ArticlePhilosophical transactions of the Royal Society of London. Series B, Biological sciences2004
A model of stereocilia adaptation based on single molecule mechanical studies of myosin I.
Article in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed, 34 citations in OpenAlex.
- RAB31 in glioma-derived endothelial cells promotes glioma cell invasion via extracellular vesicle-mediated enrichment of MYO1C.FEBS open bio · 2024Article
- Chemomechanical regulation of myosin Ic cross-bridges: Deducing the elastic properties of an ensemble from single-molecule mechanisms.PLoS computational biology · 2017Article
- Myosin-1c regulates the dynamic stability of E-cadherin-based cell-cell contacts in polarized Madin-Darby canine kidney cells.Molecular biology of the cell · 2013Article
- Regulation and control of myosin-I by the motor and light chain-binding domains.Trends in cell biology · 2013Review
- Kinetic characterization of nonmuscle myosin IIb at the single molecule level.The Journal of biological chemistry · 2013Article
- Myosin IC generates power over a range of loads via a new tension-sensing mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Myo1c regulates lipid raft recycling to control cell spreading, migration and Salmonella invasion.Journal of cell science · 2012Article
- Drosophila melanogaster myosin-18 represents a highly divergent motor with actin tethering properties.The Journal of biological chemistry · 2011Article
- A hearing loss-associated myo1c mutation (R156W) decreases the myosin duty ratio and force sensitivity.Biochemistry · 2011Article
- Myo1c mutations associated with hearing loss cause defects in the interaction with nucleotide and actin.Cellular and molecular life sciences : CMLS · 2011Article
- Single-molecule adhesion forces and attachment lifetimes of myosin-I phosphoinositide interactions.Biophysical journal · 2010Article
- Review
- Myosin I can act as a molecular force sensor.Science (New York, N.Y.) · 2008Article
- Calcium sensitivity of the cross-bridge cycle of Myo1c, the adaptation motor in the inner ear.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Fifty years on: where have we reached?Journal of muscle research and cell motility · 2006Article
- Article
- Adenosine diphosphate and strain sensitivity in myosin motors.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2004Review
- The motor mechanism of myosin V: insights for muscle contraction.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2004Review
- Introduction.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2004Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
We have used an optical tweezers-based apparatus to perform single molecule mechanical experiments using the unconventional myosins, Myo1b and Myo1c. The single-headed nature and slow ATPase kinetics of these myosins make them ideal for detailed studies of the molecular mechanism of force generation by acto-myosin. Myo1c exhibits several features that have not been seen using fast skeletal muscle myosin II. (i) The working stroke occurs in two, distinct phases, producing an initial 3 nm and then a further 1.5 nm of movement. (ii) Two types of binding interaction were observed: short-lived ATP-independent binding events that produced no movement and longer-lived, ATP-dependent events that produced a full working stroke. The stiffness of both types of interaction was similar. (iii) In a new type of experiment, using feedback to apply controlled displacements to a single acto-myosin cross-bridge, we found abrupt changes in force during attachment of the acto-Myo1b cross-bridge, a result that is consistent with the classical 'T2' behaviour of single muscle fibres. Given that these myosins might exhibit the classical T2 behaviour, we propose a new model to explain the slow phase of sensory adaptation of the hair cells of the inner ear.
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Registered trials
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.