ABP1–TMK auxin perception for global phosphorylation and auxin canalization
Samo za registrovane korisnike
2022
Autori
Friml, JiříGallei, 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
Članak u časopisu (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
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 th...e 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.
Ključne reči:
auxin / ATPase activity / plasma-membrane potential / phosphorylation / root growthIzvor:
Nature, 2022, 609, 575-581Izdavač:
- Nature Research
Finansiranje / projekti:
- The European Research Council (ERC) under the European Union’s Horizon 2020 research and innovation program (grant agreement no. 742985 to J.F. and 833867 to D.W.)
- The Austrian Science Fund (FWF; P29988 to J.F.)
- The Netherlands Organization for Scientific Research NWO; VICI grant 865.14.001 to D.W.
- The Netherlands Organization for Scientific Research NWO; VENI grant VI.Veni.212.003 to A.K.
- Ministarstvo nauke, tehnološkog razvoja i inovacija Republike Srbije, institucionalno finansiranje - 200053 (Univerzitet u Beogradu, Institut za multidisciplinarna istraživanja) (RS-MESTD-inst-2020-200053)
- The MEXT/JSPS KAKENHI to K.T. (20K06685) and T.K. (20H05687 and 20H05910)
Institucija/grupa
Institut za multidisciplinarna istraživanjaTY - 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 . .