ArticleBiophysical journal2004
Changes in orientation of actin during contraction of muscle.
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 19 papers.
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Who cites it
19 citing papers in PubMed, 43 citations in OpenAlex.
- Decoding ultrasensitive self-assembly of the calcium-regulated Tetrahymena cytoskeletal protein Tcb2 using optical actuation.The Journal of biological chemistry · 2025Article
- The Twisting and Untwisting of Actin and Tropomyosin Filaments Are Involved in the Molecular Mechanisms of Muscle Contraction, and Their Disruption Can Result in Muscle Disorders.International journal of molecular sciences · 2025Review
- A periodized winter training block enhances anaerobic capacity in elite female rowers during 30-second maximal rowing.Frontiers in physiology · 2025Article
- Illuminating cellular architecture and dynamics with fluorescence polarization microscopy.Journal of cell science · 2024Review
- OOPS: Object-Oriented Polarization Software for analysis of fluorescence polarization microscopy images.PLoS computational biology · 2024Article
- From amino-acid to disease: the effects of oxidation on actin-myosin interactions in muscle.Journal of muscle research and cell motility · 2023Review
- The Primary Causes of Muscle Dysfunction Associated with the Point Mutations in Tpm3.12; Conformational Analysis of Mutant Proteins as a Tool for Classification of Myopathies.International journal of molecular sciences · 2018Article
- The spatial distribution of actin and mechanical cycle of myosin are different in right and left ventricles of healthy mouse hearts.Biochemistry · 2014Article
- Cross-bridge kinetics in myofibrils containing familial hypertrophic cardiomyopathy R58Q mutation in the regulatory light chain of myosin.Journal of theoretical biology · 2011Article
- Observing cycling of a few cross-bridges during isometric contraction of skeletal muscle.Cytoskeleton (Hoboken, N.J.) · 2010Article
- Fluorescence lifetime of actin in the familial hypertrophic cardiomyopathy transgenic heart.Biochemistry · 2009Article
- Close proximity of myosin loop 3 to troponin determined by triangulation of resonance energy transfer distance measurements.Biochemistry · 2009Article
- Site-directed spectroscopic probes of actomyosin structural dynamics.Annual review of biophysics · 2009Review
- Decreasing photobleaching by silver island films: application to muscle.Analytical biochemistry · 2007Article
- Application of surface plasmon coupled emission to study of muscle.Biophysical journal · 2006Article
- Fluorescence imaging of two-photon linear dichroism: cholesterol depletion disrupts molecular orientation in cell membranes.Biophysical journal · 2005Article
- Rotation of the lever arm of Myosin in contracting skeletal muscle fiber measured by two-photon anisotropy.Biophysical journal · 2004Article
- Simultaneous measurement of rotations of myosin, actin and ADP in a contracting skeletal muscle fiber.Journal of muscle research and cell motility · 2004Article
- Kinetics of a single cross-bridge in familial hypertrophic cardiomyopathy heart muscle measured by reverse Kretschmann fluorescence.Journal of biomedical opticsArticle
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
It is well documented that muscle contraction results from cyclic rotations of actin-bound myosin cross-bridges. The role of actin is hypothesized to be limited to accelerating phosphate release from myosin and to serving as a rigid substrate for cross-bridge rotations. To test this hypothesis, we have measured actin rotations during contraction of a skeletal muscle. Actin filaments of rabbit psoas fiber were labeled with rhodamine-phalloidin. Muscle contraction was induced by a pulse of ATP photogenerated from caged precursor. ATP induced a single turnover of cross-bridges. The rotations were measured by anisotropy of fluorescence originating from a small volume defined by a narrow aperture of a confocal microscope. The anisotropy of phalloidin-actin changed rapidly at first and was followed by a slow relaxation to a steady-state value. The kinetics of orientation changes of actin and myosin were the same. Extracting myosin abolished anisotropy changes. To test whether the rotation of actin was imposed by cross-bridges or whether it reflected hydrolytic activity of actin itself, we labeled actin with fluorescent ADP. The time-course of anisotropy change of fluorescent nucleotide was similar to that of phalloidin-actin. These results suggest that orientation changes of actin are caused by dissociation and rebinding of myosin cross-bridges, and that during contraction, nucleotide does not dissociate from actin.
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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.