line Retinoic acid-inducible orphan G protein-coupled receptor chemistry.chemical_compound Endocrinology Cyclic AMP medicine Humans Phosphorylation Promoter Regions Genetic Protein kinase A Molecular Biology Transcription factor Base Sequence General Medicine Molecular biology Retinoic acid receptor chemistry Signal transduction Carrier Proteins Protein Kinases HeLa Cells Plasmids Signal Transduction medicine.drug |
Zdroj: | Molecular Endocrinology. 7:543-550 |
ISSN: | 1944-9917 0888-8809 |
Popis: | Retinoic acid receptors (RARs) are ligand-activated nuclear transcription factors that belong to the steroid-thyroid hormone receptor superfamily. We have used the transient transfection of a retinoic acid-responsive reporter plasmid (RARECAT) to investigate the potential interactions between the retinoic acid (RA) and cAMP signaling pathways. Cotransfections of expression plasmids for the catalytic (C) subunits of cAMP-dependent protein kinase with RARECAT showed ligand-independent activation in both CV-1 and HeLa cells and a further 2-fold increase in RARECAT activity in the presence of RA. In CV-1 cells, cotransfections of the expression plasmids for RAR and the C-subunits produced increases in RARECAT activity (12- and 8-fold in the absence of ligand and 21- and 15-fold in the presence of RA for the C alpha- and C beta-isoforms, respectively). Cotransfections of both the C beta-subunit and RAR expression plasmids in HeLa cells produced 22- and 114-fold increases in RARECAT activity in the absence and presence of RA, respectively. These results provide evidence to suggest that the RA and cAMP signaling pathways are coupled, and signaling cross-talk may occur through the direct phosphorylation of RARs by the C-subunit as indicated by in vitro phosphorylation of the receptor. |
Databáze: | OpenAIRE |
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