Post-translational modification of cardiac proteasomes: functional delineation enabled by proteomics

Am J Physiol Heart Circ Physiol. 2012 Jul;303(1):H9-18. doi: 10.1152/ajpheart.00189.2012. Epub 2012 Apr 20.


Proteasomes are ubiquitously expressed multicatalytic complexes that serve as key regulators of protein homeostasis. There are several lines of evidence indicating that proteasomes exist in heterogeneous subpopulations in cardiac muscle, differentiated, in part, by post-translational modifications (PTMs). PTMs regulate numerous facets of proteasome function, including catalytic activities, complex assembly, interactions with associating partners, subcellular localization, substrate preference, and complex turnover. Classical technologies used to identify PTMs on proteasomes have lacked the ability to determine site specificity, quantify stoichiometry, and perform large-scale, multi-PTM analysis. Recent advancements in proteomic technologies have largely overcome these limitations. We present here a discussion on the importance of PTMs in modulating proteasome function in cardiac physiology and pathophysiology, followed by the presentation of a state-of-the-art proteomic workflow for identifying and quantifying PTMs of cardiac proteasomes.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Animals
  • Computational Biology
  • Heart / physiology*
  • Humans
  • Molecular Sequence Data
  • Myocardium / metabolism*
  • Myocytes, Cardiac / physiology
  • Proteasome Endopeptidase Complex / genetics*
  • Protein Processing, Post-Translational / genetics*
  • Protein Processing, Post-Translational / physiology*
  • Proteomics*
  • Signal Transduction / physiology
  • Subcellular Fractions / metabolism


  • Proteasome Endopeptidase Complex