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Backbone resonance assignments of the F-actin binding domain of mouse αN-catenin

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Abstract

α-Catenin is a filamentous actin (F-actin) binding protein that links the classical cadherin–catenin complex to the actin cytoskeleton at adherens junctions (AJs). Its C-terminal F-actin binding domain is required for regulating the dynamic interaction between AJs and the actin cytoskeleton during tissue development. Thus, obtaining the molecular details of this interaction is a crucial step towards understanding how α-catenin plays critical roles in biological processes, such as morphogenesis, cell polarity, wound healing and tissue maintenance. Here we report the backbone atom (1HN, 15N, 13Cα, 13Cβ and 13C′) resonance assignments of the C-terminal F-actin binding domain of αN-catenin.

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Acknowledgments

This work was supported by CIHR Grant (MOP 130267) to M.I. The 800 MHz NMR spectrometer used in this study was funded by the Canada Foundation for Innovation. M.I. holds Canada Research Chair in cancer structural biology.

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Author notes

  1. Feng Wang

    Present address: Department of Biochemistry, School of Medicine, Vanderbilt University, 2215 Garland Ave., 607 Light Hall, Nashville, TN, 37232-0146, USA

Authors and Affiliations

  1. Princess Margaret Cancer Centre, University Health Network and Department of Medical Biophysics, University of Toronto, 101 College Street, Toronto, ON, M5G 1L7, Canada

    Tadateru Nishikawa, Noboru Ishiyama, Feng Wang & Mitsuhiko Ikura

Authors
  1. Tadateru Nishikawa
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  2. Noboru Ishiyama
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  3. Feng Wang
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  4. Mitsuhiko Ikura
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Correspondence to Mitsuhiko Ikura.

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Nishikawa, T., Ishiyama, N., Wang, F. et al. Backbone resonance assignments of the F-actin binding domain of mouse αN-catenin. Biomol NMR Assign 11, 21–24 (2017). https://doi.org/10.1007/s12104-016-9713-8

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  • DOI: https://doi.org/10.1007/s12104-016-9713-8

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