title: Mid1p/anillin and the septation initiation network orchestrate contractile ring assembly for cytokinesis.
abstract: In both animal cells and fungi, cytokinesis proceeds via a contractile actomyosin ring (CAR). Many CAR components and regulators are evolutionarily conserved. In Schizosaccharomyces pombe, the spatial cue for cytokinesis is provided by Mid1p/Anillin, whereas temporal coordination is ensured by the septation initiation network (SIN). However, neither Mid1p nor the SIN is considered to be essential for CAR assembly per se. Here, using 4D imaging, we reveal an unanticipated, novel role for the SIN in CAR assembly. We demonstrate that CAR assembly involves three, genetically separable steps: establishment of a cortical network of CAR proteins, its lateral condensation, and finally, the formation of a homogeneous CAR. We show that SIN mutants fail to form a homogeneous CAR; we identify hypophosphorylation and recruitment of the conserved PCH-family protein Cdc15p to the CAR as critical steps requiring SIN function. Furthermore, we show that in the absence of Mid1p, CAR assembly proceeds via an actomyosin filament, rather than a cortical network of CAR proteins. This mode of assembly is totally dependent on SIN signaling, thereby demonstrating a direct role for the SIN in CAR formation. Taken together, these data establish that Mid1p and the SIN are the key regulators that orchestrate CAR assembly.
authors.affiliation: Cell Cycle Control Laboratory, Swiss Institute for Experimental Cancer Research (ISREC), School of Life Sciences, Ecole Polytechnique Fédérale de Lausanne (EPFL), 1066 Epalinges s/Lausanne, Switzerland.
authors.forename: Olivier
authors.initials: O
authors.lastname: Hachet
authors.forename: Viesturs
authors.initials: V
authors.lastname: Simanis
mesh_terms: D000205:Actomyosin / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D002453:Cell Cycle / Q000235:genetics / Q000502:physiology; D018797:Cell Cycle Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D003285:Contractile Proteins / Q000235:genetics / Q000378:metabolism* / Q000502:physiology*; D048749:Cytokinesis / Q000235:genetics / Q000502:physiology*; D019204:GTP-Binding Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D015966:Gene Expression Regulation, Fungal; D008954:Models, Biological; D017346:Protein Serine-Threonine Kinases / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D012568:Schizosaccharomyces / Q000166:cytology / Q000235:genetics / Q000378:metabolism; D029702:Schizosaccharomyces pombe Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*
chemical_list: C082279:CDC15 protein; D018797:Cell Cycle Proteins; D003285:Contractile Proteins; C489694:Mid1 protein, S pombe; D029702:Schizosaccharomyces pombe Proteins; C095886:anillin; D000205:Actomyosin; C489406:cdc7 protein, S pombe; D017346:Protein Serine-Threonine Kinases; D019204:GTP-Binding Proteins