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Opposite Surfaces of the Cdc15 F-BAR Domain Create a Membrane Platform That Coordinates Cytoskeletal and Signaling Components for Cytokinesis.
Snider, Chloe E; Chandra, Mintu; McDonald, Nathan A; Willet, Alaina H; Collier, Scott E; Ohi, Melanie D; Jackson, Lauren P; Gould, Kathleen L.
Afiliación
  • Snider CE; Department of Cell and Developmental Biology, Vanderbilt University, Nashville, TN 37232, USA.
  • Chandra M; Department of Biological Sciences, Vanderbilt University, Nashville, TN 37232, USA; Center for Structural Biology, Vanderbilt University, Nashville, TN 37232, USA.
  • McDonald NA; Department of Cell and Developmental Biology, Vanderbilt University, Nashville, TN 37232, USA.
  • Willet AH; Department of Cell and Developmental Biology, Vanderbilt University, Nashville, TN 37232, USA.
  • Collier SE; Center for Structural Biology, Vanderbilt University, Nashville, TN 37232, USA.
  • Ohi MD; Department of Cell and Developmental Biology, Vanderbilt University, Nashville, TN 37232, USA; Center for Structural Biology, Vanderbilt University, Nashville, TN 37232, USA.
  • Jackson LP; Department of Biological Sciences, Vanderbilt University, Nashville, TN 37232, USA; Center for Structural Biology, Vanderbilt University, Nashville, TN 37232, USA.
  • Gould KL; Department of Cell and Developmental Biology, Vanderbilt University, Nashville, TN 37232, USA. Electronic address: kathy.gould@vanderbilt.edu.
Cell Rep ; 33(12): 108526, 2020 12 22.
Article en En | MEDLINE | ID: mdl-33357436
Many eukaryotes assemble an actin- and myosin-based cytokinetic ring (CR) on the plasma membrane (PM) for cell division, but how it is anchored there remains unclear. In Schizosaccharomyces pombe, the F-BAR protein Cdc15 links the PM via its F-BAR domain to proteins in the CR's interior via its SH3 domain. However, Cdc15's F-BAR domain also directly binds formin Cdc12, suggesting that Cdc15 may polymerize a protein network directly adjacent to the membrane. Here, we determine that the F-BAR domain binds Cdc12 using residues on the face opposite its membrane-binding surface. These residues also bind paxillin-like Pxl1, promoting its recruitment with calcineurin to the CR. Mutation of these F-BAR domain residues results in a shallower CR, with components localizing ∼35% closer to the PM than in wild type, and aberrant CR constriction. Thus, F-BAR domains serve as oligomeric membrane-bound platforms that can modulate the architecture of an entire actin structure.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Citoesqueleto / Proteínas de Ciclo Celular / Proteínas de Unión al GTP / Proteínas de Schizosaccharomyces pombe / Citocinesis Límite: Humans Idioma: En Revista: Cell Rep Año: 2020 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Citoesqueleto / Proteínas de Ciclo Celular / Proteínas de Unión al GTP / Proteínas de Schizosaccharomyces pombe / Citocinesis Límite: Humans Idioma: En Revista: Cell Rep Año: 2020 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos