UCL  IRIS
Institutional Research Information Service
UCL Logo
Please report any queries concerning the funding data grouped in the sections named "Externally Awarded" or "Internally Disbursed" (shown on the profile page) to your Research Finance Administrator. Your can find your Research Finance Administrator at http://www.ucl.ac.uk/finance/research/post_award/post_award_contacts.php by entering your department
Please report any queries concerning the student data shown on the profile page to:

Email: portico-services@ucl.ac.uk

Help Desk: http://www.ucl.ac.uk/ras/portico/helpdesk
Publication Detail
Role of septins in the orientation of forespore membrane extension during sporulation in fission yeast.
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Journal Article
  • Authors:
    Onishi M, Koga T, Hirata A, Nakamura T, Asakawa H, Shimoda C, Bähler J, Wu J-Q, Takegawa K, Tachikawa H, Pringle JR, Fukui Y
  • Publication date:
    04/2010
  • Pagination:
    2057, 2074
  • Journal:
    Mol Cell Biol
  • Volume:
    30
  • Issue:
    8
  • Status:
    Published
  • Country:
    United States
  • PII:
    MCB.01529-09
  • Language:
    eng
  • Keywords:
    Amino Acid Sequence, Cell Membrane, Cell Surface Extensions, GTP-Binding Proteins, Molecular Sequence Data, Mutation, Phosphatidylinositol Phosphates, Schizosaccharomyces, Schizosaccharomyces pombe Proteins, Sequence Alignment, Spores, Fungal
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.
Publication data is maintained in RPS. Visit https://rps.ucl.ac.uk
 More search options
UCL Researchers
Author
Genetics, Evolution & Environment
University College London - Gower Street - London - WC1E 6BT Tel:+44 (0)20 7679 2000

© UCL 1999–2011

Search by