ArticleThe Journal of biological chemistry2013
A periodic pattern of evolutionarily conserved basic and acidic residues constitutes the binding interface of actin-tropomyosin.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 59 citations in OpenAlex.
- Myosin-1C differentially displaces tropomyosin isoforms altering their inhibition of motility.The Journal of biological chemistry · 2024Article
- Acetylation of fission yeast tropomyosin does not promote differential association with cognate formins.Cytoskeleton (Hoboken, N.J.) · 2023Article
- Alternative splicing of a single exon causes a major impact on the affinity ofFrontiers in cell and developmental biology · 2023Article
- High-resolution cryo-EM structure of the junction region of the native cardiac thin filament in relaxed state.PNAS nexus · 2023Article
- Genotype-Phenotype Associations with Restrictive Cardiomyopathy Induced by Pathogenic Genetic Mutations.Reviews in cardiovascular medicine · 2022Review
- Lysine acetylation of F-actin decreases tropomyosin-based inhibition of actomyosin activity.The Journal of biological chemistry · 2020Article
- Article
- Protein-Protein Docking Reveals Dynamic Interactions of Tropomyosin on Actin Filaments.Biophysical journal · 2020Article
- The actin 'A-triad's' role in contractile regulation in health and disease.The Journal of physiology · 2020Review
- Actin Mutations and Their Role in Disease.International journal of molecular sciences · 2020Review
- Functional outcomes of structural peculiarities of striated muscle tropomyosin.Journal of muscle research and cell motility · 2020Review
- A new twist on tropomyosin binding to actin filaments: perspectives on thin filament function, assembly and biomechanics.Journal of muscle research and cell motility · 2020Review
- Tropomyosin dynamics during cardiac muscle contraction as governed by a multi-well energy landscape.Progress in biophysics and molecular biology · 2019Article
- The Effect of Tropomyosin Mutations on Actin-Tropomyosin Binding: In Search of Lost Time.Biophysical journal · 2019Article
- Tropomyosin isoforms differentially affect muscle contractility in the head and body regions of the nematode Caenorhabditis elegans.Molecular biology of the cell · 2018Article
- Biophysical Derangements in Genetic Cardiomyopathies.Heart failure clinics · 2018Review
- Distinct sites in tropomyosin specify shared and isoform-specific regulation of myosins II and V.Cytoskeleton (Hoboken, N.J.) · 2018Article
- Tropomyosin Must Interact Weakly with Actin to Effectively Regulate Thin Filament Function.Biophysical journal · 2017Article
- Distortion of the Actin A-Triad Results in Contractile Disinhibition and Cardiomyopathy.Cell reports · 2017Article
- Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Actin filament cytoskeletal and muscle functions are regulated by actin binding proteins using a variety of mechanisms. A universal actin filament regulator is the protein tropomyosin, which binds end-to-end along the length of the filament. The actin-tropomyosin filament structure is unknown, but there are atomic models in different regulatory states based on electron microscopy reconstructions, computational modeling of actin-tropomyosin, and docking of atomic resolution structures of tropomyosin to actin filament models. Here, we have tested models of the actin-tropomyosin interface in the "closed state" where tropomyosin binds to actin in the absence of myosin or troponin. Using mutagenesis coupled with functional analyses, we determined residues of actin and tropomyosin required for complex formation. The sites of mutations in tropomyosin were based on an evolutionary analysis and revealed a pattern of basic and acidic residues in the first halves of the periodic repeats (periods) in tropomyosin. In periods P1, P4, and P6, basic residues are most important for actin affinity, in contrast to periods P2, P3, P5, and P7, where both basic and acidic residues or predominantly acidic residues contribute to actin affinity. Hydrophobic interactions were found to be relatively less important for actin binding. We mutated actin residues in subdomains 1 and 3 (Asp(25)-Glu(334)-Lys(326)-Lys(328)) that are poised to make electrostatic interactions with the residues in the repeating motif on tropomyosin in the models. Tropomyosin failed to bind mutant actin filaments. Our mutagenesis studies provide the first experimental support for the atomic models of the actin-tropomyosin interface.
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