Detecting Cardiovascular Protein-Protein Interactions by Proximity Proteomics

Document Type

Article

Publication Date

1-21-2022

Publication Title

Circulation research

Keywords

JGM, animals, mass spectrometry, muscle cells, protein interaction mapping, proteomics

JAX Source

Circ Res . 2022 Jan 21;130(2):273-287

Volume

130

Issue

2

First Page

273

Last Page

287

PMID

35050691

DOI

10.1161/CIRCRESAHA.121.319810

Grant

The research was supported by K08 HL151969 and AHA CDA 35320208 to J.S. Kushner, NHLBI R01 HL142787 and U01 HL156349 to J.T. Hinson; R01 HL146149, R01 HL155377, and R01 HL121253 to S.O. Marx; and NHLBI R01 HL160089 to G.S. Pitt and S.O. Marx.

Abstract

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.

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