ArticleBiophysical journal1997
ATPase activity of myosin in hair bundles of the bullfrog's sacculus.
Article in Biophysical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 21 citations in OpenAlex.
- Cy3-ATP labeling of unfixed, permeabilized mouse hair cells.Scientific reports · 2021Article
- Distribution of frequencies of spontaneous oscillations in hair cells of the bullfrog sacculus.Biophysical journal · 2009Article
- Two mechanisms for transducer adaptation in vertebrate hair cells.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- ATP-Induced Ca(2+) release in cochlear outer hair cells: localization of an inositol triphosphate-gated Ca(2+) store to the base of the sensory hair bundle.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1999Article
- Localization of myosin-Ibeta near both ends of tip links in frog saccular hair cells.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1998Article
- Regulation of free Ca2+ concentration in hair-cell stereocilia.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1998Article
- Myosin Ibeta is located at tip link anchors in vestibular hair bundles.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1998Article
- The selectivity of the hair cell's mechanoelectrical-transduction channel promotes Ca2+ flux at low Ca2+ concentrations.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Unconventional myosins in inner-ear sensory epithelia.The Journal of cell biology · 1997Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Mechanoelectrical transduction by a hair cell displays adaptation, which is thought to occur as myosin-based molecular motors within the mechanically sensitive hair bundle adjust the tension transmitted to transduction channels. To assess the enzymatic capabilities of the myosin isozymes in hair bundles, we examined the actin-dependent ATPase activity of bundles isolated from the bullfrog's sacculus. Separation of 32P-labeled inorganic phosphate from unreacted [gamma-32P]ATP by thin-layer chromatography enabled us to measure the liberation of as little as 0.1 fmol phosphate. To distinguish the Mg(2+)-ATPase activity of myosin isozymes from that of other hair-bundle enzymes, we inhibited the interaction of hair-bundle myosin with actin and determined the reduction in ATPase activity. N-ethylmaleimide (NEM) decreased neither physiologically measured adaptation nor the nucleotide-hydrolytic activity of a 120-kDa protein thought to be myosin 1 beta. The NEM-insensitive, actin-activated ATPase activity of myosin increased from 1.0 fmol x s-1 in 1 mM EGTA to 2.3 fmol x s-1 in 10 microM Ca2+. This activity was largely inhibited by calmidazolium, but was unaffected by the addition of exogenous calmodulin. These results, which indicate that hair bundles contain enzymatically active, Ca(2+)-sensitive myosin molecules, are consistent with the role of Ca2+ in adaptation and with the hypothesis that myosin forms the hair cell's adaptation motor.
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