Article
cAMP-induced phosphorylation of 26S proteasomes on Rpn6/PSMD11 enhances their activity and the degradation of misfolded proteins.
Proceedings of the National Academy of Sciences of the United States of America - 29 Dec 2015
Lokireddy Sudarsanareddy, Kukushkin Nikolay Vadimovich, Goldberg Alfred Lewis
Abstract excerpt
Although rates of protein degradation by the ubiquitin-proteasome pathway (UPS) are determined by their rates of ubiquitination, we show here that the proteasome's capacity to degrade ubiquitinated proteins is also tightly regulated. We studied the effects of cAMP-dependent protein kinase (PKA) on proteolysis by the UPS in several mammalian cell lines. Various agents that raise intracellular cAMP and activate PKA...
Topics
- Animals
- Cell Line
- Cell Line, Tumor
- Colforsin
- Cyclic AMP
- Cyclic AMP-Dependent Protein Kinases
- HEK293 Cells
- Humans
- Immunoblotting
- Mutation
- Phosphodiesterase 4 Inhibitors