ArticleMolecular biology of the cell2009
Role of tropomyosin in formin-mediated contractile ring assembly in fission yeast.
Article in Molecular biology of the cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 70 citations in OpenAlex.
- mNG-tagged fusion proteins and nanobodies to visualize tropomyosins in yeast and mammalian cells.Journal of cell science · 2022Article
- Review
- Specialization of actin isoforms derived from the loss of key interactions with regulatory factors.The EMBO journal · 2022Article
- Cooperative bundling by fascin generates actin structures with architectures that depend on filament length.Frontiers in cell and developmental biology · 2022Article
- Deletion of the Actin-Associated TropomyosinCells · 2021Article
- Diversity from similarity: cellular strategies for assigning particular identities to actin filaments and networks.Open biology · 2020Article
- Phosphoregulation of tropomyosin-actin interaction revealed using a genetic code expansion strategy.Wellcome open research · 2020Article
- Capping Protein Insulates Arp2/3-Assembled Actin Patches from Formins.Current biology : CB · 2019Article
- Sizes of actin networks sharing a common environment are determined by the relative rates of assembly.PLoS biology · 2019Article
- Dip1 Co-opts Features of Branching Nucleation to Create Linear Actin Filaments that Activate WASP-Bound Arp2/3 Complex.Current biology : CB · 2018Article
- Tropomyosin 3.5 protects the F-actin networks required for tissue biomechanical properties.Journal of cell science · 2018Article
- Helical rotation of the diaphanous-related formin mDia1 generates actin filaments resistant to cofilin.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Interaction between cardiac myosin-binding protein C and formin Fhod3.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Tropomyosin isoforms differentially affect muscle contractility in the head and body regions of the nematode Caenorhabditis elegans.Molecular biology of the cell · 2018Article
- Stabilization of F-actin by tropomyosin isoforms regulates the morphology and mechanical behavior of red blood cells.Molecular biology of the cell · 2017Article
- Article
- Tropomyosin and Profilin Cooperate to Promote Formin-Mediated Actin Nucleation and Drive Yeast Actin Cable Assembly.Current biology : CB · 2016Article
- The final cut: cell polarity meets cytokinesis at the bud neck in S. cerevisiae.Cellular and molecular life sciences : CMLS · 2016Review
- Coupling changes in cell shape to chromosome segregation.Nature reviews. Molecular cell biology · 2016Review
- The F-actin bundler α-actinin Ain1 is tailored for ring assembly and constriction during cytokinesis in fission yeast.Molecular biology of the cell · 2016Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Like animal cells, fission yeast divides by assembling actin filaments into a contractile ring. In addition to formin Cdc12p and profilin, the single tropomyosin isoform SpTm is required for contractile ring assembly. Cdc12p nucleates actin filaments and remains processively associated with the elongating barbed end while driving the addition of profilin-actin. SpTm is thought to stabilize mature filaments, but it is not known how SpTm localizes to the contractile ring and whether SpTm plays a direct role in Cdc12p-mediated actin polymerization. Using "bulk" and single actin filament assays, we discovered that Cdc12p can recruit SpTm to actin filaments and that SpTm has diverse effects on Cdc12p-mediated actin assembly. On its own, SpTm inhibits actin filament elongation and depolymerization. However, Cdc12p completely overcomes the combined inhibition of actin nucleation and barbed end elongation by profilin and SpTm. Furthermore, SpTm increases the length of Cdc12p-nucleated actin filaments by enhancing the elongation rate twofold and by allowing them to anneal end to end. In contrast, SpTm ultimately turns off Cdc12p-mediated elongation by "trapping" Cdc12p within annealed filaments or by dissociating Cdc12p from the barbed end. Therefore, SpTm makes multiple contributions to contractile ring assembly during and after actin polymerization.
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