ArticleBiochemistry2007
Tropomyosin regulates elongation by formin at the fast-growing end of the actin filament.
Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 71 citations in OpenAlex.
- The Sole Essential Low Molecular Weight Tropomyosin Isoform of Caenorhabditis elegans Is Essential for Pharyngeal Muscle Function.Cytoskeleton (Hoboken, N.J.) · 2025Article
- The sole essential low molecular weight tropomyosin isoform ofbioRxiv : the preprint server for biology · 2024Article
- Acetylation of fission yeast tropomyosin does not promote differential association with cognate formins.Cytoskeleton (Hoboken, N.J.) · 2023Article
- Diversity from similarity: cellular strategies for assigning particular identities to actin filaments and networks.Open biology · 2020Article
- Visualizing the in vitro assembly of tropomyosin/actin filaments using TIRF microscopy.Biophysical reviews · 2020Review
- Roles of TGF β and FGF Signals in the Lens: Tropomyosin Regulation for Posterior Capsule Opacity.International journal of molecular sciences · 2018Review
- Tropomyosin isoforms differentially affect muscle contractility in the head and body regions of the nematode Caenorhabditis elegans.Molecular biology of the cell · 2018Article
- Tropomyosin 2 heterozygous knockout in mice using CRISPR-Cas9 system displays the inhibition of injury-induced epithelial-mesenchymal transition, and lens opacity.Mechanisms of ageing and development · 2018Article
- FGF2 antagonizes aberrant TGFβ regulation of tropomyosin: role for posterior capsule opacity.Journal of cellular and molecular medicine · 2017Article
- Tropomyosin and Profilin Cooperate to Promote Formin-Mediated Actin Nucleation and Drive Yeast Actin Cable Assembly.Current biology : CB · 2016Article
- The impact of tropomyosins on actin filament assembly is isoform specific.Bioarchitecture · 2016Article
- A small molecule inhibitor of tropomyosin dissociates actin binding from tropomyosin-directed regulation of actin dynamics.Scientific reports · 2016Article
- Evolutionarily conserved sites in yeast tropomyosin function in cell polarity, transport and contractile ring formation.Biology open · 2015Article
- Myosin motor isoforms direct specification of actomyosin function by tropomyosins.Cytoskeleton (Hoboken, N.J.) · 2015Article
- Cytoskeletal tropomyosins: choreographers of actin filament functional diversity.Journal of muscle research and cell motility · 2013Review
- Article
- Srv2/cyclase-associated protein forms hexameric shurikens that directly catalyze actin filament severing by cofilin.Molecular biology of the cell · 2013Article
- Elevated tropomyosin expression is associated with epithelial-mesenchymal transition of lens epithelial cells.Journal of cellular and molecular medicine · 2013Article
- Controlling the cortical actin motor.Protoplasma · 2012Review
- Dynamic remodeling of the actin cytoskeleton by FMNL1γ is required for structural maintenance of the Golgi complex.Journal of cell science · 2011Article
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Authors and funding
6 authors.
Funding
Abstract
The balance between dynamic and stable actin filaments is essential for the regulation of cellular functions including the determination of cell shape and polarity, cell migration, and cytokinesis. Proteins that regulate polymerization at the filament ends and filament stability confer specificity to actin filament structure and cellular function. The dynamics of the barbed, fast-growing end of the filament are controlled in space and time by both positive and negative regulators of actin polymerization. Capping proteins inhibit the addition and loss of subunits, whereas other proteins, including formins, bind at the barbed end and allow filament growth. In this work, we show that tropomyosin regulates dynamics at the barbed end. Tropomyosin binds to constructs of FRL1 and mDia2 that contain the FH2 domain and modulates formin-dependent capping of the barbed end by relieving inhibition of elongation by FRL1-FH1FH2, mDia1-FH2, and mDia2-FH2 in an isoform-dependent fashion. In this role, tropomyosin functions as an activator of formin. Tropomyosin also inhibits the binding of FRL1-FH1FH2 to the sides of actin filaments independent of the isoform. In contrast, tropomyosin does not affect the ability of capping protein to block the barbed end. We suggest that tropomyosin and formin act together to ensure the formation of unbranched actin filaments, protected from severing, that could be capped in stable cellular structures. This role, in addition to its cooperative control of myosin function, establishes tropomyosin as a universal regulator of the multifaceted actin cytoskeleton.
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