Serine 157, a Retinoic Acid Receptor α Residue Phosphorylated by Protein Kinase C in Vitro, Is Involved in RXR·RARα Heterodimerization and Transcriptional Activity
Open Access
- 1 December 1999
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 274 (53) , 38225-38231
- https://doi.org/10.1074/jbc.274.53.38225
Abstract
No abstract availableKeywords
This publication has 42 references indexed in Scilit:
- H11-H12 Loop Retinoic Acid Receptor Mutants Exhibit Distinct trans-Activating and trans-Repressing Activities in the Presence of Natural or Synthetic RetinoidsBiochemistry, 1998
- Estrogens Cause Rapid Activation of IP3-PKC-α Signal Transduction Pathway in HEPG2 CellsBiochemical and Biophysical Research Communications, 1998
- Inhibition of Adipogenesis Through MAP Kinase-Mediated Phosphorylation of PPARγScience, 1996
- Protein Kinase C δ Activates the MEK-ERK Pathway in a Manner Independent of Ras and Dependent on RafJournal of Biological Chemistry, 1996
- Identification of Amino Acids Critical for the DNA Binding and Dimerization Properties of the Human Retinoic Acid Receptor αPublished by Elsevier ,1996
- Protein kinase C isozymes and substratesCurrent Opinion in Cell Biology, 1996
- Retinoic acid stimulates the protein kinase C pathway before activation of its β-nuclear receptor during human teratocarcinoma differentiationBiochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1993
- Deletion of the regulatory domain of protein kinase C alpha exposes regions in the hinge and catalytic domains that mediate nuclear targeting.The Journal of cell biology, 1992
- The proteolysis of membrane-associated protein kinase C as a possible component of the signalling pathway leading to c-myc induction in B lymphocytesCellular Signalling, 1991
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976