Mso1p: A yeast protein that functions in secretion and interacts physically and genetically with Sec1p

Markku Aalto, Jussi Jäntti, Jonas Östling, Sirkka Keränen, Hans Ronne

    Research output: Contribution to journalArticleScientificpeer-review

    30 Citations (Scopus)

    Abstract

    The yeast Sec1p protein functions in the docking of secretory transport vesicles to the plasma membrane. We previously have cloned two yeast genes encoding syntaxins, SSO1 and SSO2, as suppressors of the temperature-sensitive sec1–1 mutation. We now describe a third suppressor of sec1–1, which we call MSO1. Unlike SSO1 and SSO2, MSO1 is specific for sec1 and does not suppress mutations in any other SEC genes. MSO1 encodes a small hydrophilic protein that is enriched in a microsomal membrane fraction. Cells that lack MSO1 are viable, but they accumulate secretory vesicles in the bud, indicating that the terminal step in secretion is partially impaired. Moreover, loss of MSO1 shows synthetic lethality with mutations in SEC1, SEC2, and SEC4, and other synthetic phenotypes with mutations in several other late-acting SEC genes. We further found that Mso1p interacts with Sec1p both in vitro and in the two-hybrid system. These findings suggest that Mso1p is a component of the secretory vesicle docking complex whose function is closely associated with that of Sec1p.
    Original languageEnglish
    Pages (from-to)7331-7336
    JournalProceedings of the National Academy of Sciences of the United States of America
    Volume94
    Issue number14
    DOIs
    Publication statusPublished - 1997
    MoE publication typeA1 Journal article-refereed

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