%0 Journal Article
%T Phosphorylation of the F-BAR protein Hof1 drives septin ring splitting in budding yeast
%+ Centre de recherche en Biologie cellulaire de Montpellier (CRBM)
%+ Université Sorbonne Paris Cité (USPC)
%+ Institut Jacques Monod (IJM (UMR_7592))
%+ Centre de Biologie Structurale [Montpellier] (CBS)
%+ Laboratoire Charles Coulomb (L2C)
%+ Institut universitaire de France (IUF)
%+ Institut de Recherche en Infectiologie de Montpellier (IRIM)
%A Varela Salgado, Maritzaida
%A Adriaans, Ingrid, E
%A Touati, Sandra, A
%A Ibanes, Sandy
%A Lai-Kee-Him, Joséphine
%A Ancelin, Aurélie
%A Cipelletti, Luca
%A Picas, Laura
%A Piatti, Simonetta
%Z FRM project EQU202303016309FRM project FDT202106012881
%< avec comité de lecture
%@ 2041-1723
%J Nature Communications
%I Nature Publishing Group
%V 15
%N 1
%P 3383
%8 2024-04-22
%D 2024
%R 10.1038/s41467-024-47709-3
%M 38649354
%K cytokinesis
%K septins
%K Mitotic exit network
%K F-BAR protein
%Z Life Sciences [q-bio]Journal articles
%X 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.
%G English
%2 https://hal.science/hal-04732675v1/document
%2 https://hal.science/hal-04732675v1/file/published.pdf
%L hal-04732675
%U https://hal.science/hal-04732675
%~ INSERM
%~ CNRS
%~ IJM
%~ CRBM
%~ CBS
%~ L2C
%~ UNIV-MONTPELLIER
%~ UNIV-PARIS
%~ UNIVERSITE-PARIS
%~ UP-SCIENCES
%~ ANR
%~ UM-2015-2021
%~ UM-EPE
%~ FRM
%~ IRIM