Imaging Nanoscale Changes in Desmosome Protein Organization

    Emily I. Bartle, Tara Urner, Tejeshwar C. Rao, Andrew P. Kowalczyk, Alexa L. Mattheyses
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    Studysummary This study found that desmosomal cadherin desmoglein 3 loses its rigidity upon Ca2+ removal, regardless of desmosome functional state, suggesting a central role for signaling in hyper-adhesion.
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    The study investigated the organization of desmosome proteins, specifically desmoglein 3, and their role in cell adhesion. Using fluorescence polarization microscopy, the researchers found that desmoglein 3 is ordered in desmosomes both in the presence and absence of calcium. However, when cells with calcium-dependent adhesion were placed in low calcium media, desmoglein 3 became disordered and adhesion was lost, while hyper-adhesive cells maintained adhesion despite the loss of protein order. This indicates that desmoglein 3's rigidity is compromised without calcium, but trans-binding of cadherin can continue, suggesting that signaling at the desmosomal plaque is crucial for hyper-adhesion. The study highlights the potential of fluorescence polarization microscopy to explore desmosome structure in relation to human diseases.
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