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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
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When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze...
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Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
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A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
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PR65A phosphorylation regulates PP2A complex signaling.

Kumar Kotlo1, Yongna Xing2, Sonia Lather3

  • 1Department of Medicine and Center for Cardiovascular Research, University of Illinois at Chicago, Chicago, Illinois, United States of America.

Plos One
|January 28, 2014
PubMed
Summary
This summary is machine-generated.

Phosphorylation of PR65A in cardiac tissue regulates Protein phosphatase 2 A (PP2A) activity. Reduced PR65A phosphorylation correlates with increased PP2A activity in heart failure.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cardiovascular Research

Background:

  • Protein phosphatase 2 A (PP2A) is crucial for numerous cellular functions.
  • Elevated PP2A activity in the heart is associated with adverse cardiac remodeling, dysfunction, and arrhythmias.
  • The PP2A holoenzyme comprises catalytic (PP2Ac), scaffold (PR65A), and regulatory (B subunits) components.

Purpose of the Study:

  • To identify in vivo phosphorylation sites on cardiac PR65A.
  • To investigate the functional impact of PR65A phosphorylation on PP2A holoenzyme assembly and signaling.
  • To determine the role of PR65A phosphorylation in the context of heart failure.

Main Methods:

  • Identification of three novel in vivo phosphorylation sites on cardiac PR65A (S303, T268, S314).
  • Utilized HEK cells expressing phosphomimetic (P-PR65A) and non-phosphorylated (N-PR65A) PR65A variants.
  • Employed 2D-DIGE analysis for phospho-protein profiling and assessed PP2A activity in Dahl rat hearts.

Main Results:

  • PR65A phosphorylation inhibits its interaction with PP2Ac, impacting PP2A holoenzyme signaling.
  • Phospho-protein profiling revealed increased abundance of 47 proteins, including EF1A and HSP60, in P-PR65A versus N-PR65A expressing cells.
  • Failing Dahl rat hearts exhibited reduced phosphorylated PR65A and heightened PP2A activity compared to controls.

Conclusions:

  • PR65A phosphorylation serves as an endogenous regulatory mechanism for the PP2A signaling complex.
  • Dysregulation of PR65A phosphorylation contributes to increased PP2A activity observed in heart failure.
  • Targeting PR65A phosphorylation may offer a therapeutic strategy for heart failure.