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Molecular mechanism of cell-cell adhesion mediated by cadherin-23

G. S. Singaraju, A. Kumar, J. S. Samuel, A. Sagar, J. P. Hazra, M. K. Sannigrahi, R. M. Yennamalli, Ashish, S. Rakshit
doi: https://doi.org/10.1101/208272
G. S. Singaraju
1Department of Chemical Sciences, Indian Institute of Science Education and Research Mohali, Punjab, India.
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A. Kumar
2Department of Physical Sciences, Department of Biotechnology and Bioinformatics, Jaypee University of Information Technology, Waknaghat, Himachal Pradesh, India
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J. S. Samuel
1Department of Chemical Sciences, Indian Institute of Science Education and Research Mohali, Punjab, India.
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A. Sagar
1Department of Chemical Sciences, Indian Institute of Science Education and Research Mohali, Punjab, India.
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J. P. Hazra
1Department of Chemical Sciences, Indian Institute of Science Education and Research Mohali, Punjab, India.
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M. K. Sannigrahi
1Department of Chemical Sciences, Indian Institute of Science Education and Research Mohali, Punjab, India.
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R. M. Yennamalli
2Department of Physical Sciences, Department of Biotechnology and Bioinformatics, Jaypee University of Information Technology, Waknaghat, Himachal Pradesh, India
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Ashish
3Institute of Microbial Technology (CSIR), Chandigarh, India.
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S. Rakshit
1Department of Chemical Sciences, Indian Institute of Science Education and Research Mohali, Punjab, India.
4Centre for Protein Science Design and Engineering, Indian Institute of Science Education and Research Mohali, Punjab, India.
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  • For correspondence: srakshit@iisermohali.ac.in
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Abstract

Adherin-junctions are traditionally described by the homophilic-interactions of classical cadherin-proteins at the extracellular region. However, the role of long-chain non-classical cadherins like cadherin-23(Cdh23) is not explored as yet even though it is implicated in tissue-morphogenesis, cancer, and force-sensing in neuronal tissues. Here, we identified a novel antiparallel-binding interface of Cdh23 homodimer in solution by combining biophysical and computational methods, in-vitro cell-binding, and mutational modifications. The dimer consists of two electrostatic-based interfaces extended up to two terminal domains, atypical to classical-cadherins known so far, and forms the strongest interactions in cadherin-family as measured using single-molecule force-spectroscopy. We further identified single point-mutation, E78K, that completely disrupts this binding. Interestingly, the mutation, S77L, found in skin cancers falls within the binding interface of the antiparallel-dimer. Overall, we provide the molecular architecture of Cdh23 at the cell-cell junctions which are likely to have far-reaching applications in the fields of mechanobiology and cancer.

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Posted October 24, 2017.
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Molecular mechanism of cell-cell adhesion mediated by cadherin-23
G. S. Singaraju, A. Kumar, J. S. Samuel, A. Sagar, J. P. Hazra, M. K. Sannigrahi, R. M. Yennamalli, Ashish, S. Rakshit
bioRxiv 208272; doi: https://doi.org/10.1101/208272
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Molecular mechanism of cell-cell adhesion mediated by cadherin-23
G. S. Singaraju, A. Kumar, J. S. Samuel, A. Sagar, J. P. Hazra, M. K. Sannigrahi, R. M. Yennamalli, Ashish, S. Rakshit
bioRxiv 208272; doi: https://doi.org/10.1101/208272

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