Inn1 couples contraction of the actomyosin ring to membrane ingression during cytokinesis in budding yeast

Alberto Sanchez-Diaz, Vanessa Marchesi, Stephen Murray, Richard Jones, Gislene Pereira, Ricky Edmondson, Terry Allen, Karim Labib (Lead / Corresponding author)

    Research output: Contribution to journalArticlepeer-review

    67 Citations (Scopus)

    Abstract

    By rapidly depleting each of the essential budding yeast proteins of unknown function, we identified a novel factor that we call Inn1, which associates with the contractile actomyosin ring at the end of mitosis and is needed for cytokinesis. We show that Inn1 has a C2 domain at the amino terminus of the protein that is required for ingression of the plasma membrane, whereas the remainder of the protein recruits Inn1 to the actomyosin ring. The lethal effects of deleting the INN1 gene can be suppressed by artificial fusion of the C2 domain to other components of the actomyosin ring, restoring membrane ingression on contraction of the actomyosin ring. Our data indicate that recruitment of the C2 domain of Inn1 to the contractile actomyosin ring is crucial for ingression of the plasma membrane during cytokinesis in budding yeast.
    Original languageEnglish
    Pages (from-to)395-406
    Number of pages12
    JournalNature Cell Biology
    Volume10
    Issue number4
    DOIs
    Publication statusPublished - Apr 2008

    Keywords

    • Cell Cycle Proteins
    • Models, Molecular
    • Saccharomyces cerevisiae Proteins
    • Amino Acid Sequence
    • Recombinant Fusion Proteins
    • Saccharomyces cerevisiae
    • Cytoskeleton
    • Actomyosin
    • Sequence Alignment
    • Cytokinesis
    • Mitosis
    • Proteomics
    • Cell Membrane
    • Molecular Sequence Data
    • Cytoskeletal Proteins
    • Protein Conformation

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