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Design of a photoswitchable cadherin.

ABSTRACT: There is a growing interest in engineering proteins whose function can be controlled with the spatial and temporal precision of light. Here, we present a novel example of a functional light-triggered switch in the Ca-dependent cell-cell adhesion protein E-cadherin, created using a mechanism-based design strategy. We report an 18-fold change in apparent Ca(2+) binding affinity upon illumination. Our results include a detailed examination of functional switching via linked changes in Ca(2+) binding and cadherin dimerization. This design opens avenues toward controllable tools that could be applied to many long-standing questions about cadherin's biological function in cell-cell adhesion and downstream signaling.

SUBMITTER: Ritterson RS

PROVIDER: S-EPMC3774674 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature

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Design of a photoswitchable cadherin.

Ritterson Ryan S RS Kuchenbecker Kristopher M KM Michalik Michael M Kortemme Tanja T

Journal of the American Chemical Society 20130814 34

There is a growing interest in engineering proteins whose function can be controlled with the spatial and temporal precision of light. Here, we present a novel example of a functional light-triggered switch in the Ca-dependent cell-cell adhesion protein E-cadherin, created using a mechanism-based design strategy. We report an 18-fold change in apparent Ca(2+) binding affinity upon illumination. Our results include a detailed examination of functional switching via linked changes in Ca(2+) bindin ...[more]

PMID: 23923816

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