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ABP1–TMK auxin perception for global phosphorylation and auxin canalization

Author

Listed:
  • Jiří Friml

    (Institute of Science and Technology Austria (ISTA))

  • Michelle Gallei

    (Institute of Science and Technology Austria (ISTA))

  • Zuzana Gelová

    (Institute of Science and Technology Austria (ISTA))

  • Alexander Johnson

    (Institute of Science and Technology Austria (ISTA))

  • Ewa Mazur

    (University of Silesia in Katowice)

  • Aline Monzer

    (Institute of Science and Technology Austria (ISTA))

  • Lesia Rodriguez

    (Institute of Science and Technology Austria (ISTA))

  • Mark Roosjen

    (Wageningen University)

  • Inge Verstraeten

    (Institute of Science and Technology Austria (ISTA))

  • Branka D. Živanović

    (University of Belgrade)

  • Minxia Zou

    (Institute of Science and Technology Austria (ISTA))

  • Lukáš Fiedler

    (Institute of Science and Technology Austria (ISTA))

  • Caterina Giannini

    (Institute of Science and Technology Austria (ISTA))

  • Peter Grones

    (Ghent University)

  • Mónika Hrtyan

    (Institute of Science and Technology Austria (ISTA))

  • Walter A. Kaufmann

    (Institute of Science and Technology Austria (ISTA))

  • Andre Kuhn

    (Wageningen University)

  • Madhumitha Narasimhan

    (Institute of Science and Technology Austria (ISTA))

  • Marek Randuch

    (Institute of Science and Technology Austria (ISTA))

  • Nikola Rýdza

    (Masaryk University)

  • Koji Takahashi

    (Nagoya University)

  • Shutang Tan

    (Institute of Science and Technology Austria (ISTA))

  • Anastasia Teplova

    (Institute of Science and Technology Austria (ISTA))

  • Toshinori Kinoshita

    (Nagoya University)

  • Dolf Weijers

    (Wageningen University)

  • Hana Rakusová

    (Ghent University)

Abstract

The phytohormone auxin triggers transcriptional reprogramming through a well-characterized perception machinery in the nucleus. By contrast, mechanisms that underlie fast effects of auxin, such as the regulation of ion fluxes, rapid phosphorylation of proteins or auxin feedback on its transport, remain unclear1–3. Whether auxin-binding protein 1 (ABP1) is an auxin receptor has been a source of debate for decades1,4. Here we show that a fraction of Arabidopsis thaliana ABP1 is secreted and binds auxin specifically at an acidic pH that is typical of the apoplast. ABP1 and its plasma-membrane-localized partner, transmembrane kinase 1 (TMK1), are required for the auxin-induced ultrafast global phospho-response and for downstream processes that include the activation of H+-ATPase and accelerated cytoplasmic streaming. abp1 and tmk mutants cannot establish auxin-transporting channels and show defective auxin-induced vasculature formation and regeneration. An ABP1(M2X) variant that lacks the capacity to bind auxin is unable to complement these defects in abp1 mutants. These data indicate that ABP1 is the auxin receptor for TMK1-based cell-surface signalling, which mediates the global phospho-response and auxin canalization.

Suggested Citation

  • Jiří Friml & Michelle Gallei & Zuzana Gelová & Alexander Johnson & Ewa Mazur & Aline Monzer & Lesia Rodriguez & Mark Roosjen & Inge Verstraeten & Branka D. Živanović & Minxia Zou & Lukáš Fiedler & Cat, 2022. "ABP1–TMK auxin perception for global phosphorylation and auxin canalization," Nature, Nature, vol. 609(7927), pages 575-581, September.
    • Handle: RePEc:nat:nature:v:609:y:2022:i:7927:d:10.1038_s41586-022-05187-x
    DOI: 10.1038/s41586-022-05187-x
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    Cited by:

    1. Fuxi Rong & Yusong Lv & Pingchuan Deng & Xia Wu & Yaqi Zhang & Erkui Yue & Yuxin Shen & Sajid Muhammad & Fangrui Ni & Hongwu Bian & Xiangjin Wei & Weijun Zhou & Peisong Hu & Liang Wu, 2024. "Switching action modes of miR408-5p mediates auxin signaling in rice," Nature Communications, Nature, vol. 15(1), pages 1-17, December.

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