Rho1- and Pkc1-dependent phosphorylation of the F-BAR protein Syp1 contributes to septin ring assembly

Laura Merlini, Alessio Bolognesi, Maria Angeles Juanes, Franck Vandermoere, Thibault Courtellemont, Roberto Pascolutti, Martial Séveno, Yves Barral, Simonetta Piatti

    Research output: Contribution to journalArticle

    Abstract

    In many cell types, septins assemble into filaments and rings at the neck of cellular appendages and/or at the cleavage furrow to help compartmentalize the plasma membrane and support cytokinesis. How septin ring assembly is coordinated with membrane remodeling and controlled by mechanical stress at these sites is unclear. Through a genetic screen, we uncovered an unanticipated link between the conserved Rho1 GTPase and its effector protein kinase C (Pkc1) with septin ring stability in yeast. Both Rho1 and Pkc1 stabilize the septin ring, at least partly through phosphorylation of the membrane-associated F-BAR protein Syp1, which colocalizes asymmetrically with the septin ring at the bud neck. Syp1 is displaced from the bud neck upon Pkc1-dependent phosphorylation at two serines, thereby affecting the rigidity of the new-forming septin ring. We propose that Rho1 and Pkc1 coordinate septin ring assembly with membrane and cell wall remodeling partly by controlling Syp1 residence at the bud neck.
    Original languageEnglish
    Pages (from-to)3245-62
    Number of pages18
    JournalMolecular Biology of the Cell
    Volume26
    Issue number18
    DOIs
    Publication statusPublished - 15 Jul 2015

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    Merlini, L., Bolognesi, A., Juanes, M. A., Vandermoere, F., Courtellemont, T., Pascolutti, R., Séveno, M., Barral, Y., & Piatti, S. (2015). Rho1- and Pkc1-dependent phosphorylation of the F-BAR protein Syp1 contributes to septin ring assembly. Molecular Biology of the Cell, 26(18), 3245-62. https://doi.org/10.1091/mbc.E15-06-0366