The function of Sec1/Munc18 proteins - Solution of the mystery in sight?

Maria Kauppi, Jussi Jäntti, Vesa M. Olkkonen

    Research output: Chapter in Book/Report/Conference proceedingChapter or book articleScientificpeer-review


    Members of the Secl/Munc18 (SM) protein family form a central part of the machinery responsible for transport vesicle docking and fusion. Their hallmark property is interaction with SNARE proteins belonging to the syntaxin family. A wealth of evidence proposes an essential positive role for SM proteins in the different intracellular trafficking events in all cell types and organisms studied. However, the exact nature of their function is not understood. The existing data suggests functions as chaperones of syntaxins, in transport vesicle docking, promotion of SNARE complex formation, and in fusion pore opening. Intriguingly, all SM proteins do not bind their cognate syntaxin partners in a similar manner, but four different binding modes can be distinguished. This suggests that the unifying factor in SM function is not an intimate tight-fitting contact with syntaxins. We propose here a model, based on increasing experimental evidence that the key function of SM proteins is to bridge the Rab-GTPase dependent machineries of transport vesicle tethering and the SNARE apparatus responsible for vesicle docking and fusion.
    Original languageEnglish
    Title of host publicationRegulatory Mechanisms of Intracellular Membrane Transport. Keränen, S.; Jäntti, J. (Eds). Topics in Current Genetics : 10
    EditorsSirkka Keränen, Jussi Jäntti
    Place of PublicationBerlin - Heidelberg - New York
    ISBN (Electronic)978-3-540-44476-3
    ISBN (Print)978-3-540-22302-3
    Publication statusPublished - 2004
    MoE publication typeA3 Part of a book or another research book

    Publication series

    SeriesTopics in Current Genetics


    • proteins
    • SNARE proteins
    • transport vesicle docking
    • syntaxin


    Dive into the research topics of 'The function of Sec1/Munc18 proteins - Solution of the mystery in sight?'. Together they form a unique fingerprint.

    Cite this