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Título: | The putative exchange factor Gef3p interacts with Rho3p GTPase and the septin ring during cytokinesis in fission yeast |
Autor: | Muñoz, Sofía CSIC ORCID; Manjón, Elvira CSIC ORCID CVN; Sánchez, Yolanda CSIC | Palabras clave: | Yeast genetics Rho GTPases Morphogenesis Guanine nucleotide exchange factor (GEF) Cytokinesis |
Fecha de publicación: | 2014 | Editor: | American Society for Biochemistry and Molecular Biology | Citación: | Journal of Biological Chemistry 289(32): 21995-22007 (2014) | Resumen: | 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. | URI: | http://hdl.handle.net/10261/116249 | DOI: | 10.1074/jbc.M114.548792 | Identificadores: | doi: 10.1074/jbc.M114.548792 issn: 0021-9258 e-issn: 1083-351X |
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