ArticleMolecular biology of the cell2019
Tropomyosin isoforms differentially tune actin filament length and disassembly.
Article in Molecular biology of the cell, 2019. 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, 49 citations in OpenAlex.
- Loss of cyclase-associated protein 2 alters actin cytoskeleton organization and biomechanical properties of the ocular lens.Journal of cell science · 2026Article
- Cyclase associated actin cytoskeleton regulatory protein 2 (CAP2) organizes the actin cytoskeleton to influence the biomechanical properties of the ocular lens.bioRxiv : the preprint server for biology · 2025Article
- Functional redundancy and formin-isoform independent localization of tropomyosin paralogs in Saccharomyces cerevisiae.PLoS genetics · 2025Article
- Single molecule visualization of tropomyosin isoform organization in the mammalian actin cytoskeleton.Cytoskeleton (Hoboken, N.J.) · 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
- Dilated cardiomyopathy-associated skeletal muscle actin (ACTA1) mutation R256H disrupts actin structure and function and causes cardiomyocyte hypocontractility.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Keratan sulfate, an electrosensory neurosentient bioresponsive cell instructive glycosaminoglycan.Glycobiology · 2024Review
- Focal adhesions contain three specialized actin nanoscale layers.Nature communications · 2024Article
- Cytosolic concentrations of actin binding proteins and the implications for in vivo F-actin turnover.The Journal of cell biology · 2023Article
- Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023Review
- Cyclase-associated protein interacts with actin filament barbed ends to promote depolymerization and formin displacement.The Journal of biological chemistry · 2023Article
- Troponin and a Myopathy-Linked Mutation inInternational journal of molecular sciences · 2023Article
- Tropomyosin 3 (TPM3) function in skeletal muscle and in myopathy.Skeletal muscle · 2023Review
- Structural insights into actin isoforms.eLife · 2023Article
- Single-molecule analysis of actin filament debranching by cofilin and GMF.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Membrane nanodomains modulate formin condensation for actin remodeling in Arabidopsis innate immune responses.The Plant cell · 2022Article
- Celebrating 20 years of live single-actin-filament studies with five golden rules.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Novel human cell expression method reveals the role and prevalence of posttranslational modification in nonmuscle tropomyosins.The Journal of biological chemistry · 2021Article
- RTKN-1/Rhotekin shields endosome-associated F-actin from disassembly to ensure endocytic recycling.The Journal of cell biology · 2021Article
- Actin filament oxidation by MICAL1 suppresses protections from cofilin-induced disassembly.EMBO reports · 2021Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Cellular actin networks exhibit diverse filamentous architectures and turnover dynamics, but how these differences are specified remains poorly understood. Here, we used multicolor total internal reflection fluorescence microscopy to ask how decoration of actin filaments by five biologically prominent Tropomyosin (TPM) isoforms influences disassembly induced by Cofilin alone, or by the collaborative effects of Cofilin, Coronin, and AIP1 (CCA). TPM decoration restricted Cofilin binding to pointed ends, while not interfering with Coronin binding to filament sides. Different isoforms of TPM provided variable levels of protection against disassembly, with the strongest protection by Tpm3.1 and the weakest by Tpm1.6. In biomimetic assays in which filaments were simultaneously assembled by formins and disassembled by CCA, these TPM isoform-specific effects persisted, giving rise to filaments with different lengths and treadmilling behavior. Together, our data reveal that TPM isoforms have quantitatively distinct abilities to tune actin filament length and turnover.
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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.