Detecting Cardiovascular Protein-Protein Interactions by Proximity Proteomics.

Journal Article (Journal Article;Review)

Rapidly changing and transient protein-protein interactions regulate dynamic cellular processes in the cardiovascular system. Traditional methods, including affinity purification and mass spectrometry, have revealed many macromolecular complexes in cardiomyocytes and the vasculature. Yet these methods often fail to identify in vivo or transient protein-protein interactions. To capture these interactions in living cells and animals with subsequent mass spectrometry identification, enzyme-catalyzed proximity labeling techniques have been developed in the past decade. Although the application of this methodology to cardiovascular research is still in its infancy, the field is developing rapidly, and the promise is substantial. In this review, we outline important concepts and discuss how proximity proteomics has been applied to study physiological and pathophysiological processes relevant to the cardiovascular system.

Full Text

Duke Authors

Cited Authors

  • Kushner, JS; Liu, G; Eisert, RJ; Bradshaw, GA; Pitt, GS; Hinson, JT; Kalocsay, M; Marx, SO

Published Date

  • January 21, 2022

Published In

Volume / Issue

  • 130 / 2

Start / End Page

  • 273 - 287

PubMed ID

  • 35050691

Pubmed Central ID

  • PMC8852690

Electronic International Standard Serial Number (EISSN)

  • 1524-4571

Digital Object Identifier (DOI)

  • 10.1161/CIRCRESAHA.121.319810


  • eng

Conference Location

  • United States