Proximity interactome of lymphatic VE-cadherin reveals mechanisms of junctional remodeling and reelin secretion

D. Stephen Serafin, Natalie R. Harris, László Bálint, Elizabeth S. Douglas and Kathleen M. Caron ()
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D. Stephen Serafin: University of North Carolina at Chapel Hill
Natalie R. Harris: University of North Carolina at Chapel Hill
László Bálint: University of North Carolina at Chapel Hill
Elizabeth S. Douglas: University of North Carolina at Chapel Hill
Kathleen M. Caron: University of North Carolina at Chapel Hill

Nature Communications, 2024, vol. 15, issue 1, 1-18

Abstract: Abstract The adhesion receptor vascular endothelial (VE)-cadherin transduces an array of signals that modulate crucial lymphatic cell behaviors including permeability and cytoskeletal remodeling. Consequently, VE-cadherin must interact with a multitude of intracellular proteins to exert these functions. Yet, the full protein interactome of VE-cadherin in endothelial cells remains a mystery. Here, we use proximity proteomics to illuminate how the VE-cadherin interactome changes during junctional reorganization from dis-continuous to continuous junctions, triggered by the lymphangiogenic factor adrenomedullin. These analyses identified interactors that reveal roles for ADP ribosylation factor 6 (ARF6) and the exocyst complex in VE-cadherin trafficking and recycling. We also identify a requisite role for VE-cadherin in the in vitro and in vivo control of secretion of reelin—a lymphangiocrine glycoprotein with recently appreciated roles in governing heart development and injury repair. This VE-cadherin protein interactome shines light on mechanisms that control adherens junction remodeling and secretion from lymphatic endothelial cells.

Date: 2024
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DOI: 10.1038/s41467-024-51918-1

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