ArticleThe Journal of biological chemistry2014
Mouse myosin-19 is a plus-end-directed, high-duty ratio molecular motor.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 47 citations in OpenAlex.
- Dynamic Proximity Networks of Myosin-19 (Myo19) and its Mitochondrial Receptors Miro2 and Metaxin-3.Molecular & cellular proteomics : MCP · 2026Article
- Non-muscle tropomyosins inhibit myosin-19 and dynamically localize to mitochondrially associated actin filaments.The Journal of biological chemistry · 2026Article
- From Cell Architecture to Mitochondrial Signaling: Role of Intermediate Filaments in Health, Aging, and Disease.International journal of molecular sciences · 2025Review
- Nonmuscle myosin 2 filaments are processive in cells.Biophysical journal · 2023Article
- Myo19 tethers mitochondria to endoplasmic reticulum-associated actin to promote mitochondrial fission.Journal of cell science · 2023Article
- Non-muscle myosin 2 filaments are processive in cells.bioRxiv : the preprint server for biology · 2023Article
- Ensembles of human myosin-19 bound to calmodulin and regulatory light chain RLC12B drive multimicron transport.The Journal of biological chemistry · 2023Article
- Myosin II proteins are required for organization of calcium-induced actin networks upstream of mitochondrial division.Molecular biology of the cell · 2022Article
- Mechanical instability generated by Myosin 19 contributes to mitochondria cristae architecture and OXPHOS.Nature communications · 2022Article
- Mitochondria-associated myosin 19 processively transports mitochondria on actin tracks in living cells.The Journal of biological chemistry · 2022Article
- Exome sequencing of families from Ghana reveals known and candidate hearing impairment genes.Communications biology · 2022Article
- Mitochondrial dynamics involves molecular and mechanical events in motility, fusion and fission.Frontiers in cell and developmental biology · 2022Review
- Coordination of mitochondrial and cellular dynamics by the actin-based motor Myo19.Journal of cell science · 2021Article
- Motor proteins at the mitochondria-cytoskeleton interface.Journal of cell science · 2021Review
- The Functions, Methods, and Mobility of Mitochondrial Transfer Between Cells.Frontiers in oncology · 2021Review
- Effects of Mutations in the Phenamacril-Binding Site ofACS omega · 2020Article
- Miro: A molecular switch at the center of mitochondrial regulation.Protein science : a publication of the Protein Society · 2020Review
- The MyMOMA domain of MYO19 encodes for distinct Miro-dependent and Miro-independent mechanisms of interaction with mitochondrial membranes.Cytoskeleton (Hoboken, N.J.) · 2020Article
- Altered mitochondrial trafficking as a novel mechanism of cancer metastasis.Cancer reports (Hoboken, N.J.) · 2020Review
- The cargo adaptor proteins RILPL2 and melanophilin co-regulate myosin-5a motor activity.The Journal of biological chemistry · 2019Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Class XIX myosin (Myo19) is a vertebrate-specific unconventional myosin, responsible for the transport of mitochondria. To characterize biochemical properties of Myo19, we prepared recombinant mouse Myo19-truncated constructs containing the motor domain and the IQ motifs using the baculovirus/Sf9 expression system. We identified regulatory light chain (RLC) of smooth muscle/non-muscle myosin-2 as the light chain of Myo19. The actin-activated ATPase activity and the actin-gliding velocity of Myo19-truncated constructs were about one-third and one-sixth as those of myosin-5a, respectively. The apparent affinity of Myo19 to actin was about the same as that of myosin-5a. The RLCs bound to Myo19 could be phosphorylated by myosin light chain kinase, but this phosphorylation had little effect on the actin-activated ATPase activity and the actin-gliding activity of Myo19-truncated constructs. Using dual fluorescence-labeled actin filaments, we determined that Myo19 is a plus-end-directed molecular motor. We found that, similar to that of the high-duty ratio myosin, such as myosin-5a, ADP release rate was comparable with the maximal actin-activated ATPase activity of Myo19, indicating that ADP release is a rate-limiting step for the ATPase cycle of acto-Myo19. ADP strongly inhibited the actin-activated ATPase activity and actin-gliding activity of Myo19-truncated constructs. Based on the above results, we concluded that Myo19 is a high-duty ratio molecular motor moving to the plus-end of the actin filament.
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