ArticleThe Journal of biological chemistry2018
Three mammalian tropomyosin isoforms have different regulatory effects on nonmuscle myosin-2B and filamentous β-actin
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers, 1 of them a synthesis that pooled it.
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Who cites it
32 citing papers in PubMed, 1 synthesis or guideline pooled it.
- A meta-analysis of affinity purification-mass spectrometry experimental systems used to identify eukaryotic and chlamydial proteins at the Chlamydia trachomatis inclusion membrane.Journal of proteomics · 2020Pooled it
- Sarcomeric remodelling in human heart failure unraveled by single molecule long read sequencing.EMBO molecular medicine · 2026Article
- Knock-out of Tpm4.2/Actin Filaments Alters Neuronal Signaling, Neurite Outgrowth, and Behavioral Phenotypes in Mice.Molecular neurobiology · 2025Article
- The tropomyosin 3.1/3.2 inhibitor ATM-3507 alters B-cell actin dynamics and impairs the growth and motility of diffuse large B-cell lymphoma cell lines.Frontiers in immunology · 2025Article
- An allosteric inhibitor of RhoGAP class-IX myosins suppresses the metastatic features of cancer cells.Nature communications · 2024Article
- Structure, regulation, and mechanisms of nonmuscle myosin-2.Cellular and molecular life sciences : CMLS · 2024Review
- Targeting F-actin stress fibers to suppress the dedifferentiated phenotype in chondrocytes.European journal of cell biology · 2024Article
- Molecular mechanisms linking missense ACTG2 mutations to visceral myopathy.Science advances · 2024Article
- Article
- Proteomic changes in the hippocampus of large mammals after total-body low dose radiation.PloS one · 2024Article
- Motor properties of Myosin 5c are modulated by tropomyosin isoforms and inhibited by pentabromopseudilin.Frontiers in physiology · 2024Article
- Selection and validation of reference genes for the normalization of quantitative real-time PCR in different muscle tissues of rabbits.BMC zoology · 2022Article
- Stress deprivation of tendon explants or Tpm3.1 inhibition in tendon cells reduces F-actin to promote a tendinosis-like phenotype.Molecular biology of the cell · 2022Article
- Nucleotide- and Protein-Dependent Functions ofMolecular biology of the cell · 2022Article
- Distinct actin-tropomyosin cofilament populations drive the functional diversification of cytoskeletal myosin motor complexes.iScience · 2022Article
- Assessing conservation of alternative splicing with evolutionary splicing graphs.Genome research · 2021Article
- Dynamics of Tpm1.8 domains on actin filaments with single-molecule resolution.Molecular biology of the cell · 2020Article
- Visualizing the in vitro assembly of tropomyosin/actin filaments using TIRF microscopy.Biophysical reviews · 2020Review
- Collagen, stiffness, and adhesion: the evolutionary basis of vertebrate mechanobiology.Molecular biology of the cell · 2020Review
- Tropomyosin 3.1 Association With Actin Stress Fibers is Required for Lens Epithelial to Mesenchymal Transition.Investigative ophthalmology & visual science · 2020Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The metazoan actin cytoskeleton supports a wide range of contractile and transport processes. Recent studies have shown how the dynamic association with specific tropomyosin isoforms generates actin filament populations with distinct functional properties. However, critical details of the associated molecular interactions remain unclear. Here, we report the properties of actomyosin-tropomyosin complexes containing filamentous β-actin, nonmuscle myosin-2B (NM-2B) constructs, and either tropomyosin isoform Tpm1.8cy (b.-.b.d), Tpm1.12br (b.-.b.c), or Tpm3.1cy (b.-.a.d). Our results show the extent to which the association of filamentous β-actin with these different tropomyosin cofilaments affects the actin-mediated activation of NM-2B and the release of the ATP hydrolysis products ADP and phosphate from the active site. Phosphate release gates a transition from weak to strong F-actin-binding states. The release of ADP has the opposite effect. These changes in dominant rate-limiting steps have a direct effect on the duty ratio, the fraction of time that NM-2B spends in strongly F-actin-bound states during ATP turnover. The duty ratio is increased ∼3-fold in the presence of Tpm1.12 and 5-fold for both Tpm1.8 and Tpm3.1. The presence of Tpm1.12 extends the time required per ATP hydrolysis cycle 3.7-fold, whereas it is shortened by 27 and 63% in the presence of Tpm1.8 and Tpm3.1, respectively. The resulting Tpm isoform-specific changes in the frequency, duration, and efficiency of actomyosin interactions establish a molecular basis for the ability of these complexes to support cellular processes with widely divergent demands in regard to force production, capacity to move processively, and speed of movement.
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