title: Role of septins in the orientation of forespore membrane extension during sporulation in fission yeast.
abstract: During yeast sporulation, a forespore membrane (FSM) initiates at each spindle-pole body and extends to form the spore envelope. We used Schizosaccharomyces pombe to investigate the role of septins during this process. During the prior conjugation of haploid cells, the four vegetatively expressed septins (Spn1, Spn2, Spn3, and Spn4) coassemble at the fusion site and are necessary for its normal morphogenesis. Sporulation involves a different set of four septins (Spn2, Spn5, Spn6, and the atypical Spn7) that does not include the core subunits of the vegetative septin complex. The four sporulation septins form a complex in vitro and colocalize interdependently to a ring-shaped structure along each FSM, and septin mutations result in disoriented FSM extension. The septins and the leading-edge proteins appear to function in parallel to orient FSM extension. Spn2 and Spn7 bind to phosphatidylinositol 4-phosphate [PtdIns(4)P] in vitro, and PtdIns(4)P is enriched in the FSMs, suggesting that septins bind to the FSMs via this lipid. Cells expressing a mutant Spn2 protein unable to bind PtdIns(4)P still form extended septin structures, but these structures fail to associate with the FSMs, which are frequently disoriented. Thus, septins appear to form a scaffold that helps to guide the oriented extension of the FSM.
authors.affiliation: Department of Genetics, Stanford University School of Medicine, Stanford, CA 94305, USA. onishi@stanford.edu
authors.forename: Masayuki
authors.initials: M
authors.lastname: Onishi
authors.forename: Takako
authors.initials: T
authors.lastname: Koga
authors.forename: Aiko
authors.initials: A
authors.lastname: Hirata
authors.forename: Taro
authors.initials: T
authors.lastname: Nakamura
authors.forename: Haruhiko
authors.initials: H
authors.lastname: Asakawa
authors.forename: Chikashi
authors.initials: C
authors.lastname: Shimoda
authors.forename: Jürg
authors.initials: J
authors.lastname: Bähler
authors.forename: Jian-Qiu
authors.initials: JQ
authors.lastname: Wu
authors.forename: Kaoru
authors.initials: K
authors.lastname: Takegawa
authors.forename: Hiroyuki
authors.initials: H
authors.lastname: Tachikawa
authors.forename: John R
authors.initials: JR
authors.lastname: Pringle
authors.forename: Yasuhisa
authors.initials: Y
authors.lastname: Fukui
mesh_terms: D000595:Amino Acid Sequence; D002462:Cell Membrane / Q000378:metabolism* / Q000648:ultrastructure; D022081:Cell Surface Extensions / Q000378:metabolism* / Q000648:ultrastructure; D019204:GTP-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D009154:Mutation; D018129:Phosphatidylinositol Phosphates / Q000378:metabolism; D012568:Schizosaccharomyces / Q000166:cytology / Q000502:physiology; D029702:Schizosaccharomyces pombe Proteins / Q000235:genetics / Q000378:metabolism*; D016415:Sequence Alignment; D013172:Spores, Fungal / Q000502:physiology / Q000648:ultrastructure
chemical_list: D018129:Phosphatidylinositol Phosphates; D029702:Schizosaccharomyces pombe Proteins; D019204:GTP-Binding Proteins