Proteomics

Dataset Information

0

Phosphoproteomics analysis to identify PPP2R5D substrates


ABSTRACT: The purpose of this project is to identify the substrates that are specific for B'delta regulatory subunit. For this purpose, we have generated two doxycycline-inducible stable cell lines (OE and RE) that express B'delta. In the OE cell lines, B'delta is overexpressed without downregulation of the endogenous regulatory subunits. On the other hand, in the RE cell lines, B'delta is overexpressed concurrently with a downregulation of the endogenous regulatory subunits. To stimulate protein phosphorylation, we used isoproterenol, a beta-adrenergic agonist that is known to induce the PKA-mediated phosphorylation and activation of the B'd.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Laura Herring  

LAB HEAD: Stephan Strack

PROVIDER: PXD016809 | Pride | 2020-04-17

REPOSITORIES: Pride

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Publications

Reduction of protein phosphatase 2A (PP2A) complexity reveals cellular functions and dephosphorylation motifs of the PP2A/B'δ holoenzyme.

Jong Chian Ju CJ   Merrill Ronald A RA   Wilkerson Emily M EM   Herring Laura E LE   Graves Lee M LM   Strack Stefan S  

The Journal of biological chemistry 20200310 17


Protein phosphatase 2A (PP2A) is a large enzyme family responsible for most cellular Ser/Thr dephosphorylation events. PP2A substrate specificity, localization, and regulation by second messengers rely on more than a dozen regulatory subunits (including B/R2, B'/R5, and B″/R3), which form the PP2A heterotrimeric holoenzyme by associating with a dimer comprising scaffolding (A) and catalytic (C) subunits. Because of partial redundancy and high endogenous expression of PP2A holoenzymes, traditiona  ...[more]

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