Structural basis of diverse membrane target recognitions by ankyrins

  1. Chao Wang
  2. Zhiyi Wei
  3. Keyu Chen
  4. Fei Ye
  5. Cong Yu
  6. Vann Bennett
  7. Mingjie Zhang  Is a corresponding author
  1. Hong Kong University of Science and Technology, Hong Kong
  2. Howard Hughes Medical Institute, Duke University Medical Center, United States

Abstract

Ankyrin adaptors together with their spectrin partners coordinate diverse ion channels and cell adhesion molecules within plasma membrane domains and thereby promote physiological activities including fast signaling in the heart and nervous system. Ankyrins specifically bind to numerous membrane targets through their 24 ankyrin repeats (ANK repeats), although the mechanism for the facile and independent evolution of these interactions has not been resolved. Here we report the structures of ANK repeats in complex with an inhibitory segment from the C-terminal regulatory domain and with a sodium channel Nav1.2 peptide, respectively, showing that the extended, extremely conserved inner groove spanning the entire ANK repeat solenoid contains multiple target binding sites capable of accommodating target proteins with very diverse sequences via combinatorial usage of these sites. These structures establish a framework for understanding the evolution of ankyrins' membrane targets, with implications for other proteins containing extended ANK repeat domains.

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Author details

  1. Chao Wang

    Hong Kong University of Science and Technology, Hong Kong, Hong Kong
    Competing interests
    The authors declare that no competing interests exist.
  2. Zhiyi Wei

    Hong Kong University of Science and Technology, Hong Kong, Hong Kong
    Competing interests
    The authors declare that no competing interests exist.
  3. Keyu Chen

    Hong Kong University of Science and Technology, Hong Kong, Hong Kong
    Competing interests
    The authors declare that no competing interests exist.
  4. Fei Ye

    Hong Kong University of Science and Technology, Hong Kong, Hong Kong
    Competing interests
    The authors declare that no competing interests exist.
  5. Cong Yu

    Hong Kong University of Science and Technology, Hong Kong, Hong Kong
    Competing interests
    The authors declare that no competing interests exist.
  6. Vann Bennett

    Howard Hughes Medical Institute, Duke University Medical Center, Durham, United States
    Competing interests
    The authors declare that no competing interests exist.
  7. Mingjie Zhang

    Hong Kong University of Science and Technology, Hong Kong, Hong Kong
    For correspondence
    mzhang@ust.hk
    Competing interests
    The authors declare that no competing interests exist.

Copyright

© 2014, Wang et al.

This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.

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  1. Chao Wang
  2. Zhiyi Wei
  3. Keyu Chen
  4. Fei Ye
  5. Cong Yu
  6. Vann Bennett
  7. Mingjie Zhang
(2014)
Structural basis of diverse membrane target recognitions by ankyrins
eLife 3:e04353.
https://doi.org/10.7554/eLife.04353

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https://doi.org/10.7554/eLife.04353