4.5 Article

The N-cadherin interactome in primary cardiomyocytes as defined using quantitative proximity proteomics

期刊

JOURNAL OF CELL SCIENCE
卷 132, 期 3, 页码 -

出版社

COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.221606

关键词

CDH2; N-cadherin; Cardiomyocyte; Adherens junction; Intercalated disc; Proteomics; Interactome

资金

  1. National Institutes of Health [F31 HL136069, 1S10OD011967, R01 HL127711]
  2. National Cancer Institute [P30CA047904]

向作者/读者索取更多资源

The junctional complexes that couple cardiomyocytes must transmit the mechanical forces of contraction while maintaining adhesive homeostasis. The adherens junction (AJ) connects the actomyosin networks of neighboring cardiomyocytes and is required for proper heart function. Yet little is known about the molecular composition of the cardiomyocyte AJ or how it is organized to function under mechanical load. Here, we define the architecture, dynamics and proteome of the cardiomyocyte AJ. Mouse neonatal cardiomyocytes assemble stable AJs along intercellular contacts with organizational and structural hallmarks similar to mature contacts. We combine quantitative mass spectrometry with proximity labeling to identify the N-cadherin (CDH2) interactome. We define over 350 proteins in this interactome, nearly 200 of which are unique to CDH2 and not part of the E-cadherin (CDH1) interactome. CDH2-specific interactors comprise primarily adaptor and adhesion proteins that promote junction specialization. Our results provide novel insight into the cardiomyocyte AJ and offer a proteomic atlas for defining the molecular complexes that regulate cardiomyocyte intercellular adhesion. This article has an associated First Person interview with the first authors of the paper.

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