Reining in cytokinesis with a septin corral.
Septins are a family of conserved GTP-binding proteins that function in cytokinesis in fungi and animals. In budding yeast, septins form scaffolds for assembly of the actomyosin contractile ring at the cleavage plane, a role that does not appear to be conserved in other organisms. The septins form an hourglass-shaped collar at the mother-bud neck, which splits into two rings flanking the division plane at cytokinesis. A recent study(1) demonstrates that these two septin rings constitute diffusion barriers that create a cytokinetic compartment to retain cortical cytokinetic factors in proximity to the cleavage plane.
Finger
Fern P
FP
Biology Department, Rensselaer Polytechnic Institute, 110 8th St. Troy, NY 12180, USA. fingef@rpi.edu
D000818:Animals; D018797:Cell Cycle Proteins / Q000737:chemistry; D048749:Cytokinesis; D003598:Cytoskeletal Proteins / Q000737:chemistry / Q000502:physiology*; D004058:Diffusion; D005656:Fungal Proteins / Q000737:chemistry; D020558:GTP Phosphohydrolases / Q000737:chemistry; D019204:GTP-Binding Proteins / Q000737:chemistry; D006801:Humans; D046911:Macromolecular Substances / Q000737:chemistry; D008954:Models, Biological; D004718:Saccharomycetales
D018797:Cell Cycle Proteins; D003598:Cytoskeletal Proteins; D005656:Fungal Proteins; D046911:Macromolecular Substances; D020558:GTP Phosphohydrolases; D019204:GTP-Binding Proteins