Movement of myosin‐coated structures on actin cables
Abstract
Myosin-coated spheres from 0.6 to 120 microns in diameter move in vitro on a substratum of polar arrays of actin cables derived from the alga Nitella. The force for this movement is provided by skeletal muscle myosin since it is ATP-dependent, and N-ethylmaleimide (NEM) inactivation of the myosin blocks movement. These observations demonstrate that attachment of myosin in a random orientation to structures will enable those structures to move along polar arrays of actin filaments.
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Myosin and dynein generate force in only one direction with respect to their filamentous substrates.
“Myosin (Sheetz and Spudich, 1983) and dynein (Gibbons, 1981) generate force in only one direction with respect to their filamentous substrates.”
From Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility (1985) · cites this paper as Sheetz and Spudich, 1983
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Identification of a novel force-generating protein, kinesin, involved in microtubule-based motility
VALE, R., REESE, T., & SHEETZ, M. (1985) · Cell · doi:10.1016/s0092-8674(85)80099-4 · Cited by 1,993 · see citing works
Self-citationSarcopenia: Aging-Related Loss of Muscle Mass and Function
Larsson, L., Degens, H., Li, M., Salviati, L., Lee, Y. I., Thompson, W., Kirkland, J. L., & Sandri, M. (2019) · Physiological Reviews · doi:10.1152/physrev.00061.2017 · Cited by 1,797 · see citing works
- Authors
- Sheetz, M. P., & Spudich, J. A.
- Affiliations
- Stanford Medicine (US)
- Corresponding author
- Sheetz, Michael P.
- Venue
- Cell Motility
- Publisher
- Wiley
- Published
- 1983-01
- Volume
- 3
- Issue
- 5
- Pages
- 485-489
- ISSN
- 0271-6585 (ISSN-L)
- OpenAlex
- W2007379744
- Cited by
- 41
- References
- 0
- Citations by year
- 2025: 1 · 2024: 1 · 2021: 3 · 2020: 1 · 2018: 3 · 2017: 1 · 2014: 1
- FWCI
- 1.41
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Cell Motility (publishedVersion)
- PubMed (publishedVersion)
- Funders
- American Heart Association
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiomyopathy and Myosin Studies
- Keywords
- myosin, actin cables, F-actin, skeletal muscle myosin, N-ethylmaleimide, Nitella, in vitro motility
- MeSH terms
- Actins, Adenosine Triphosphate, Movement, Myosins, Eukaryota
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