ArticleBiophysical journal2004
Unconstrained steps of myosin VI appear longest among known molecular motors.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Membrane-bound myosin IC drives the chiral rotation of the gliding actin filament around its longitudinal axis.Scientific reports · 2023Article
- Landscape-Based View on the Stepping Movement of Myosin VI.The journal of physical chemistry. B · 2022Article
- Unitary step of gliding machinery in Mycoplasma mobile.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Coupling of lever arm swing and biased Brownian motion in actomyosin.PLoS computational biology · 2014Article
- Article
- Switching of myosin-V motion between the lever-arm swing and brownian search-and-catch.Nature communications · 2012Article
- How myosin motors power cellular functions: an exciting journey from structure to function: based on a lecture delivered at the 34th FEBS Congress in Prague, Czech Republic, July 2009.The FEBS journal · 2012Article
- Lever-arm mechanics of processive myosins.Biophysical journal · 2011Review
- Extension of a three-helix bundle domain of myosin VI and key role of calmodulins.Biophysical journal · 2011Article
- Direct observation of the myosin Va recovery stroke that contributes to unidirectional stepping along actin.PLoS biology · 2011Article
- The stepping pattern of myosin X is adapted for processive motility on bundled actin.Biophysical journal · 2010Article
- Unconventional processive mechanics of non-muscle myosin IIB.The Journal of biological chemistry · 2010Article
- Myosin VI undergoes a 180 degrees power stroke implying an uncoupling of the front lever arm.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Reverse conformational changes of the light chain-binding domain of myosin V and VI processive motor heads during and after hydrolysis of ATP by small-angle X-ray solution scattering.Journal of molecular biology · 2009Article
- Twirling motion of actin filaments in gliding assays with nonprocessive Myosin motors.Biophysical journal · 2009Article
- Using electrical and optical tweezers to facilitate studies of molecular motors.Physical chemistry chemical physics : PCCP · 2009Article
- Pulling out the coordination mechanism of myosin-VI.Nature chemical biology · 2009Article
- Twirling of actin by myosins II and V observed via polarized TIRF in a modified gliding assay.Biophysical journal · 2008Article
- Long single alpha-helical tail domains bridge the gap between structure and function of myosin VI.Nature structural & molecular biology · 2008Article
- Myosin VI walks "wiggly" on actin with large and variable tilting.Molecular cell · 2007Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Myosin VI is a two-headed molecular motor that moves along an actin filament in the direction opposite to most other myosins. Previously, a single myosin VI molecule has been shown to proceed with steps that are large compared to its neck size: either it walks by somehow extending its neck or one head slides along actin for a long distance before the other head lands. To inquire into these and other possible mechanism of motility, we suspended an actin filament between two plastic beads, and let a single myosin VI molecule carrying a bead duplex move along the actin. This configuration, unlike previous studies, allows unconstrained rotation of myosin VI around the right-handed double helix of actin. Myosin VI moved almost straight or as a right-handed spiral with a pitch of several micrometers, indicating that the molecule walks with strides slightly longer than the actin helical repeat of 36 nm. The large steps without much rotation suggest kinesin-type walking with extended and flexible necks, but how to move forward with flexible necks, even under a backward load, is not clear. As an answer, we propose that a conformational change in the lifted head would facilitate landing on a forward, rather than backward, site. This mechanism may underlie stepping of all two-headed molecular motors including kinesin and myosin V.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.