Simultaneous tracking of two motor domains reveals near simultaneous steps and stutter steps of myosin 10 on actin filament bundles.

Simultaneous tracking of two motor domains reveals near simultaneous steps and stutter steps of myosin 10 on actin filament bundles.
Biochem Biophys Res Commun. 2020 Feb 17;:
Authors: Qin X, Yoo H, Man Cheng HC, Nguyen QQ, Li J, Liu X, Prunetti L, Chen X, Liu T, Sweeney HL, Park H
Abstract
Myosin X (Myo10) has several unique design features including dimerization via an anti-parallel coiled coil and a long lever arm, which allow it to preferentially move on actin bundles. To understand the stepping behavior of single Myo10 on actin bundles, we labeled two heads of Myo10 dimers with different fluorophores. Unlike previously described for myosin V (Myo5) and VI (Myo6), which display alternating hand-over-hand stepping, Myo10 frequently took near simultaneous steps of both heads, and less frequently, 2-3 steps of one head before the other head stepped. We suggest that this behavior results from the unusual kinetic features of Myo10, in conjunction with the structural properties of the motor domain/lever arm, which will favor movement on actin bundles rather than on single filaments.
PMID: 32081426 [PubMed - as supplied by publisher]

Source: Biochemical and Biophysical Research communications - February 16, 2020 Category: Biochemistry Authors: Qin X, Yoo H, Man Cheng HC, Nguyen QQ, Li J, Liu X, Prunetti L, Chen X, Liu T, Sweeney HL, Park H Tags: Biochem Biophys Res Commun Source Type: research