Analyses of PDE-regulated phosphoproteomes reveal unique and specific cAMP-signaling modules in T cells.

ABSTRACT: Specific functions for different cyclic nucleotide phosphodiesterases (PDEs) have not yet been identified in most cell types. Conventional approaches to study PDE function typically rely on measurements of global cAMP, general increases in cAMP-dependent protein kinase (PKA), or the activity of exchange protein activated by cAMP (EPAC). Although newer approaches using subcellularly targeted FRET reporter sensors have helped define more compartmentalized regulation of cAMP, PKA, and EPAC, they have limited ability to link this regulation to downstream effector molecules and biological functions. To address this problem, we have begun to use an unbiased mass spectrometry-based approach coupled with treatment using PDE isozyme-selective inhibitors to characterize the phosphoproteomes of the f

SUBMITTER: Beltejar MG 

PROVIDER: S-EPMC5544305 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature