Myosin III-mediated cross-linking and stimulation of actin bundling activity of Espin
Abstract
Class III myosins (Myo3) and actin-bundling protein Espin play critical roles in regulating the development and maintenance of stereocilia in vertebrate hair cells, and their defects cause hereditary hearing impairments. Myo3 interacts with Espin1 through its tail homology I motif (THDI), however it is not clear how Myo3 specifically acts through Espin1 to regulate the actin bundle assembly and stabilization. Here we discover that Myo3 THDI contains a pair of repeat sequences capable of independently and strongly binding to the ankyrin repeats of Espin1, revealing an unexpected Myo3-mediated cross-linking mechanism of Espin1. The structures of Myo3 in complex with Espin1 not only elucidate the mechanism of the binding, but also reveal a Myo3-induced release of Espin1 auto-inhibition mechanism. We also provide evidence that Myo3-mediated cross-linking can further promote actin fiber bundling activity of Espin1.
Article and author information
Author details
Reviewing Editor
- Cynthia Wolberger, Johns Hopkins University, United States
Version history
- Received: November 5, 2015
- Accepted: January 18, 2016
- Accepted Manuscript published: January 19, 2016 (version 1)
- Version of Record published: February 5, 2016 (version 2)
- Version of Record updated: July 6, 2016 (version 3)
Copyright
© 2016, Liu 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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