ArticleThe Journal of cell biology2003
A mutant heterodimeric myosin with one inactive head generates maximal displacement.
Article in The Journal of cell biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
26 citing papers in PubMed.
- Alpha and beta myosin isoforms and human atrial and ventricular contraction.Cellular and molecular life sciences : CMLS · 2021Review
- Do Actomyosin Single-Molecule Mechanics Data Predict Mechanics of Contracting Muscle?International journal of molecular sciences · 2018Review
- Directly interrogating single quantum dot labelled UvrA2 molecules on DNA tightropes using an optically trapped nanoprobe.Scientific reports · 2015Article
- Using fluorescent myosin to directly visualize cooperative activation of thin filaments.The Journal of biological chemistry · 2015Article
- Poorly understood aspects of striated muscle contraction.BioMed research international · 2015Review
- Myosin 3A kinase activity is regulated by phosphorylation of the kinase domain activation loop.The Journal of biological chemistry · 2013Article
- Direct observation of phosphate inhibiting the force-generating capacity of a miniensemble of Myosin molecules.Biophysical journal · 2013Article
- In vitro formation and characterization of the skeletal muscle α·β tropomyosin heterodimers.Biochemistry · 2012Article
- The rates of Ca2+ dissociation and cross-bridge detachment from ventricular myofibrils as reported by a fluorescent cardiac troponin C.The Journal of biological chemistry · 2012Article
- Mechanical coupling between myosin molecules causes differences between ensemble and single-molecule measurements.Biophysical journal · 2012Article
- Gene transfer, expression, and sarcomeric incorporation of a headless myosin molecule in cardiac myocytes: evidence for a reserve in myofilament motor function.American journal of physiology. Heart and circulatory physiology · 2011Article
- Simultaneous observation of tail and head movements of myosin V during processive motion.The Journal of biological chemistry · 2010Article
- Modeling smooth muscle myosin's two heads: long-lived enzymatic roles and phosphorylation-dependent equilibria.Biophysical journal · 2010Article
- Collaborative dynamic DNA scanning by nucleotide excision repair proteins investigated by single- molecule imaging of quantum-dot-labeled proteins.Molecular cell · 2010Article
- Human actin mutations associated with hypertrophic and dilated cardiomyopathies demonstrate distinct thin filament regulatory properties in vitro.Journal of molecular and cellular cardiology · 2010Article
- Smooth muscle heavy meromyosin phosphorylated on one of its two heads supports force and motion.The Journal of biological chemistry · 2009Article
- Processive movement by a kinesin heterodimer with an inactivating mutation in one head.Biochemistry · 2008Article
- Effect of low pH on single skeletal muscle myosin mechanics and kinetics.American journal of physiology. Cell physiology · 2008Article
- Load and Pi control flux through the branched kinetic cycle of myosin V.The Journal of biological chemistry · 2008Article
- Mutation of a conserved glycine in the SH1-SH2 helix affects the load-dependent kinetics of myosin.Biophysical journal · 2007Article
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
Each of the heads of the motor protein myosin II is capable of supporting motion. A previous report showed that double-headed myosin generates twice the displacement of single-headed myosin (Tyska, M.J., D.E. Dupuis, W.H. Guilford, J.B. Patlak, G.S. Waller, K.M. Trybus, D.M. Warshaw, and S. Lowey. 1999. Proc. Natl. Acad. Sci. USA. 96:4402-4407). To determine the role of the second head, we expressed a smooth muscle heterodimeric heavy meromyosin (HMM) with one wild-type head, and the other locked in a weak actin-binding state by introducing a point mutation in switch II (E470A). Homodimeric E470A HMM did not support in vitro motility, and only slowly hydrolyzed MgATP. Optical trap measurements revealed that the heterodimer generated unitary displacements of 10.4 nm, strikingly similar to wild-type HMM (10.2 nm) and approximately twice that of single-headed subfragment-1 (4.4 nm). These data show that a double-headed molecule can achieve a working stroke of approximately 10 nm with only one active head and an inactive weak-binding partner. We propose that the second head optimizes the orientation and/or stabilizes the structure of the motion-generating head, thereby resulting in maximum displacement.
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Registered trials
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