Phosphorylation of the F-BAR protein Hof1 drives septin ring splitting in budding yeast

Maritzaida Varela Salgado, Ingrid E. Adriaans, Sandra A. Touati, Sandy Ibanes, Joséphine Lai-Kee-Him, Aurélie Ancelin, Luca Cipelletti, Laura Picas and Simonetta Piatti ()
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Maritzaida Varela Salgado: University of Montpellier
Ingrid E. Adriaans: University of Montpellier
Sandra A. Touati: Institut Jacques Monod
Sandy Ibanes: University of Montpellier
Joséphine Lai-Kee-Him: University of Montpellier
Aurélie Ancelin: University of Montpellier
Luca Cipelletti: University of Montpellier
Laura Picas: University of Montpellier
Simonetta Piatti: University of Montpellier

Nature Communications, 2024, vol. 15, issue 1, 1-17

Abstract: Abstract A double septin ring accompanies cytokinesis in yeasts and mammalian cells. In budding yeast, reorganisation of the septin collar at the bud neck into a dynamic double ring is essential for actomyosin ring constriction and cytokinesis. Septin reorganisation requires the Mitotic Exit Network (MEN), a kinase cascade essential for cytokinesis. However, the effectors of MEN in this process are unknown. Here we identify the F-BAR protein Hof1 as a critical target of MEN in septin remodelling. Phospho-mimicking HOF1 mutant alleles overcome the inability of MEN mutants to undergo septin reorganisation by decreasing Hof1 binding to septins and facilitating its translocation to the actomyosin ring. Hof1-mediated septin rearrangement requires its F-BAR domain, suggesting that it may involve a local membrane remodelling that leads to septin reorganisation. In vitro Hof1 can induce the formation of intertwined septin bundles, while a phosphomimetic Hof1 protein has impaired septin-bundling activity. Altogether, our data indicate that Hof1 modulates septin architecture in distinct ways depending on its phosphorylation status.

Date: 2024
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DOI: 10.1038/s41467-024-47709-3

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