The N-cadherin interactome in primary cardiomyocytes as defined using quantitative proximity proteomics
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Abstract
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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- Authors
- Li, Y., Merkel, C. D., Zeng, X., Heier, J. A., Cantrell, P. S., Sun, M., Stolz, D. B., Watkins, S. C., Yates, N. A., & Kwiatkowski, A. V.
- Affiliations
- University of Pittsburgh School of Medicine 1 Department of Cell Biology , , Pittsburgh, PA 15261 , USA
- University of Pittsburgh (US)
- Corresponding author
- Kwiatkowski, Adam V.
- ORCID
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2019-02-01
- Volume
- 132
- Issue
- 3
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- PMC
- PMC6382013
- OpenAlex
- W2808271009
- Cited by
- 58
- References
- 94
- Citations by year
- 2026: 10 · 2025: 3 · 2024: 4 · 2023: 6 · 2022: 10 · 2021: 8 · 2020: 12 · 2019: 4 · 2018: 1
- FWCI
- 6.47
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Cell Science (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- Europe PMC (PubMed Central) (publishedVersion, other-oa)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- HighWire Press Open Archive (submittedVersion)
- Funders
- National Institutes of Health (F31 HL136069, 1S10OD011967, R01 HL127711)
- National Cancer Institute (P30CA047904)
- Topics
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Biotin and Related Studies
- Physical Sciences › Chemistry › Spectroscopy › Advanced Proteomics Techniques and Applications
- Keywords
- N-cadherin, E-cadherin, CDH1, adherens junctions, cardiomyocytes, protein-protein interaction network, cell-cell adhesion, junctional complexes, mechanical force transmission, proximity labeling, neonatal cardiomyocytes
- MeSH terms
- Actomyosin, Animals, Animals, Newborn, Cell Adhesion, Cell Communication, Gene Expression Regulation, Actin Cytoskeleton, Protein Binding, Cadherins, Adherens Junctions, Protein Interaction Mapping, Myocytes, Cardiac, Mechanotransduction, Cellular, Proteomics, Mice, Molecular Sequence Annotation, Primary Cell Culture, Gene Ontology
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