ABP1–TMK auxin perception for global phosphorylation and auxin canalization

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, rem...

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Vydáno v:	Nature (London) Ročník 609; číslo 7927; s. 575 - 581
Hlavní autoři:	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
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	London Nature Publishing Group UK 15.09.2022 Nature Publishing Group
Témata:	14/19 14/28 38/70 631/208/2491 631/449/2675 82/103 96/35 96/44 Acids Apoplast Arabidopsis - genetics Arabidopsis - metabolism Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Auxins Cell surface Cytoplasmic Streaming H+-transporting ATPase Humanities and Social Sciences Hydrogen-Ion Concentration Indoleacetic Acids - metabolism Ion flux Ion fluxes Kinases Localization multidisciplinary Mutants Mutation Perception Phosphorylation Plant Growth Regulators - metabolism Plant hormones Plasma Protein Serine-Threonine Kinases - genetics Protein Serine-Threonine Kinases - metabolism Proteins Proton-Translocating ATPases - metabolism Receptors Science Science (multidisciplinary)
ISSN:	0028-0836, 1476-4687, 1476-4687
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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 unclear 1 – 3 . Whether auxin-binding protein 1 (ABP1) is an auxin receptor has been a source of debate for decades 1 , 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. Auxin-binding protein 1 (ABP1) is an auxin receptor that, in complex with transmembrane kinase 1 (TMK1), has a key role in the auxin-induced global phosphorylation of proteins and downstream responses such as vascular regeneration.
AbstractList	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.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. 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 unclear . Whether auxin-binding protein 1 (ABP1) is an auxin receptor has been a source of debate for decades . 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. 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 unclear 1 – 3 . Whether auxin-binding protein 1 (ABP1) is an auxin receptor has been a source of debate for decades 1 , 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. Auxin-binding protein 1 (ABP1) is an auxin receptor that, in complex with transmembrane kinase 1 (TMK1), has a key role in the auxin-induced global phosphorylation of proteins and downstream responses such as vascular regeneration. 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. abpl 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 abpl 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.
Author	Monzer, Aline Mazur, Ewa Živanović, Branka D. Kaufmann, Walter A. Johnson, Alexander Gallei, Michelle Teplova, Anastasia Verstraeten, Inge Giannini, Caterina Rodriguez, Lesia Tan, Shutang Gelová, Zuzana Kinoshita, Toshinori Narasimhan, Madhumitha Hrtyan, Mónika Friml, Jiří Weijers, Dolf Roosjen, Mark Randuch, Marek Kuhn, Andre Zou, Minxia Rýdza, Nikola Fiedler, Lukáš Grones, Peter Takahashi, Koji Rakusová, Hana
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Copyright	The Author(s), under exclusive licence to Springer Nature Limited 2022. Springer Nature or its licensor holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law. 2022. The Author(s), under exclusive licence to Springer Nature Limited. Copyright Nature Publishing Group Sep 15, 2022
Copyright_xml	– notice: The Author(s), under exclusive licence to Springer Nature Limited 2022. Springer Nature or its licensor holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law. – notice: 2022. The Author(s), under exclusive licence to Springer Nature Limited. – notice: Copyright Nature Publishing Group Sep 15, 2022
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Snippet	The phytohormone auxin triggers transcriptional reprogramming through a well-characterized perception machinery in the nucleus. By contrast, mechanisms that...
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SubjectTerms	14/19 14/28 38/70 631/208/2491 631/449/2675 82/103 96/35 96/44 Acids Apoplast Arabidopsis - genetics Arabidopsis - metabolism Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Auxins Cell surface Cytoplasmic Streaming H+-transporting ATPase Humanities and Social Sciences Hydrogen-Ion Concentration Indoleacetic Acids - metabolism Ion flux Ion fluxes Kinases Localization multidisciplinary Mutants Mutation Perception Phosphorylation Plant Growth Regulators - metabolism Plant hormones Plasma Protein Serine-Threonine Kinases - genetics Protein Serine-Threonine Kinases - metabolism Proteins Proton-Translocating ATPases - metabolism Receptors Science Science (multidisciplinary)
Title	ABP1–TMK auxin perception for global phosphorylation and auxin canalization
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