TY  - JOUR
AU  - Friml, Jiří
AU  - Gallei, Michelle
AU  - Gelová, Zuzana
AU  - Johnson, Alexander
AU  - Mazur, Ewa
AU  - Monzer, Aline
AU  - Rodriguez, Lesia
AU  - Roosjen, Mark
AU  - Verstraeten, Inge
AU  - Živanović, Branka  D.
AU  - Zou, Minxia
AU  - Fiedler, Lukáš
AU  - Giannini, Caterina
AU  - Grones, Peter
AU  - Hrtyan, Mónika
AU  - Kaufmann, Walter A.
AU  - Kuhn, Andre
AU  - Narasimhan, Madhumitha
AU  - Randuch, Marek
AU  - Rýdza, Nikola
AU  - Takahashi, Koji
AU  - Tan, Shutang
AU  - Teplova, Anastasia
AU  - Kinoshita, Toshinori
AU  - Weijers, Dolf
AU  - Rakusová, Hana
PY  - 2022
UR  - http://rimsi.imsi.bg.ac.rs/handle/123456789/1616
AB  - 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 unclear1,2,3. 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.
PB  - Nature Research
T2  - Nature
T1  - ABP1–TMK auxin perception for global phosphorylation and auxin canalization
EP  - 581
SP  - 575
VL  - 609
DO  - 10.1038/s41586-022-05187-x
ER  - 

@article{
author = "Friml, Jiří and Gallei, Michelle and Gelová, Zuzana and Johnson, Alexander and Mazur, Ewa and Monzer, Aline and Rodriguez, Lesia and Roosjen, Mark and Verstraeten, Inge and Živanović, Branka  D. and Zou, Minxia and Fiedler, Lukáš and Giannini, Caterina and Grones, Peter and Hrtyan, Mónika and Kaufmann, Walter A. and Kuhn, Andre and Narasimhan, Madhumitha and Randuch, Marek and Rýdza, Nikola and Takahashi, Koji and Tan, Shutang and Teplova, Anastasia and Kinoshita, Toshinori and Weijers, Dolf and Rakusová, Hana",
year = "2022",
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 unclear1,2,3. 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.",
publisher = "Nature Research",
journal = "Nature",
title = "ABP1–TMK auxin perception for global phosphorylation and auxin canalization",
pages = "581-575",
volume = "609",
doi = "10.1038/s41586-022-05187-x"
}

Friml, J., Gallei, M., Gelová, Z., Johnson, A., Mazur, E., Monzer, A., Rodriguez, L., Roosjen, M., Verstraeten, I., Živanović, Branka  D., Zou, M., Fiedler, L., Giannini, C., Grones, P., Hrtyan, M., Kaufmann, W. A., Kuhn, A., Narasimhan, M., Randuch, M., Rýdza, N., Takahashi, K., Tan, S., Teplova, A., Kinoshita, T., Weijers, D.,& Rakusová, H.. (2022). ABP1–TMK auxin perception for global phosphorylation and auxin canalization. in Nature
Nature Research., 609, 575-581.
https://doi.org/10.1038/s41586-022-05187-x

Friml J, Gallei M, Gelová Z, Johnson A, Mazur E, Monzer A, Rodriguez L, Roosjen M, Verstraeten I, Živanović, Branka  D., Zou M, Fiedler L, Giannini C, Grones P, Hrtyan M, Kaufmann WA, Kuhn A, Narasimhan M, Randuch M, Rýdza N, Takahashi K, Tan S, Teplova A, Kinoshita T, Weijers D, Rakusová H. ABP1–TMK auxin perception for global phosphorylation and auxin canalization. in Nature. 2022;609:575-581.
doi:10.1038/s41586-022-05187-x .

Friml, Jiří, Gallei, Michelle, Gelová, Zuzana, Johnson, Alexander, Mazur, Ewa, Monzer, Aline, Rodriguez, Lesia, Roosjen, Mark, Verstraeten, Inge, Živanović, Branka  D., Zou, Minxia, Fiedler, Lukáš, Giannini, Caterina, Grones, Peter, Hrtyan, Mónika, Kaufmann, Walter A., Kuhn, Andre, Narasimhan, Madhumitha, Randuch, Marek, Rýdza, Nikola, Takahashi, Koji, Tan, Shutang, Teplova, Anastasia, Kinoshita, Toshinori, Weijers, Dolf, Rakusová, Hana, "ABP1–TMK auxin perception for global phosphorylation and auxin canalization" in Nature, 609 (2022):575-581,
https://doi.org/10.1038/s41586-022-05187-x . .