MassIVE MSV000081115

Partial Public

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

Description

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 global cAMP measurements, general increases in cAMP- dependent protein kinase (PKA) activity, or activity of exchange protein activated by cAMP (EPAC). Although newer approaches utilizing subcellularly-targeted FRET reporter sensors have helped to 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 phosphoproteome of the "functional pools" of cAMP/PKA/EPAC that are regulated by specific cAMP-PDEs (the PDE-regulated phosphoproteomes). [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: Phosphodiesterase Kinase cAMP Jurkat

Contact

Principal Investigators:
(in alphabetical order)
Joseph Beavo, University of Washington, United States of America
Submitting User: cbeltejar
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