ArticleThe Journal of cell biology1998
FH3, a domain found in formins, targets the fission yeast formin Fus1 to the projection tip during conjugation.
Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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Who cites it
65 citing papers in PubMed, 161 citations in OpenAlex.
- Constitutively active RAS prolongs Cdc42 signalling, while MAPK signalling is attenuated during fission yeast mating.PLoS genetics · 2026Article
- Genome-Wide Characterization and Analysis of theGenes · 2025Article
- Condensation of the fusion focus by the intrinsically disordered region of the formin Fus1 is essential for cell-cell fusion.Current biology : CB · 2022Article
- Actin assembly requirements of the formin Fus1 to build the fusion focus.Journal of cell science · 2022Article
- Formin Cdc12's specific actin assembly properties are tailored for cytokinesis in fission yeast.Biophysical journal · 2021Article
- Profilin's Affinity for Formin Regulates the Availability of Filament Ends for Actin Monomer Binding.Journal of molecular biology · 2020Article
- Mechanisms of formin-mediated actin assembly and dynamics.Biophysical reviews · 2018Review
- Dissection of two parallel pathways for formin-mediated actin filament elongation.The Journal of biological chemistry · 2018Article
- A systematic screen for morphological abnormalities during fission yeast sexual reproduction identifies a mechanism of actin aster formation for cell fusion.PLoS genetics · 2017Article
- Control of Formin Distribution and Actin Cable Assembly by the E3 Ubiquitin Ligases Dma1 and Dma2.Genetics · 2016Article
- Phosphorylation of the amino-terminus of the AGC kinase Gad8 prevents its interaction with TORC2.Open biology · 2016Article
- A formin-nucleated actin aster concentrates cell wall hydrolases for cell fusion in fission yeast.The Journal of cell biology · 2015Article
- The diaphanous gene of Drosophila interacts antagonistically with multiple wing hairs and plays a key role in wing hair morphogenesis.PloS one · 2015Article
- Formins as effector proteins of Rho GTPases.Small GTPases · 2014Review
- The formins Cdc12 and For3 cooperate during contractile ring assembly in cytokinesis.The Journal of cell biology · 2013Article
- SIN-dependent phosphoinhibition of formin multimerization controls fission yeast cytokinesis.Genes & development · 2013Article
- Mate and fuse: how yeast cells do it.Open biology · 2013Review
- Nonmedially assembled F-actin cables incorporate into the actomyosin ring in fission yeast.The Journal of cell biology · 2012Article
- Ndm, a coiled-coil domain protein that suppresses macropinocytosis and has effects on cell migration.Molecular biology of the cell · 2012Article
- Formins: emerging players in the dynamic plant cell cortex.Scientifica · 2012Review
5 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Formins are involved in diverse aspects of morphogenesis, and share two regions of homology: FH1 and FH2. We describe a new formin homology region, FH3. FH3 is an amino-terminal domain that differs from the Rho binding site identified in Bni1p and p140mDia. The Schizosaccharomyces pombe formin Fus1 is required for conjugation, and is localized to the projection tip in cells of mating pairs. We replaced genomic fus1+ with green fluorescent protein (GFP)- tagged versions that lacked either the FH1, FH2, or FH3 domain. Deletion of any FH domain essentially abolished mating. FH3, but neither FH1 nor FH2, was required for Fus1 localization. An FH3 domain-GFP fusion protein localized to the projection tips of mating pairs. Thus, the FH3 domain alone can direct protein localization. The FH3 domains of both Fus1 and the S. pombe cytokinesis formin Cdc12 were able to localize GFP to the spindle pole body in half of the late G2 cells in a vegetatively growing population. Expression of both FH3-GFP fusions also affected cytokinesis. Overexpression of the spindle pole body component Sad1 altered the distribution of both Sad1 and the FH3-GFP domain. Together these data suggest that proteins at multiple sites can interact with FH3 domains.
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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.