Complex effects of kinase localization revealed by compartment-specific regulation of protein kinase A activity.

ABSTRACT: Kinase activity in signaling networks frequently depends on regulatory subunits that can both inhibit activity by interacting with the catalytic subunits and target the kinase to distinct molecular partners and subcellular compartments. Here, using a new synthetic molecular interaction system, we show that translocation of a regulatory subunit of the protein kinase A (PKA-R) to the plasma membrane has a paradoxical effect on the membrane kinase activity. It can both enhance it at lower translocation levels, even in the absence of signaling inputs, and inhibit it at higher translocation levels, suggesting its role as a linker that can both couple and decouple signaling processes in a concentration-dependent manner. We further demonstrate that superposition of gradients of PKA-R abundance ac

SUBMITTER: LaCroix R 

PROVIDER: S-EPMC8871369 | biostudies-literature | 2022 Feb

REPOSITORIES: biostudies-literature