A tripartite SNARE-K+ channel complex involved in Arabidopsis potassium nutrition

Annegret Honsbein, Sergei Sokolovski, Prisca Campanoni, Rejane Pratelli, Manuel Paneque, Ingela Johansson, Michael Blatt

    Research output: Contribution to journalSpecial issue

    Abstract

    In addition to their roles in vesicle delivery and fusion, a few membrane trafficking (SNARE) proteins interact with ion channels, notably mammalian Syntaxin1A which binds to specific Ca2+ and K+ channels in nerves and neuroendocrine tissues to modulate their gating properties. Such interactions have been thought to be restricted to mammalian tissues in which they serve highly specialized roles to facilitate signaling and its coupling to membrane traffic. We discovered that the SNARE protein SYP121 of the model plant Arabidopsis binds directly and selectively to the regulatory (‘silent') K+ channel subunit KC1, which assembles with different inward-rectifying Shaker K+ channels to affect their activities. The Shaker subunits AKT1 and KC1 form heterotetramers that are involved in potassium uptake at the root hair and epidermis. We found that SYP121 promotes gating of the inward-rectifying K+ channel AKT1 when heterologously co-expressed with KC1, and that the SYP121–KC1 complex is essential in vivo for AKT1-associated K+ current, channel-mediated K+ uptake at the root epidermis and for growth. These results demonstrate a role for a SNARE as part of protein complex facilitating plant mineral nutrition and they implicate additional roles for SNARE binding to control the activity of other ion channels through the common KC1 subunit
    Original languageEnglish
    Pages (from-to)S190-S190
    Number of pages1
    JournalComparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology
    Volume153
    Issue number2
    DOIs
    Publication statusPublished - 2009

    Cite this

    Honsbein, Annegret ; Sokolovski, Sergei ; Campanoni, Prisca ; Pratelli, Rejane ; Paneque, Manuel ; Johansson, Ingela ; Blatt, Michael. / A tripartite SNARE-K+ channel complex involved in Arabidopsis potassium nutrition. In: Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology. 2009 ; Vol. 153, No. 2. pp. S190-S190.
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    title = "A tripartite SNARE-K+ channel complex involved in Arabidopsis potassium nutrition",
    abstract = "In addition to their roles in vesicle delivery and fusion, a few membrane trafficking (SNARE) proteins interact with ion channels, notably mammalian Syntaxin1A which binds to specific Ca2+ and K+ channels in nerves and neuroendocrine tissues to modulate their gating properties. Such interactions have been thought to be restricted to mammalian tissues in which they serve highly specialized roles to facilitate signaling and its coupling to membrane traffic. We discovered that the SNARE protein SYP121 of the model plant Arabidopsis binds directly and selectively to the regulatory (‘silent') K+ channel subunit KC1, which assembles with different inward-rectifying Shaker K+ channels to affect their activities. The Shaker subunits AKT1 and KC1 form heterotetramers that are involved in potassium uptake at the root hair and epidermis. We found that SYP121 promotes gating of the inward-rectifying K+ channel AKT1 when heterologously co-expressed with KC1, and that the SYP121–KC1 complex is essential in vivo for AKT1-associated K+ current, channel-mediated K+ uptake at the root epidermis and for growth. These results demonstrate a role for a SNARE as part of protein complex facilitating plant mineral nutrition and they implicate additional roles for SNARE binding to control the activity of other ion channels through the common KC1 subunit",
    author = "Annegret Honsbein and Sergei Sokolovski and Prisca Campanoni and Rejane Pratelli and Manuel Paneque and Ingela Johansson and Michael Blatt",
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    A tripartite SNARE-K+ channel complex involved in Arabidopsis potassium nutrition. / Honsbein, Annegret; Sokolovski, Sergei; Campanoni, Prisca; Pratelli, Rejane; Paneque, Manuel; Johansson, Ingela; Blatt, Michael.

    In: Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology, Vol. 153, No. 2, 2009, p. S190-S190.

    Research output: Contribution to journalSpecial issue

    TY - JOUR

    T1 - A tripartite SNARE-K+ channel complex involved in Arabidopsis potassium nutrition

    AU - Honsbein, Annegret

    AU - Sokolovski, Sergei

    AU - Campanoni, Prisca

    AU - Pratelli, Rejane

    AU - Paneque, Manuel

    AU - Johansson, Ingela

    AU - Blatt, Michael

    PY - 2009

    Y1 - 2009

    N2 - In addition to their roles in vesicle delivery and fusion, a few membrane trafficking (SNARE) proteins interact with ion channels, notably mammalian Syntaxin1A which binds to specific Ca2+ and K+ channels in nerves and neuroendocrine tissues to modulate their gating properties. Such interactions have been thought to be restricted to mammalian tissues in which they serve highly specialized roles to facilitate signaling and its coupling to membrane traffic. We discovered that the SNARE protein SYP121 of the model plant Arabidopsis binds directly and selectively to the regulatory (‘silent') K+ channel subunit KC1, which assembles with different inward-rectifying Shaker K+ channels to affect their activities. The Shaker subunits AKT1 and KC1 form heterotetramers that are involved in potassium uptake at the root hair and epidermis. We found that SYP121 promotes gating of the inward-rectifying K+ channel AKT1 when heterologously co-expressed with KC1, and that the SYP121–KC1 complex is essential in vivo for AKT1-associated K+ current, channel-mediated K+ uptake at the root epidermis and for growth. These results demonstrate a role for a SNARE as part of protein complex facilitating plant mineral nutrition and they implicate additional roles for SNARE binding to control the activity of other ion channels through the common KC1 subunit

    AB - In addition to their roles in vesicle delivery and fusion, a few membrane trafficking (SNARE) proteins interact with ion channels, notably mammalian Syntaxin1A which binds to specific Ca2+ and K+ channels in nerves and neuroendocrine tissues to modulate their gating properties. Such interactions have been thought to be restricted to mammalian tissues in which they serve highly specialized roles to facilitate signaling and its coupling to membrane traffic. We discovered that the SNARE protein SYP121 of the model plant Arabidopsis binds directly and selectively to the regulatory (‘silent') K+ channel subunit KC1, which assembles with different inward-rectifying Shaker K+ channels to affect their activities. The Shaker subunits AKT1 and KC1 form heterotetramers that are involved in potassium uptake at the root hair and epidermis. We found that SYP121 promotes gating of the inward-rectifying K+ channel AKT1 when heterologously co-expressed with KC1, and that the SYP121–KC1 complex is essential in vivo for AKT1-associated K+ current, channel-mediated K+ uptake at the root epidermis and for growth. These results demonstrate a role for a SNARE as part of protein complex facilitating plant mineral nutrition and they implicate additional roles for SNARE binding to control the activity of other ion channels through the common KC1 subunit

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    DO - 10.1016/j.cbpa.2009.04.422

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    SN - 1095-6433

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