SNAREs at the traffic junction with signalling, transport and nutrition

M. Blatt, I. Johansson, M. Paneque, R. Pratelli, P. Campanoni, S. Sokolovski, A. Honsbein

    Research output: Contribution to journalSpecial issue

    Abstract

    SNARE proteins contribute to vesicle targeting and membrane fusion in all eukaryotic cells, and are essential to the mechanics of cell growth and development. Nonetheless, there is clear evidence that SNAREs play additional roles, for example in facilitating cellular signalling and synaptic transmission. I report here that SYP121, an Arabidopsis SNARE found at the plasma membrane, contributes to scaffolds that anchor ion channels within the plane of the membrane, and it is a critical structural element determining the K+ channel gating and K+ mineral nutrition. Work from my laboratory has shown that SYP121 interacts in vitro and in vivo with the regulatory (‘silent’) K+ channel subunit KC1 which assembles with different inward-rectifying K+ channels to affect their activities in the plant.SYP121-KC1 interaction was found to be specific to these two protein partners and to be essential for the activity of K+ channels, channel-mediated K+ uptake at the root epidermis and for growth. Electrophysiological studies have shown changes in channel gating that can only result from an altered conformation of the channel and profound changes in the exposure of the channel voltage sensor to the membrane electric field. Intriguingly, when heterologously expressed on its own AKT1 does yield an inward-rectifying K+ current, but its gating characteristics – and those of AKT1 expressed together with KC1 – differ significantly from the K+ current in vivo unless co-expressed together with SYP121. In short, SYP121 is a missing component of the K+ channel complex and is essential for its gating in the plant. These results demonstrate a wholly unexpected role for a SNARE in eukaryotes as part of protein complex facilitating mineral nutrition and wholly unrelated to signalling or to membrane vesicle traffic
    Original languageEnglish
    Pages (from-to)S141-S141
    Number of pages1
    JournalComparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology
    Volume150
    Issue number3
    DOIs
    Publication statusPublished - 2008

    Cite this

    Blatt, M., Johansson, I., Paneque, M., Pratelli, R., Campanoni, P., Sokolovski, S., & Honsbein, A. (2008). SNAREs at the traffic junction with signalling, transport and nutrition. Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology, 150(3), S141-S141. https://doi.org/10.1016/j.cbpa.2008.04.348
    Blatt, M. ; Johansson, I. ; Paneque, M. ; Pratelli, R. ; Campanoni, P. ; Sokolovski, S. ; Honsbein, A. / SNAREs at the traffic junction with signalling, transport and nutrition. In: Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology. 2008 ; Vol. 150, No. 3. pp. S141-S141.
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    abstract = "SNARE proteins contribute to vesicle targeting and membrane fusion in all eukaryotic cells, and are essential to the mechanics of cell growth and development. Nonetheless, there is clear evidence that SNAREs play additional roles, for example in facilitating cellular signalling and synaptic transmission. I report here that SYP121, an Arabidopsis SNARE found at the plasma membrane, contributes to scaffolds that anchor ion channels within the plane of the membrane, and it is a critical structural element determining the K+ channel gating and K+ mineral nutrition. Work from my laboratory has shown that SYP121 interacts in vitro and in vivo with the regulatory (‘silent’) K+ channel subunit KC1 which assembles with different inward-rectifying K+ channels to affect their activities in the plant.SYP121-KC1 interaction was found to be specific to these two protein partners and to be essential for the activity of K+ channels, channel-mediated K+ uptake at the root epidermis and for growth. Electrophysiological studies have shown changes in channel gating that can only result from an altered conformation of the channel and profound changes in the exposure of the channel voltage sensor to the membrane electric field. Intriguingly, when heterologously expressed on its own AKT1 does yield an inward-rectifying K+ current, but its gating characteristics – and those of AKT1 expressed together with KC1 – differ significantly from the K+ current in vivo unless co-expressed together with SYP121. In short, SYP121 is a missing component of the K+ channel complex and is essential for its gating in the plant. These results demonstrate a wholly unexpected role for a SNARE in eukaryotes as part of protein complex facilitating mineral nutrition and wholly unrelated to signalling or to membrane vesicle traffic",
    author = "M. Blatt and I. Johansson and M. Paneque and R. Pratelli and P. Campanoni and S. Sokolovski and A. Honsbein",
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    Blatt, M, Johansson, I, Paneque, M, Pratelli, R, Campanoni, P, Sokolovski, S & Honsbein, A 2008, 'SNAREs at the traffic junction with signalling, transport and nutrition', Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology, vol. 150, no. 3, pp. S141-S141. https://doi.org/10.1016/j.cbpa.2008.04.348

    SNAREs at the traffic junction with signalling, transport and nutrition. / Blatt, M.; Johansson, I.; Paneque, M.; Pratelli, R.; Campanoni, P.; Sokolovski, S.; Honsbein, A.

    In: Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology, Vol. 150, No. 3, 2008, p. S141-S141.

    Research output: Contribution to journalSpecial issue

    TY - JOUR

    T1 - SNAREs at the traffic junction with signalling, transport and nutrition

    AU - Blatt, M.

    AU - Johansson, I.

    AU - Paneque, M.

    AU - Pratelli, R.

    AU - Campanoni, P.

    AU - Sokolovski, S.

    AU - Honsbein, A.

    PY - 2008

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    N2 - SNARE proteins contribute to vesicle targeting and membrane fusion in all eukaryotic cells, and are essential to the mechanics of cell growth and development. Nonetheless, there is clear evidence that SNAREs play additional roles, for example in facilitating cellular signalling and synaptic transmission. I report here that SYP121, an Arabidopsis SNARE found at the plasma membrane, contributes to scaffolds that anchor ion channels within the plane of the membrane, and it is a critical structural element determining the K+ channel gating and K+ mineral nutrition. Work from my laboratory has shown that SYP121 interacts in vitro and in vivo with the regulatory (‘silent’) K+ channel subunit KC1 which assembles with different inward-rectifying K+ channels to affect their activities in the plant.SYP121-KC1 interaction was found to be specific to these two protein partners and to be essential for the activity of K+ channels, channel-mediated K+ uptake at the root epidermis and for growth. Electrophysiological studies have shown changes in channel gating that can only result from an altered conformation of the channel and profound changes in the exposure of the channel voltage sensor to the membrane electric field. Intriguingly, when heterologously expressed on its own AKT1 does yield an inward-rectifying K+ current, but its gating characteristics – and those of AKT1 expressed together with KC1 – differ significantly from the K+ current in vivo unless co-expressed together with SYP121. In short, SYP121 is a missing component of the K+ channel complex and is essential for its gating in the plant. These results demonstrate a wholly unexpected role for a SNARE in eukaryotes as part of protein complex facilitating mineral nutrition and wholly unrelated to signalling or to membrane vesicle traffic

    AB - SNARE proteins contribute to vesicle targeting and membrane fusion in all eukaryotic cells, and are essential to the mechanics of cell growth and development. Nonetheless, there is clear evidence that SNAREs play additional roles, for example in facilitating cellular signalling and synaptic transmission. I report here that SYP121, an Arabidopsis SNARE found at the plasma membrane, contributes to scaffolds that anchor ion channels within the plane of the membrane, and it is a critical structural element determining the K+ channel gating and K+ mineral nutrition. Work from my laboratory has shown that SYP121 interacts in vitro and in vivo with the regulatory (‘silent’) K+ channel subunit KC1 which assembles with different inward-rectifying K+ channels to affect their activities in the plant.SYP121-KC1 interaction was found to be specific to these two protein partners and to be essential for the activity of K+ channels, channel-mediated K+ uptake at the root epidermis and for growth. Electrophysiological studies have shown changes in channel gating that can only result from an altered conformation of the channel and profound changes in the exposure of the channel voltage sensor to the membrane electric field. Intriguingly, when heterologously expressed on its own AKT1 does yield an inward-rectifying K+ current, but its gating characteristics – and those of AKT1 expressed together with KC1 – differ significantly from the K+ current in vivo unless co-expressed together with SYP121. In short, SYP121 is a missing component of the K+ channel complex and is essential for its gating in the plant. These results demonstrate a wholly unexpected role for a SNARE in eukaryotes as part of protein complex facilitating mineral nutrition and wholly unrelated to signalling or to membrane vesicle traffic

    U2 - 10.1016/j.cbpa.2008.04.348

    DO - 10.1016/j.cbpa.2008.04.348

    M3 - Special issue

    VL - 150

    SP - S141-S141

    JO - Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology

    JF - Comparative Biochemistry and Physiology Part A: Molecular & Integrative Physiology

    SN - 1095-6433

    IS - 3

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