Myosin III-mediated cross-linking and stimulation of actin bundling activity of Espin

ELife
Haiyang LiuMingjie Zhang

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.

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Citations

Jan 28, 2017·Journal of Chemical Information and Modeling·Yuwei ZhangFei Xia
Sep 2, 2016·The Journal of Biological Chemistry·Manmeet H RavalChristopher M Yengo
Mar 16, 2021·Frontiers in Cell and Developmental Biology·Joseph A CiriloChristopher M Yengo
May 26, 2021·Current Biology : CB·Anne Houdusse, Margaret A Titus

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Methods Mentioned

BETA
gel filtration
isothermal titration calorimetry
gel
static light scattering
light scattering
X-ray
transmission electron microscopy
PCR
size-exclusion chromatography
transfection

Software Mentioned

ImageJ
PyMOL
ASTRA
WebLogo
PHASER
PHENIX
COOT
MolProbity
HKL2000

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