Distinct functions of TIR1 and AFB1 receptors in auxin signalling

Auxin is the major plant hormone regulating growth and development ([Friml, 2022][1]). Forward genetic approaches in the model plant Arabidopsis thaliana have identified major components of auxin signalling and established the canonical mechanism mediating transcriptional and thus developmental reprogramming. In this textbook view, TRANSPORT INHIBITOR RESPONSE 1 (TIR1)/AUXIN-SIGNALING F-BOX (AFBs) are auxin receptors, which act as F-box subunits determining the substrate specificity of the Skp1-Cullin1-F box protein (SCF) type E3 ubiquitin ligase complex. Auxin acts as a “molecular glue” increasing the affinity between TIR1/AFBs and the Aux/IAA repressors. Subsequently, Aux/IAAs are ubiquitinated and degraded, thus releasing auxin transcription factors from their repression making them free to mediate transcription of auxin response genes ([Yu et al ., 2022][2]). Nonetheless, accumulating evidence suggests existence of rapid, non-transcriptional responses downstream of TIR1/AFBs such as auxin-induced cytosolic calcium (Ca2+) transients, plasma membrane depolarization and apoplast alkalinisation, all converging on the process of root growth inhibition and root gravitropism ([Li et al ., 2022][3]). Particularly, these rapid responses are mostly contributed by predominantly cytosolic AFB1, while the long-term growth responses are mediated by mainly nuclear TIR1 and AFB2-AFB5 ([Li et al ., 2021][4]; [Prigge et al ., 2020][5]; [Serre et al ., 2021][6]). How AFB1 conducts auxin-triggered rapid responses and how it is different from TIR1 and AFB2-AFB5 remains elusive. Here, we compare the roles of TIR1 and AFB1 in transcriptional and rapid responses by modulating their subcellular localization in Arabidopsis and by testing their ability to mediate transcriptional responses when part of the minimal auxin circuit reconstituted in yeast. Short summary Auxin receptors TIR1 and AFB1 have distinct functions in mediating transcriptional and non-transcriptional responses, respectively. Manipulation of their subcellular localizations revealed that these functional differences cannot be attributed to nuclear versus cytosolic enrichment of TIR1 and AFB1 but to different, specific properties of these proteins, not least to their ability to associate with ubiquitin ligase components. ### Competing Interest Statement The authors have declared no competing interest. [1]: #ref-1 [2]: #ref-9 [3]: #ref-2 [4]: #ref-3 [5]: #ref-5 [6]: #ref-7