ArticleBiophysical journal2002
Tropomyosin requires an intact N-terminal coiled coil to interact with tropomodulin.
Article in Biophysical journal, 2002. 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, 72 citations in OpenAlex.
- Actin Filament Pointed Ends: Assays for Regulation of Assembly and Disassembly by Tropomodulin and Tropomyosin.Cytoskeleton (Hoboken, N.J.) · 2025Article
- Prediction and biological significance of small changes in binding of leiomodin to tropomyosin.The Journal of general physiology · 2025Article
- Tropomodulin-Tropomyosin Interplay Modulates Interaction Between Cardiac Myosin and Thin Filaments.Biomolecules · 2025Article
- Tropomyosin 3 (TPM3) function in skeletal muscle and in myopathy.Skeletal muscle · 2023Review
- Structural insights into the tropomodulin assembly at the pointed ends of actin filaments.Protein science : a publication of the Protein Society · 2021Article
- Leiomodin creates a leaky cap at the pointed end of actin-thin filaments.PLoS biology · 2020Article
- Thin filament dysfunctions caused by mutations in tropomyosin Tpm3.12 and Tpm1.1.Journal of muscle research and cell motility · 2020Review
- Congenital myopathy-related mutations in tropomyosin disrupt regulatory function through altered actin affinity and tropomodulin binding.The FEBS journal · 2019Article
- Role of intrinsic disorder in muscle sarcomeres.Progress in molecular biology and translational science · 2019Review
- Structural destabilization of tropomyosin induced by the cardiomyopathy-linked mutation R21H.Protein science : a publication of the Protein Society · 2018Article
- The Anti-activator QslA Negatively Regulates Phenazine-1-Carboxylic Acid Biosynthesis by Interacting With the Quorum Sensing Regulator MvfR in the RhizobacteriumFrontiers in microbiology · 2018Article
- Actin regulation by tropomodulin and tropomyosin in neuronal morphogenesis and function.Molecular and cellular neurosciences · 2017Review
- The cardiomyopathy-associated K15N mutation in tropomyosin alters actin filament pointed end dynamics.Archives of biochemistry and biophysics · 2017Article
- Localization of the binding interface between leiomodin-2 and α-tropomyosin.Biochimica et biophysica acta · 2016Article
- Review
- Functional effects of mutations in the tropomyosin-binding sites of tropomodulin1 and tropomodulin3.Cytoskeleton (Hoboken, N.J.) · 2014Article
- Differential actin-regulatory activities of Tropomodulin1 and Tropomodulin3 with diverse tropomyosin and actin isoforms.The Journal of biological chemistry · 2014Article
- Tropomodulins and tropomyosins: working as a team.Journal of muscle research and cell motility · 2013Review
- Tropomodulins: pointed-end capping proteins that regulate actin filament architecture in diverse cell types.Cytoskeleton (Hoboken, N.J.) · 2012Review
- Identification of residues within tropomodulin-1 responsible for its localization at the pointed ends of the actin filaments in cardiac myocytes.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Tropomodulins (Tmods) are tropomyosin (TM) binding proteins that bind to the pointed end of actin filaments and modulate thin filament dynamics. They bind to the N termini of both "long" TMs (with the N terminus encoded by exon 1a of the alpha-TM gene) and "short" nonmuscle TMs (with the N terminus encoded by exon 1b). In this present study, circular dichroism was used to study the interaction of two designed chimeric proteins, AcTM1aZip and AcTM1bZip, containing the N terminus of a long or a short TM, respectively, with protein fragments containing residues 1 to 130 of erythrocyte or skeletal muscle Tmod. The binding of either TMZip causes similar conformational changes in both Tmod fragments promoting increases in both alpha-helix and beta-structure, although they differ in binding affinity. The circular dichroism changes in the Tmod upon binding and modeling of the Tmod sequences suggest that the interface between TM and Tmod includes a three- or four-stranded coiled coil. An intact coiled coil at the N terminus of the TMs is essential for Tmod binding, as modifications that disrupt the N-terminal helix, such as removal of the N-terminal acetyl group from AcTM1aZip or striated muscle alpha-TM, or introduction of a mutation that causes nemaline myopathy, Met-8-Arg, into AcTM1aZip destroyed Tmod binding.
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