title: Septin pairs, a complex choreography.
abstract: Septins form a filamentous collar at the mother-bud neck in budding yeast. In cytokinesis, this collar splits into two rings and the septin complexes undergo a dramatic reorientation. Using fluorescence polarization microscopy, DeMay et al. (2011. J. Cell Biol. doi:10.1083/jcb.201012143) now demonstrate that septin complexes assemble as paired filaments in vivo and reveal new insights into septin organization during cytokinesis.
authors.affiliation: Institute of Biochemistry, Eidgenössische Technische Hochschule Zürich, 8093 Zürich, Switzerland.
authors.forename: Helge
authors.initials: H
authors.lastname: Ewers
mesh_terms: D048749:Cytokinesis / Q000502:physiology; D008856:Microscopy, Fluorescence / Q000379:methods*; D008954:Models, Biological; D012441:Saccharomyces cerevisiae / Q000166:cytology / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism*; D058112:Septins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D029701:Saccharomyces cerevisiae Proteins; D058112:Septins