@article{21490,
  abstract     = {Auxin canalization is a self-organizing process that governs the flexible formation of vasculature by reinforcing the formation of auxin transport channels. A key prerequisite is the feedback between auxin signaling and directional auxin transport, mediated by PIN transporters. Despite the developmental importance of canalization, the molecular components linking auxin perception to the regulation of PIN auxin transporters remain poorly understood. Here, we identify TOW, a novel and essential component of auxin canalization that links intracellular auxin signaling with cell surface auxin perception. TOW is regulated downstream of TIR1/AFB-Aux/IAA-WRKY23 transcriptional auxin signaling. tow mutants exhibit defects in regeneration and de novo vasculature formation, along with impaired formation of polarized, PIN-expressing auxin channels. At the subcellular level, these mutants display disrupted auxin-induced PIN polarization and altered PIN endocytic trafficking dynamics. TOW localizes predominantly to the plasma membrane, where it interacts with receptor-like kinases involved in auxin canalization, including the TMK1 auxin co-receptor and the CAMEL-CANAR complex. TOW promotes PIN interaction with these kinases and stabilizes PINs at the cell surface. Together, our findings identify TOW as a molecular link between intracellular and cell surface auxin signaling mechanisms that converge on PIN trafficking and polarity, providing new insights into how auxin signaling regulates directional auxin transport for the self-organizing formation of vasculature during flexible plant development.},
  author       = {Li, Mingyue and Rydza, Nikola and Mazur, Ewa and Molnar, Gergely and Nodzyński, Tomasz and Friml, Jiří},
  issn         = {0960-9822},
  journal      = {Current Biology},
  number       = {6},
  pages        = {1468--1480.e6},
  publisher    = {Elsevier},
  title        = {{Receptor-like-kinase-interacting protein TOW stabilizes PIN transporters for auxin canalization}},
  doi          = {10.1016/j.cub.2026.02.023},
  volume       = {36},
  year         = {2026},
}

@article{21914,
  abstract     = {Cyclic adenosine monophosphate (cAMP) is a fundamental second messenger involved in diverse signaling pathways across both animals and plants. While the role of 3′,5′-cAMP has been extensively characterized, the biological significance of its structural isomer, 2′,3′-cAMP, remains largely unexplored, particularly in plants. Here, we show that 2′,3′-cAMP and 3′,5′-cAMP represent parallel signaling systems in Arabidopsis thaliana, with different enzymatic origins and largely distinct downstream effects. In vitro enzymatic assays show that plant adenylate cyclases (ACs), including AFB5 and HpAC1, produce specifically 3′,5′-cAMP from ATP, whereas the TIR domain of protein L7 also catalyzes the formation of 2′,3′-cAMP from RNA. Comprehensive multiomics analyses reveal that two isomers elicit distinct yet partially overlapping metabolic, proteomic, and transcriptional response: 2′,3′-cAMP activates broad, stress-adaptive gene expression reprogramming, while 3′,5′-cAMP fine-tunes responses related to nutrient status and cellular homeostasis. Our findings establish the existence of dual cAMP signaling systems in plants, each with specialized functions and provide insights into the complex regulatory networks governing plant physiology.},
  author       = {Li, Mingyue and Chodasiewicz, Monika and Muraleedharan, Malavika and Lopez, Israel M. and Gorka, Michal and Kerber, Olga and Alotaibi, Saqer S. and Nelson, Andrew D.L. and Lenobel, Rene and Friedecká, Jaroslava and Skirycz, Aleksandra and Friml, Jiří},
  issn         = {2375-2548},
  journal      = {Science Advances},
  number       = {19},
  publisher    = {AAAS},
  title        = {{Biogenesis and downstream effects of 3',5' and 2',3' cAMP isomers in plants}},
  doi          = {10.1126/sciadv.aea7828},
  volume       = {12},
  year         = {2026},
}