Redox Modification of PKA-Cα Differentially Affects Its Substrate Selection.

ABSTRACT: The cyclic AMP-dependent protein kinase (PKA) plays an essential role in the regulation of many important cellular processes and is dysregulated in several pervasive diseases, including diabetes, cardiovascular disease, and various neurodegenerative disorders. Previous studies suggest that the alpha isoform of the catalytic subunit of PKA (PKA-Cα) is oxidized on C199, both in vitro and in situ. However, the molecular consequences of these modifications on PKA-Cα's substrate selection remain largely unexplored. C199 is located on the P + 1 loop within PKA-Cα's active site, suggesting that redox modification may affect its kinase activity. Given the proximity of C199 to the substrate binding pocket, we hypothesized that oxidation could differentially alter PKA-Cα's activity toward its substr

SUBMITTER: Delva-Wiley J 

PROVIDER: S-EPMC10532679 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature