%0 Journal Article
%T The Syp1/FCHo2 protein induces septin filament bundling through its intrinsically disordered domain
%+ Centre de recherche en Biologie cellulaire de Montpellier (CRBM)
%+ Institut de Recherche en Infectiologie de Montpellier (IRIM)
%+ Centre de Biologie Structurale [Montpellier] (CBS)
%+ Institut des Neurosciences de Montpellier (INM)
%+ Centre d’études des Maladies Infectieuses et Pharmacologie Anti-Infectieuse -  [Montpellier] (CEMIPAI)
%+ Laboratoire Charles Coulomb (L2C)
%+ Institut universitaire de France (IUF)
%A Ibanes, Sandy
%A El Alaoui, Fatima
%A Him, Josephine Lai Kee
%A Cazevieille, Chantal
%A Hoh, François
%A Lyonnais, Sébastien
%A Bron, Patrick
%A Cipelletti, Luca
%A Picas, Laura
%A Piatti, Simonetta
%< avec comité de lecture
%@ 2211-1247
%J Cell Reports
%I Elsevier Inc
%V 41
%N 10
%P 111765
%8 2022-12
%D 2022
%R 10.1016/j.celrep.2022.111765
%M 36476870
%K CP: Cell biology
%K Cytokinesis
%K F-BAR
%K FCHo2
%K Syp1
%K budding yeast
%K septin
%K unstructured domains
%Z Life Sciences [q-bio]/Cellular BiologyJournal articles
%X The septin collar of budding yeast is an ordered array of septin filaments that serves a scaffolding function for the cytokinetic machinery at the bud neck and compartmentalizes the membrane between mother and daughter cell. How septin architecture is aided by septin-binding proteins is largely unknown. Syp1 is an endocytic protein that was implicated in the timely recruitment of septins to the newly forming collar through an unknown mechanism. Using advanced microscopy and in vitro reconstitution assays, we show that Syp1 is able to align laterally and tightly pack septin filaments, thereby forming flat bundles or sheets. This property is shared by the Syp1 mammalian counterpart FCHo2, thus emphasizing conserved protein functions. Interestingly, the septin-bundling activity of Syp1 resides mainly in its intrinsically disordered region. Our data uncover the mechanism through which Syp1 promotes septin collar assembly and offer another example of functional diversity of unstructured protein domains.
%G English
%2 https://hal.umontpellier.fr/hal-04114167/document
%2 https://hal.umontpellier.fr/hal-04114167/file/2022-Cell%20report.pdf
%L hal-04114167
%U https://hal.umontpellier.fr/hal-04114167
%~ CNRS
%~ CRBM
%~ INM
%~ CBS
%~ L2C
%~ UNIV-MONTPELLIER
%~ ANR
%~ UM-2015-2021
%~ UM-EPE
%~ IRIM