@article{14313,
  abstract     = {To respond to auxin, the chief orchestrator of their multicellularity, plants evolved multiple receptor systems and signal transduction cascades. Despite decades of research, however, we are still lacking a satisfactory synthesis of various auxin signaling mechanisms. The chief discrepancy and historical controversy of the field is that of rapid and slow auxin effects on plant physiology and development. How is it possible that ions begin to trickle across the plasma membrane as soon as auxin enters the cell, even though the best-characterized transcriptional auxin pathway can take effect only after tens of minutes? Recently, unexpected progress has been made in understanding this and other unknowns of auxin signaling. We provide a perspective on these exciting developments and concepts whose general applicability might have ramifications beyond auxin signaling.},
  author       = {Fiedler, Lukas and Friml, Jiří},
  issn         = {1369-5266},
  journal      = {Current Opinion in Plant Biology},
  number       = {10},
  publisher    = {Elsevier},
  title        = {{Rapid auxin signaling: Unknowns old and new}},
  doi          = {10.1016/j.pbi.2023.102443},
  volume       = {75},
  year         = {2023},
}

@article{14447,
  abstract     = {Auxin belongs among major phytohormones and governs multiple aspects of plant growth and development. The establishment of auxin concentration gradients, determines, among other processes, plant organ positioning and growth responses to environmental stimuli.
Herein we report the synthesis of new NBD- or DNS-labelled IAA derivatives and the elucidation of their biological activity, fluorescence properties and subcellular accumulation patterns in planta. These novel compounds did not show auxin-like activity, but instead antagonized physiological auxin effects. The DNS-labelled derivatives FL5 and FL6 showed strong anti-auxin activity in roots and hypocotyls, which also occurred at the level of gene transcription as confirmed by quantitative PCR analysis. The auxin antagonism of our derivatives was further demonstrated in vitro using an SPR-based binding assay. The NBD-labelled compound FL4 with the best fluorescence properties proved to be unsuitable to study auxin accumulation patterns in planta. On the other hand, the strongest anti-auxin activity possessing compounds FL5 and FL6 could be useful to study binding mechanisms to auxin receptors and for manipulations of auxin-regulated processes.},
  author       = {Bieleszová, Kristýna and Hladík, Pavel and Kubala, Martin and Napier, Richard and Brunoni, Federica and Gelová, Zuzana and Fiedler, Lukas and Kulich, Ivan and Strnad, Miroslav and Doležal, Karel and Novák, Ondřej and Friml, Jiří and Žukauskaitė, Asta},
  issn         = {1573-5087},
  journal      = {Plant Growth Regulation},
  publisher    = {Springer Nature},
  title        = {{New fluorescent auxin derivatives: anti-auxin activity and accumulation patterns in Arabidopsis thaliana}},
  doi          = {10.1007/s10725-023-01083-0},
  year         = {2023},
}

@article{12291,
  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.},
  author       = {Friml, Jiří and Gallei, Michelle C and Gelová, Zuzana and Johnson, Alexander J and Mazur, Ewa and Monzer, Aline and Rodriguez Solovey, Lesia and Roosjen, Mark and Verstraeten, Inge and Živanović, Branka D. and Zou, Minxia and Fiedler, Lukas and Giannini, Caterina and Grones, Peter and Hrtyan, Mónika and Kaufmann, Walter and Kuhn, Andre and Narasimhan, Madhumitha and Randuch, Marek and Rýdza, Nikola and Takahashi, Koji and Tan, Shutang and Teplova, Anastasiia and Kinoshita, Toshinori and Weijers, Dolf and Rakusová, Hana},
  issn         = {1476-4687},
  journal      = {Nature},
  number       = {7927},
  pages        = {575--581},
  publisher    = {Springer Nature},
  title        = {{ABP1–TMK auxin perception for global phosphorylation and auxin canalization}},
  doi          = {10.1038/s41586-022-05187-x},
  volume       = {609},
  year         = {2022},
}