ArticleThe Journal of biological chemistry2014
The putative exchange factor Gef3p interacts with Rho3p GTPase and the septin ring during cytokinesis in fission yeast.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 23 citations in OpenAlex.
- Article
- Article
- Localizations of the septin Spn4 tagged with GFP and mEGFP in fission yeast.microPublication biology · 2025Article
- The Roles of Septins in Regulating Fission Yeast Cytokinesis.Journal of fungi (Basel, Switzerland) · 2024Review
- Review
- Septin Assembly and Remodeling at the Cell Division Site During the Cell Cycle.Frontiers in cell and developmental biology · 2021Review
- Coordinating septum formation and the actomyosin ring during cytokinesis in Schizosaccharomyces pombe.Molecular microbiology · 2019Review
- Rho Family GTPases in Fission Yeast Cytokinesis.Communicative & integrative biology · 2019Review
- The price of independence: cell separation in fission yeast.World journal of microbiology & biotechnology · 2016Review
- Phosphorylation-dependent inhibition of Cdc42 GEF Gef1 by 14-3-3 protein Rad24 spatially regulates Cdc42 GTPase activity and oscillatory dynamics during cell morphogenesis.Molecular biology of the cell · 2015Article
- The Rho-GEF Gef3 interacts with the septin complex and activates the GTPase Rho4 during fission yeast cytokinesis.Molecular biology of the cell · 2015Article
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
The small GTP-binding proteins of the Rho family and its regulatory proteins play a central role in cytokinetic actomyosin ring assembly and cytokinesis. Here we show that the fission yeast guanine nucleotide exchange factor Gef3p interacts with Rho3p at the division site. Gef3p contains a putative DH homology domain and a BAR/IMD-like domain. The protein localized to the division site late in mitosis, where it formed a ring that did not constrict with actomyosin ring (cytokinetic actomyosin ring) invagination; instead, it split into a double ring that resembled the septin ring. Gef3p co-localized with septins and Mid2p and required septins and Mid2p for its localization. Gef3p interacts physically with the GTP-bound form of Rho3p. Although Gef3p is not essential for cell separation, the simultaneous disruption of gef3(+) and Rho3p-interacting proteins, such as Sec8p, an exocyst component, Apm1p, a subunit of the clathrin adaptor complex or For3p, an actin-polymerizing protein, yielded cells with strong defects in septation and polarity respectively. Our results suggest that interactions between septins and Rho-GEFs provide a new targeting mechanism for GTPases in cytokinesis, in this case probably contributing to Rho3p function in vesicle tethering and vesicle trafficking in the later steps of cell separation.
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