The Binding of CSL Proteins to Either Co-Activators or Co-Repressors Protects from Proteasomal Degradation Induced by MAPK-Dependent Phosphorylation
Abstract
:1. Introduction
2. Results
2.1. H Binding-Defective Su(H)LLL Protein Is Degraded More Rapidly Than Wildtype Su(H) Protein
2.2. Su(H) Protein Is Subjected to Proteasomal Degradation
2.3. Su(H) Protein Levels Depend on the Presence of H
2.4. Su(H)–H Protein Interactions Are Short-Lived
2.5. Protection of Su(H) by Co-Activator and Co-Repressor Alike
2.6. RBPJ Might Be Stabilised by Cofactors as well
2.7. Stability of Su(H) Is Regulated by MAPK-Dependent Phosphorylation
3. Discussion
4. Materials and Methods
4.1. Generation of Su(H) and RBPJ Constructs
4.2. Fly Work
4.2.1. Husbandry and Transgenic Lines
4.2.2. Heat Shock Regimen
4.2.3. DTS5 Experiment
4.2.4. Immunocytochemistry of Fly Tissue
4.3. Cell Culture Experiments
4.4. Yeast Two-Hybrid Experiments
Supplementary Materials
Author Contributions
Funding
Institutional Review Board Statement
Informed Consent Statement
Data Availability Statement
Acknowledgments
Conflicts of Interest
References
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Fechner, J.; Ketelhut, M.; Maier, D.; Preiss, A.; Nagel, A.C. The Binding of CSL Proteins to Either Co-Activators or Co-Repressors Protects from Proteasomal Degradation Induced by MAPK-Dependent Phosphorylation. Int. J. Mol. Sci. 2022, 23, 12336. https://doi.org/10.3390/ijms232012336
Fechner J, Ketelhut M, Maier D, Preiss A, Nagel AC. The Binding of CSL Proteins to Either Co-Activators or Co-Repressors Protects from Proteasomal Degradation Induced by MAPK-Dependent Phosphorylation. International Journal of Molecular Sciences. 2022; 23(20):12336. https://doi.org/10.3390/ijms232012336
Chicago/Turabian StyleFechner, Johannes, Manuela Ketelhut, Dieter Maier, Anette Preiss, and Anja C. Nagel. 2022. "The Binding of CSL Proteins to Either Co-Activators or Co-Repressors Protects from Proteasomal Degradation Induced by MAPK-Dependent Phosphorylation" International Journal of Molecular Sciences 23, no. 20: 12336. https://doi.org/10.3390/ijms232012336