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Cadherins can dimerize via asymmetric interactions.

ABSTRACT: Cadherins are essential cell-cell adhesion proteins that interact in two distinct conformations: X-dimers and strand-swap dimers. Both X-dimers and strand-swap dimers are thought to exclusively rely on symmetric sets of interactions between key amino acids on both cadherin binding partners. Here, we use single-molecule atomic force microscopy and computer simulations to show that symmetry in cadherin binding is dispensable and that cadherins can also interact in a novel conformation that asymmetrically incorporates key elements of both strand-swap dimers and X-dimers. Our results clarify the biophysical rules for cadherin binding and demonstrate that cadherins interact in a more diverse range of conformations than previously understood.

SUBMITTER: Priest AV

PROVIDER: S-EPMC9829383 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature

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Cadherins can dimerize via asymmetric interactions.

Priest Andrew Vae AV Koirala Ramesh R Sivasankar Sanjeevi S

FEBS letters 20220516 13

Cadherins are essential cell-cell adhesion proteins that interact in two distinct conformations: X-dimers and strand-swap dimers. Both X-dimers and strand-swap dimers are thought to exclusively rely on symmetric sets of interactions between key amino acids on both cadherin binding partners. Here, we use single-molecule atomic force microscopy and computer simulations to show that symmetry in cadherin binding is dispensable and that cadherins can also interact in a novel conformation that asymmet ...[more]

PMID: 35532156

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