Show simple item record

dc.contributor.authorNkosi, Pedro Junior
dc.contributor.authorTargosz, Bianca-Sabrina
dc.contributor.authorLabib, Karim
dc.contributor.authorSanchez-Diaz, Alberto
dc.date.accessioned2013-04-05T12:58:26Z
dc.date.available2013-04-05T12:58:26Z
dc.date.issued2013
dc.identifier.citationHof1 and Rvs167 have redundant roles in actomyosin ring function during cytokinesis in budding yeast. 2013, 8 (2):e57846 PLoS ONEen_GB
dc.identifier.issn1932-6203
dc.identifier.pmid23469085
dc.identifier.doi10.1371/journal.pone.0057846
dc.identifier.urihttp://hdl.handle.net/10541/279113
dc.description.abstractThe Hof1 protein (Homologue of Fifteen) regulates formation of the primary septum during cytokinesis in the budding yeast , whereas the orthologous Cdc15 protein in fission yeast regulates the actomyosin ring by using its F-BAR domain to recruit actin nucleators to the cleavage site. Here we show that budding yeast Hof1 also contributes to actin ring assembly in parallel with the Rvs167 protein. Simultaneous deletion of the and genes is lethal, and cells fail to assemble the actomyosin ring as they progress through mitosis. Although Hof1 and Rvs167 are not orthologues, they both share an analogous structure, with an F-BAR or BAR domain at the amino terminus, capable of inducing membrane curvature, and SH3 domains at the carboxyl terminus that bind to specific proline-rich targets. The SH3 domain of Rvs167 becomes essential for assembly of the actomyosin ring in cells lacking Hof1, suggesting that it helps to recruit a regulator of the actin cytoskeleton. This new function of Rvs167 appears to be independent of its known role as a regulator of the Arp2/3 actin nucleator, as actin ring assembly is not abolished by the simultaneous inactivation of Hof1 and Arp2/3. Instead we find that recruitment to the bud-neck of the Iqg1 actin regulator is defective in cells lacking Hof1 and Rvs167, though future studies will be needed to determine if this reflects a direct interaction between these factors. The redundant role of Hof1 in actin ring assembly suggests that the mechanism of actin ring assembly has been conserved to a greater extent across evolution than anticipated previously.
dc.language.isoenen
dc.rightsArchived with thanks to PloS oneen_GB
dc.titleHof1 and Rvs167 have redundant roles in actomyosin ring function during cytokinesis in budding yeast.en
dc.typeArticleen
dc.contributor.departmentPaterson Institute for Cancer Research, University of Manchester, Manchester, United Kingdom.en_GB
dc.identifier.journalPLoS ONEen_GB
html.description.abstractThe Hof1 protein (Homologue of Fifteen) regulates formation of the primary septum during cytokinesis in the budding yeast , whereas the orthologous Cdc15 protein in fission yeast regulates the actomyosin ring by using its F-BAR domain to recruit actin nucleators to the cleavage site. Here we show that budding yeast Hof1 also contributes to actin ring assembly in parallel with the Rvs167 protein. Simultaneous deletion of the and genes is lethal, and cells fail to assemble the actomyosin ring as they progress through mitosis. Although Hof1 and Rvs167 are not orthologues, they both share an analogous structure, with an F-BAR or BAR domain at the amino terminus, capable of inducing membrane curvature, and SH3 domains at the carboxyl terminus that bind to specific proline-rich targets. The SH3 domain of Rvs167 becomes essential for assembly of the actomyosin ring in cells lacking Hof1, suggesting that it helps to recruit a regulator of the actin cytoskeleton. This new function of Rvs167 appears to be independent of its known role as a regulator of the Arp2/3 actin nucleator, as actin ring assembly is not abolished by the simultaneous inactivation of Hof1 and Arp2/3. Instead we find that recruitment to the bud-neck of the Iqg1 actin regulator is defective in cells lacking Hof1 and Rvs167, though future studies will be needed to determine if this reflects a direct interaction between these factors. The redundant role of Hof1 in actin ring assembly suggests that the mechanism of actin ring assembly has been conserved to a greater extent across evolution than anticipated previously.


This item appears in the following Collection(s)

Show simple item record