ArticleThe Journal of cell biology1992
Myosin-I moves actin filaments on a phospholipid substrate: implications for membrane targeting.
Article in The Journal of cell biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 110 citations in OpenAlex.
- Long-tailed class I myosins rely on tail-mediated phosphoinositide recognition for specific membrane recruitment.Cell communication and signaling : CCS · 2025Article
- Membrane-bound myosin IC drives the chiral rotation of the gliding actin filament around its longitudinal axis.Scientific reports · 2023Article
- Discovery of the first unconventional myosin:Frontiers in physiology · 2023Review
- Adhesion force and attachment lifetime of the KIF16B-PX domain interaction with lipid membranes.Molecular biology of the cell · 2017Article
- Dynamics of membrane tethers reveal novel aspects of cytoskeleton-membrane interactions in axons.Biophysical journal · 2015Article
- Membrane-bound myo1c powers asymmetric motility of actin filaments.Current biology : CB · 2012Article
- Myo1e binds anionic phospholipids with high affinity.Biochemistry · 2010Article
- The three-dimensional dynamics of actin waves, a model of cytoskeletal self-organization.Biophysical journal · 2009Article
- Interaction of the endocytic scaffold protein Pan1 with the type I myosins contributes to the late stages of endocytosis.Molecular biology of the cell · 2007Article
- Subdomain organization of the Acanthamoeba myosin IC tail from cryo-electron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2004Article
- The Dictyostelium class I myosin, MyoD, contains a novel light chain that lacks high-affinity calcium-binding sites.The Biochemical journal · 2003Article
- The Dictyostelium CARMIL protein links capping protein and the Arp2/3 complex to type I myosins through their SH3 domains.The Journal of cell biology · 2001Article
- Direct involvement of yeast type I myosins in Cdc42-dependent actin polymerization.The Journal of cell biology · 2000Article
- The tails of two myosins.The Journal of cell biology · 2000Article
- A role for myosin-I in actin assembly through interactions with Vrp1p, Bee1p, and the Arp2/3 complex.The Journal of cell biology · 2000Article
- Three-dimensional structure of Acanthamoeba castellanii myosin-IB (MIB) determined by cryoelectron microscopy of decorated actin filaments.The Journal of cell biology · 1998Article
- The myosin I SH3 domain and TEDS rule phosphorylation site are required for in vivo function.Molecular biology of the cell · 1998Article
- Cytoskeletal protein binding kinetics at planar phospholipid membranes.Biophysical journal · 1997Article
- p21-activated kinase has substrate specificity similar to Acanthamoeba myosin I heavy chain kinase and activates Acanthamoeba myosin I.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- ATPase activity of myosin in hair bundles of the bullfrog's sacculus.Biophysical journal · 1997Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Acanthamoeba myosin-I bound to substrates of nitrocellulose or planar lipid membranes on glass moved actin filaments at an average velocity of 0.2 micron/s. This movement required ATP and phosphorylation of the myosin-I heavy chain. We prepared planar lipid membranes on a glass support by passive fusion of lipid vesicles (Brian, A. A., and H. M. McConnell. 1984. Proc. Natl. Acad. Sci. USA. 81:6159-6163) composed of phosphatidylcholine and containing 0-40% phosphatidylserine. The mass of lipid that bound to the glass was the same for membranes of 2 and 20% phosphatidylserine in phosphatidylcholine and was sufficient to form a single bilayer. Myosin-I moved actin filaments on planar membranes of 5-40% but not 0-2% phosphatidylserine. At the low concentrations of phosphatidylserine, actin filaments tended to detach suggesting that less myosin-I was bound. We used the cooperative activation of Acanthamoeba myosin-I ATPase by low concentrations of actin to assess the association of phospholipids with myosin-I. Under conditions where activity depends on the binding of actin to the tail of myosin-I (Albanesi, J. P., H. Fujisaki, and E. D. Korn. 1985. J. Biol. Chem. 260:11174-11179), phospholipid vesicles with 5-40% phosphatidylserine inhibited ATPase activity. The motility and ATPase results demonstrate a specific interaction of the tail of myosin-I with physiological concentrations of phosphatidylserine. This interaction is sufficient to support motility and may provide a mechanism to target myosin-I to biological membranes.
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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.