title: The F-BAR Cdc15 promotes contractile ring formation through the direct recruitment of the formin Cdc12.
abstract: In Schizosaccharomyces pombe, cytokinesis requires the assembly and constriction of an actomyosin-based contractile ring (CR). Nucleation of F-actin for the CR requires a single formin, Cdc12, that localizes to the cell middle at mitotic onset. Although genetic requirements for formin Cdc12 recruitment have been determined, the molecular mechanisms dictating its targeting to the medial cortex during cytokinesis are unknown. In this paper, we define a short motif within the N terminus of Cdc12 that binds directly to the F-BAR domain of the scaffolding protein Cdc15. Mutations preventing the Cdc12-Cdc15 interaction resulted in reduced Cdc12, F-actin, and actin-binding proteins at the CR, which in turn led to a delay in CR formation and sensitivity to other perturbations of CR assembly. We conclude that Cdc15 contributes to CR formation and cytokinesis via formin Cdc12 recruitment, defining a novel cytokinetic function for an F-BAR domain.
authors: Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232.
authors: Alaina H
authors: AH
authors: Willet
authors: Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232.
authors: Nathan A
authors: NA
authors: McDonald
authors: Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232.
authors: K Adam
authors: KA
authors: Bohnert
authors: National High Magnetic Field Laboratory and Department of Biological Science, The Florida State University, Tallahassee, FL 32306 National High Magnetic Field Laboratory and Department of Biological Science, The Florida State University, Tallahassee, FL 32306.
authors: Michelle A
authors: MA
authors: Baird
authors: National High Magnetic Field Laboratory and Department of Biological Science, The Florida State University, Tallahassee, FL 32306 National High Magnetic Field Laboratory and Department of Biological Science, The Florida State University, Tallahassee, FL 32306.
authors: John R
authors: JR
authors: Allen
authors: National High Magnetic Field Laboratory and Department of Biological Science, The Florida State University, Tallahassee, FL 32306 National High Magnetic Field Laboratory and Department of Biological Science, The Florida State University, Tallahassee, FL 32306.
authors: Michael W
authors: MW
authors: Davidson
authors: Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232 kathy.gould@vanderbilt.edu.
authors: Kathleen L
authors: KL
authors: Gould
mesh_terms: D008841:Actin Cytoskeleton / Q000378:metabolism*; D000199:Actins / Q000378:metabolism; D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D018797:Cell Cycle Proteins / Q000235:genetics / Q000378:metabolism*; D003285:Contractile Proteins / Q000235:genetics / Q000378:metabolism*; D048749:Cytokinesis / Q000235:genetics / Q000502:physiology; D003598:Cytoskeletal Proteins / Q000235:genetics / Q000378:metabolism*; D019204:GTP-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D020690:GTPase-Activating Proteins / Q000235:genetics; D009154:Mutation; D024462:Myosin Type II / Q000235:genetics; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D012568:Schizosaccharomyces / Q000166:cytology* / Q000235:genetics / Q000378:metabolism; D029702:Schizosaccharomyces pombe Proteins / Q000235:genetics / Q000378:metabolism*; D016415:Sequence Alignment; D017385:Sequence Homology
chemical_list: D000199:Actins; C082279:CDC15 protein; C531994:Cdc12 protein, S pombe; D018797:Cell Cycle Proteins; D003285:Contractile Proteins; D003598:Cytoskeletal Proteins; D020690:GTPase-Activating Proteins; C114172:Rng2 protein, S pombe; D029702:Schizosaccharomyces pombe Proteins; D019204:GTP-Binding Proteins; D024462:Myosin Type II