ArticleThe Journal of biological chemistry2009
D-loop of actin differently regulates the motor function of myosins II and V.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 16 citations in OpenAlex.
- Molecular features of myosin F adapted for driving actin flows in Toxoplasma gondii.Journal of cell science · 2026Article
- Molecular features of Myosin F adapted for driving actin flows inbioRxiv : the preprint server for biology · 2025Article
- Protein design of two-component tubular assemblies similar to cytoskeletons.Nature communications · 2025Article
- Multiple Mechanisms to Regulate Actin Functions: "Fundamental" Versus Lineage-Specific Mechanisms and Hierarchical Relationships.Biomolecules · 2025Review
- Actin-binding domain of Rng2 sparsely bound on F-actin strongly inhibits actin movement on myosin II.Life science alliance · 2023Article
- ANGUSTIFOLIA Regulates Actin Filament Alignment for Nuclear Positioning in Leaves.Plant physiology · 2019Article
- Article
- Improvement of the yields of recombinant actin and myosin V-HMM in the insect cell/baculovirus system by the addition of nutrients to the high-density cell culture.Journal of muscle research and cell motility · 2012Article
- G146V mutation at the hinge region of actin reveals a myosin class-specific requirement of actin conformations for motility.The Journal of biological chemistry · 2012Article
- A novel interplay between oncogenic PFTK1 protein kinase and tumor suppressor TAGLN2 in the control of liver cancer cell motility.Oncogene · 2011Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To gain more information on the manner of actin-myosin interaction, we examined how the motile properties of myosins II and V are affected by the modifications of the DNase I binding loop (D-loop) of actin, performed in two different ways, namely, the proteolytic digestion with subtilisin and the M47A point mutation. In an in vitro motility assay, both modifications significantly decreased the gliding velocity on myosin II-heavy meromyosin due to a weaker generated force but increased it on myosin V. On the other hand, single molecules of myosin V "walked" with the same velocity on both the wild-type and modified actins; however, the run lengths decreased sharply, correlating with a lower affinity of myosin for actin due to the D-loop modifications. The difference between the single-molecule and the ensemble measurements with myosin V indicates that in an in vitro motility assay the non-coordinated multiple myosin V molecules impose internal friction on each other via binding to the same actin filament, which is reduced by the weaker binding to the modified actins. These results show that the D-loop strongly modulates the force generation by myosin II and the processivity of myosin V, presumably affecting actin-myosin interaction in the actomyosin-ADP.P(i) state of both myosins.
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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.