ArticleProtein science : a publication of the Protein Society2021
Structural insights into the tropomodulin assembly at the pointed ends of actin filaments.
Article in Protein science : a publication of the Protein Society, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 13 citations in OpenAlex.
- N-Terminal Actin-Binding Site of Lmod2 Promotes Controlled Pointed End Elongation.Circulation research · 2026Article
- Prediction and biological significance of small changes in binding of leiomodin to tropomyosin.The Journal of general physiology · 2025Article
- A novel pathogenic variant c.44A > G (p. Asp15Gly) inMolecular genetics and metabolism reports · 2025Article
- Tropomodulin-Tropomyosin Interplay Modulates Interaction Between Cardiac Myosin and Thin Filaments.Biomolecules · 2025Article
- Genome-Wide Association Study of Conformation Traits in Brazilian Holstein Cattle.Animals : an open access journal from MDPI · 2024Article
- Nucleus Mechanosensing in Cardiomyocytes.International journal of molecular sciences · 2023Review
- Effects of Tropomodulin 2 on Dendritic Spine Reorganization and Dynamics.Biomolecules · 2023Article
- Myofilament-associated proteins with intrinsic disorder (MAPIDs) and their resolution by computational modeling.Quarterly reviews of biophysics · 2023Review
- Nuclear Magnetic Resonance-Guided Structural Analysis of Moderate-Affinity Protein Complexes with Intrinsically Disordered Polypeptides.Methods in molecular biology (Clifton, N.J.) · 2023Article
- CaProtein science : a publication of the Protein Society · 2022Article
- Structural insights into the tropomodulin assembly at the pointed ends of actin filaments.Protein science : a publication of the Protein Society · 2021Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Tropomodulins are a family of important regulators of actin dynamics at the pointed ends of actin filaments. Four isoforms of tropomodulin, Tmod1-Tmod4, are expressed in vertebrates. Binding of tropomodulin to the pointed end is dependent on tropomyosin, an actin binding protein that itself is represented in mammals by up to 40 isoforms. The understanding of the regulatory role of the tropomodulin/tropomyosin molecular diversity has been limited due to the lack of a three-dimensional structure of the tropomodulin/tropomyosin complex. In this study, we mapped tropomyosin residues interacting with two tropomyosin-binding sites of tropomodulin and generated a three-dimensional model of the tropomodulin/tropomyosin complex for each of these sites. The models were refined by molecular dynamics simulations and validated via building a self-consistent three-dimensional model of tropomodulin assembly at the pointed end. The model of the pointed-end Tmod assembly offers new insights in how Tmod binding ensures tight control over the pointed end dynamics.
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Registered trials
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.