@article{20321,
  abstract     = {Microsecond-to-millisecond motions are instrumental for many biomolecular functions, including enzymatic activity and ligand binding. Bloch-McConnell Relaxation Dispersion (BMRD) Nuclear Magnetic Resonance (NMR) spectroscopy is a key technique for studying these dynamic processes. While BMRD experiments are routinely used to probe protein motions in solution, the experiment is more demanding in the solid state, where dipolar couplings complicate the spin dynamics. It is believed that high deuteration levels are required and sufficient to obtain accurate and quantitative data. Here we show that even under fast magic-angle spinning and high levels of deuteration artifactual “bumps” in 15N R1ρ BMRD profiles are common. The origin of these artifacts is identified as a second-order three-spin Mixed Rotational and Rotary Resonance (MIRROR) recoupling condition. These artifacts are found to be a significant confounding factor for the accurate quantification of microsecond protein dynamics using BMRD in the solid state. We show that the application of low-power continuous wave (CW) decoupling simultaneously with the 15N spin-lock leads to the suppression of these conditions and enables quantitative measurements of microsecond exchange in the solid state. Remarkably, the application of decoupling allows the measurement of accurate BMRD even in fully protonated proteins at 100 kHz MAS, thus extending the scope of μs dynamics measurements in MAS NMR.},
  author       = {Tatman, Benjamin and Sridharan, Vidhyalakshmi and Uttarkabat, Motilal and Jaroniec, Christopher P. and Ernst, Matthias and Rovo, Petra and Schanda, Paul},
  issn         = {1520-5126},
  journal      = {Journal of the American Chemical Society},
  number       = {32},
  pages        = {29315--29326},
  publisher    = {American Chemical Society},
  title        = {{Bumps on the road: The way to clean relaxation dispersion magic-angle spinning NMR}},
  doi          = {10.1021/jacs.5c09057},
  volume       = {147},
  year         = {2025},
}

@article{20331,
  abstract     = {Here, we present a foundational investigation of charge transport through three BODIPY-based molecules using the scanning tunneling microscope–break junction (STM-BJ) technique. We demonstrate that molecular conductance through the BODIPY core can be measured by introducing aurophilic linkers at the 2,6-positions. By varying these linkers, we systematically modulate the frontier molecular orbital energies and fine-tune transport behavior. Our experimental results are supported by DFT-based calculations, which feature a new computationally efficient correction to standard PBE-level transmission predictions. Together, these findings establish the viability of BODIPY-based systems for molecular junction applications and lay the groundwork for future studies of their single-molecule optoelectronic properties.},
  author       = {York, Emma and Stone, Ilana and Shi, Wanzhuo and Roy, Xavier and Venkataraman, Latha},
  issn         = {1530-6992},
  journal      = {Nano Letters},
  number       = {36},
  pages        = {13697--13702},
  publisher    = {American Chemical Society},
  title        = {{Tuning conductance in BODIPY-based single-molecule junctions}},
  doi          = {10.1021/acs.nanolett.5c03764},
  volume       = {25},
  year         = {2025},
}

@article{20481,
  abstract     = {Kelvin probe force microscopy (KPFM) is widely used in stationary and dynamic studies of contact electrification. An obvious question that connects these two has been overlooked: when are charge dynamics too fast for stationary studies to be meaningful? Using a rapid transfer system to quickly perform KPFM after contact, we find the dynamics are too fast in all but the best insulators. Our data further suggest that dynamics are caused by bulk as opposed to surface conductivity, and that charge-transfer heterogeneity is less prevalent than previously suggested.},
  author       = {Pertl, Felix and Lenton, Isaac C and Cramer, Tobias and Waitukaitis, Scott R},
  issn         = {1079-7114},
  journal      = {Physical Review Letters},
  number       = {14},
  publisher    = {American Physical Society},
  title        = {{No time for surface charge: How bulk conductivity hides charge patterns from Kelvin probe force microscopy in contact-electrified surfaces}},
  doi          = {10.1103/lcsm-xxty},
  volume       = {135},
  year         = {2025},
}

@article{20538,
  abstract     = {In this study, we describe an integrated approach for methyl group assignment comprising precursor-based selective methyl group labeling, a novel pulse sequence for methyl to backbone coherence transfer and chemical shift predictions using UCBShift 2.0. The utility of this novel α-ketoacid isotopologue is shown by the adaptation of an HMBC-HMQC pulse sequence that simultaneously connects geminal methyl groups of leucine and valine residues to each other and to the protein backbone. By additional 13C,2H-labeling of residues other than valine and leucine residues of the protein, important chemical shift information about neighboring residues (following valine and leucine residues) can be achieved. Thus, different valine and leucine residues in a protein can be characterized as a specific chemical shift vector. Frequency matching with predicted chemical shifts via UCBShift 2.0 using experimental data taken from a subset of the BMRB database revealed a correct assignment performance of about 90%. With applications to proteins of 60.2 kDa and 134 kDa (4 × 33.5 kDa) in size, we demonstrate that the approach provides valuable information even for very large proteins.},
  author       = {Knödlstorfer, Sonja and Toscano, Giorgia and Ptaszek, Aleksandra L. and Kontaxis, Georg and Napoli, Federico and Schneider, Jakob and Maier, Katharina and Kapitonova, Anna and Lichtenecker, Roman J. and Schanda, Paul and Konrat, Robert},
  issn         = {1089-8638},
  journal      = {Journal of Molecular Biology},
  number       = {23},
  publisher    = {Elsevier},
  title        = {{A novel HMBC-CC-HMQC NMR strategy for methyl assignment using triple-13C-labeled α-ketoisovalerate integrated with UCBShift 2.0}},
  doi          = {10.1016/j.jmb.2025.169465},
  volume       = {437},
  year         = {2025},
}

@misc{20641,
  abstract     = {Protein conformational energy landscapes are shaped not only by intramolecular interactions but also by their environment. In protein crystals and protein-protein complexes, intermolecular contacts alter this energy landscape, but the exact nature of this alteration is difficult to decipher. Understanding how the crystal lattice affects protein dynamics is crucial for crystallography-based studies of motion, yet its influence on collective motions remains unclear. Aromatic ring flips in the hydrophobic core represent sensitive probes of such dynamics. Here, we compare the kinetics of aromatic ring flips in the protein GB1 in crystals, in complex with its binding partner IgG, and in solution, combining advanced isotope labeling with quantitative NMR methods. We show that rings in the core flip nearly a thousand times less frequently in crystals than in solution. Enhanced-sampling molecular dynamics simulations, based on a new crystal structure, reproduce these elevated barriers and reveal how the crystal restrains motions. },
  author       = {Becker, Lea Marie and Schanda, Paul},
  publisher    = {Institute of Science and Technology Austria},
  title        = {{Data for "Aromatic Ring Flips Reveal Reshaping of Protein Dynamics in Crystals and Complexes"}},
  doi          = {10.15479/AT-ISTA-20641},
  year         = {2025},
}

@article{20656,
  abstract     = {Phytohormone auxin and its directional transport mediate much of the remarkably plastic development of higher plants. Positive feedback between auxin signaling and transport is a prerequisite for (1) self-organizing processes, including vascular tissue formation, and (2) directional growth responses such as gravitropism. Here, we identify a mechanism by which auxin signaling directly targets PIN auxin transporters. Via the cell-surface AUXIN-BINDING PROTEIN1 (ABP1)-TRANSMEMBRANE KINASE 1 (TMK1) receptor module, auxin rapidly induces phosphorylation and thus stabilization of PIN2. Following gravistimulation, initial auxin asymmetry activates autophosphorylation of the TMK1 kinase. This induces TMK1 interaction with and phosphorylation of PIN2, stabilizing PIN2 at the lower root side, thus reinforcing asymmetric auxin flow for root bending. Upstream of TMK1 in this regulation, ABP1 acts redundantly with the root-expressed ABP1-LIKE 3 (ABL3) auxin receptor. Such positive feedback between cell-surface auxin signaling and PIN-mediated polar auxin transport is fundamental for robust root gravitropism and presumably for other self-organizing developmental phenomena.},
  author       = {Rodriguez Solovey, Lesia and Fiedler, Lukas and Zou, Minxia and Giannini, Caterina and Monzer, Aline and Vladimirtsev, Dmitrii and Randuch, Marek and Yu, Yongfan and Gelová, Zuzana and Verstraeten, Inge and Hajny, Jakub and Chen, Meng and Tan, Shutang and Hörmayer, Lukas and Li, Lanxin and Marques-Bueno, Maria Mar and Quddoos, Zainab and Molnar, Gergely and Kulich, Ivan and Jaillais, Yvon and Friml, Jiří},
  issn         = {0092-8674},
  journal      = {Cell},
  number       = {22},
  pages        = {6138--6150.e17},
  publisher    = {Elsevier},
  title        = {{ABP1/ABL3-TMK1 cell-surface auxin signaling targets PIN2-mediated auxin fluxes for root gravitropism}},
  doi          = {10.1016/j.cell.2025.08.026},
  volume       = {188},
  year         = {2025},
}

@unpublished{20804,
  abstract     = {RNA polymerase II (Pol II) must be assembled in the cytoplasm before it enters the nucleus, where it transcribes protein-coding genes. Although transcription by Pol II is intensively studied, how this central multi-subunit enzyme is made and the role of dedicated factors remains unclear. Here, we report the integrative structural analysis of a native human Pol II from the cytoplasm captured near the end of biogenesis. The complex contained Gdown1 and three biogenesis factors – RPAP2 and the critical small GTPases GPN1 and GPN3. Cryo-EM analysis of the complex revealed how Gdown1 and RPAP2 associate with Pol II and prevent the premature association of transcription factors. Further biochemical and cryo-EM analysis revealed how RPAP2 recruits GPN1–GPN3 to the complex, and how the assembly of the RPAP2–GPN1–GPN3 complex is controlled by GTP hydrolysis. The combined results uncover a network of interactions that chaperone cytoplasmic Pol II to prevent aberrant interactions, reveal a GTP-controlled switch during the final stages of Pol II biogenesis, and suggest a general mechanism for the action of GPN-loop GTPase family of enzymes.},
  author       = {Hlavata, Annamaria and Neuditschko, Benjamin and Schellhaas, Ulla and Plaschka, Clemens and Herzog, Franz and Bernecky, Carrie A},
  publisher    = {bioRxiv},
  title        = {{Structure of cytoplasmic RNA polymerase II}},
  doi          = {10.64898/2025.12.10.692585},
  year         = {2025},
}

@article{18778,
  abstract     = {Transcription by RNA polymerase II (Pol II) can be repressed by noncoding RNA, including the human RNA Alu. However, the mechanism by which endogenous RNAs repress transcription remains unclear. Here we present cryogenic-electron microscopy structures of Pol II bound to Alu RNA, which reveal that Alu RNA mimics how DNA and RNA bind to Pol II during transcription elongation. Further, we show how distinct domains of the general transcription factor TFIIF control repressive activity. Together, we reveal how a noncoding RNA can regulate mammalian gene expression.},
  author       = {Tluckova, Katarina and Kaczmarek, Beata M and Testa Salmazo, Anita P and Bernecky, Carrie A},
  issn         = {1545-9985},
  journal      = {Nature Structural & Molecular Biology},
  pages        = {607--612},
  publisher    = {Springer Nature},
  title        = {{Mechanism of mammalian transcriptional repression by noncoding RNA}},
  doi          = {10.1038/s41594-024-01448-7},
  volume       = {32},
  year         = {2025},
}

@article{19003,
  abstract     = {Super-resolution methods provide far better spatial resolution than the optical diffraction limit of about half the wavelength of light (∼200-300 nm). Nevertheless, they have yet to attain widespread use in plants, largely due to plants’ challenging optical properties. Expansion microscopy improves effective resolution by isotropically increasing the physical distances between sample structures while preserving relative spatial arrangements and clearing the sample. However, its application to plants has been hindered by the rigid, mechanically cohesive structure of plant tissues. Here, we report on whole-mount expansion microscopy of thale cress (Arabidopsis thaliana) root tissues (PlantEx), achieving a four-fold resolution increase over conventional microscopy. Our results highlight the microtubule cytoskeleton organization and interaction between molecularly defined cellular constituents. Combining PlantEx with stimulated emission depletion (STED) microscopy, we increase nanoscale resolution and visualize the complex organization of subcellular organelles from intact tissues by example of the densely packed COPI-coated vesicles associated with the Golgi apparatus and put these into a cellular structural context. Our results show that expansion microscopy can be applied to increase effective imaging resolution in Arabidopsis root specimens. },
  author       = {Gallei, Michelle C and Truckenbrodt, Sven M and Kreuzinger, Caroline and Inumella, Syamala and Vistunou, Vitali and Sommer, Christoph M and Tavakoli, Mojtaba and Agudelo Duenas, Nathalie and Vorlaufer, Jakob and Jahr, Wiebke and Randuch, Marek and Johnson, Alexander J and Benková, Eva and Friml, Jiří and Danzl, Johann G},
  issn         = {1532-298X},
  journal      = {The Plant Cell},
  number       = {4},
  publisher    = {Oxford University Press},
  title        = {{Super-resolution expansion microscopy in plant roots}},
  doi          = {10.1093/plcell/koaf006},
  volume       = {37},
  year         = {2025},
}

@article{19076,
  abstract     = {For accurate perception and motor control, an animal must distinguish between sensory experiences elicited by external stimuli and those elicited by its own actions. The diversity of behaviors and their complex influences on the senses make this distinction challenging. Here, we uncover an action–cue hub that coordinates motor commands with visual processing in the brain’s first visual relay. We show that the ventral lateral geniculate nucleus (vLGN) acts as a corollary discharge center, integrating visual translational optic flow signals with motor copies from saccades, locomotion and pupil dynamics. The vLGN relays these signals to correct action-specific visual distortions and to refine perception, as shown for the superior colliculus and in a depth-estimation task. Simultaneously, brain-wide vLGN projections drive corrective actions necessary for accurate visuomotor control. Our results reveal an extended corollary discharge architecture that refines early visual transformations and coordinates actions via a distributed hub-and-spoke network to enable visual perception during action.},
  author       = {Vega Zuniga, Tomas A and Sumser, Anton L and Symonova, Olga and Koppensteiner, Peter and Schmidt, Florian and Jösch, Maximilian A},
  issn         = {1546-1726},
  journal      = {Nature Neuroscience},
  publisher    = {Springer Nature},
  title        = {{A thalamic hub-and-spoke network enables visual perception during action by coordinating visuomotor dynamics}},
  doi          = {10.1038/s41593-025-01874-w},
  volume       = {28},
  year         = {2025},
}

@article{19404,
  abstract     = {Cell migration is a fundamental process during embryonic development. Most studies in vivo have focused on the migration of cells using the extracellular matrix (ECM) as their substrate for migration. In contrast, much less is known about how cells migrate on other cells, as found in early embryos when the ECM has not yet formed. Here, we show that lateral mesendoderm (LME) cells in the early zebrafish gastrula use the ectoderm as their substrate for migration. We show that the lateral ectoderm is permissive for the animal-pole-directed migration of LME cells, while the ectoderm at the animal pole halts it. These differences in permissiveness depend on the lateral ectoderm being more cohesive than the animal ectoderm, a property controlled by bone morphogenetic protein (BMP) signaling within the ectoderm. Collectively, these findings identify ectoderm tissue cohesion as one critical factor in regulating LME migration during zebrafish gastrulation.},
  author       = {Tavano, Ste and Brückner, David and Tasciyan, Saren and Tong, Xin and Kardos, Roland and Schauer, Alexandra and Hauschild, Robert and Heisenberg, Carl-Philipp J},
  issn         = {2211-1247},
  journal      = {Cell Reports},
  number       = {3},
  publisher    = {Elsevier},
  title        = {{BMP-dependent patterning of ectoderm tissue material properties modulates lateral mesendoderm cell migration during early zebrafish gastrulation}},
  doi          = {10.1016/j.celrep.2025.115387},
  volume       = {44},
  year         = {2025},
}

@article{19599,
  abstract     = {Advances in nickel catalysis have significantly broadened the synthetic chemists’ toolbox, particularly through methodologies leveraging paramagnetic nickel species via photoredox catalysis or electrochemistry. Key to these reactions is the oxidation state modulation of nickel via single-electron transfer events. Recent mechanistic studies indicate that C(sp2)–heteroatom bond formations proceed through NiI/NiIII cycles. Related C(sp2)–C(sp3) cross-couplings operate via the photocatalytic generation of C-centered radicals and a catalytic cycle that involves Ni0, NiI, and NiIII species. Here, we show that light-mediated nickel-catalyzed C(sp2)–C(sp3) bond formations can be carried out without using exogenous photoredox catalysts but with a photoactive ligand. In a pursuit of expanding the scope of C(sp2)–heteroatom couplings using donor–acceptor ligands, we identified a photoactive nickel complex capable of catalyzing cross-couplings between aryl halides and benzyltrifluoroborate salts. Mechanistic investigations provide evidence that transmetalation between a photochemically generated NiI species and the organoboron compound is the key catalytic step in a NiI/NiIII catalytic cycle under these conditions.},
  author       = {Anghileri, Lucia and Baunis, Haralds and Bena, Aleksander and Giannoudis, Christos and Burke, John H. and Reischauer, Susanne and Merschjann, Christoph and Wallick, Rachel F. and Al Said, Tarek and Adams, Callum E and Simionato, Gianluca and Kovalenko, Sergey and Dell’Amico, Luca and Van Der Veen, Renske M. and Pieber, Bartholomäus},
  issn         = {1520-5126},
  journal      = {Journal of the American Chemical Society},
  number       = {16},
  pages        = {13169–13179},
  publisher    = {American Chemical Society},
  title        = {{Evidence for a unifying NiI/NiIII mechanism in light-mediated cross-coupling catalysis}},
  doi          = {10.1021/jacs.4c16050},
  volume       = {147},
  year         = {2025},
}

@misc{19696,
  author       = {Tatman, Benjamin},
  publisher    = {Institute of Science and Technology Austria},
  title        = {{Dataset for "Bumps on the Road: The Way to Clean Relaxation Dispersion in the Solid State"}},
  doi          = {10.15479/AT-ISTA-19696},
  year         = {2025},
}

@article{20847,
  abstract     = {We report on an experimental active matter system with motion restricted to four cardinal directions. Our particles are magnetite-doped colloidal spheres driven by the Quincke electrorotational instability. The absence of a magnetic field (|𝑩|=0) leads to circular trajectories interspersed with short spontaneous runs. Intermediate fields (|𝑩|≲20mT) linearize the motion along the axis perpendicular to 𝑩. At high magnetic fields, we observe the surprising emergence of a second, distinct linearization along the axis parallel to 𝑩. With numerical simulations, we show that this behavior can be explained by anisotropic magnetic susceptibility.},
  author       = {Fitzgerald, Eavan and Clavaud, Cécile and Das, Debasish and Lenton, Isaac C and Waitukaitis, Scott R},
  issn         = {2470-0053},
  journal      = {Physical Review E},
  number       = {6},
  publisher    = {American Physical Society},
  title        = {{Rolling at right angles: Magnetic anisotropy enables dual-anisotropic active matter}},
  doi          = {10.1103/1ss8-31rb},
  volume       = {112},
  year         = {2025},
}

@article{17884,
  abstract     = {Human T cell leukemia virus type 1 (HTLV-1) immature particles differ in morphology from other retroviruses, suggesting a distinct way of assembly. Here we report the results of cryo-electron tomography studies of HTLV-1 virus-like particles assembled in vitro, as well as derived from cells. This work shows that HTLV-1 uses a distinct mechanism of Gag–Gag interactions to form the immature viral lattice. Analysis of high-resolution structural information from immature capsid (CA) tubular arrays reveals that the primary stabilizing component in HTLV-1 is the N-terminal domain of CA. Mutagenesis analysis supports this observation. This distinguishes HTLV-1 from other retroviruses, in which the stabilization is provided primarily by the C-terminal domain of CA. These results provide structural details of the quaternary arrangement of Gag for an immature deltaretrovirus and this helps explain why HTLV-1 particles are morphologically distinct.},
  author       = {Obr, Martin and Percipalle, Mathias and Chernikova, Darya and Yang, Huixin and Thader, Andreas and Pinke, Gergely and Porley, Dario J and Mansky, Louis M. and Dick, Robert A. and Schur, Florian KM},
  issn         = {1545-9985},
  journal      = {Nature Structural & Molecular Biology},
  pages        = {268--276},
  publisher    = {Springer Nature},
  title        = {{Distinct stabilization of the human T cell leukemia virus type 1 immature Gag lattice}},
  doi          = {10.1038/s41594-024-01390-8},
  volume       = {32},
  year         = {2025},
}

@article{20326,
  abstract     = {Ag2Se is a promising n-type thermoelectric material, but its performance is limited by excessive carrier concentration, compositional inhomogeneity, and phase instability, challenges rooted in a narrow homogeneity range and uncontrolled Ag+ diffusion in the superionic phase. Here, we address these issues by exploiting liquid–solid interface reactions using CdSe complexes that remove surface excess Ag to yield stoichiometric Ag2Se and generate CdSe nanodomains that inhibit Ag+ diffusion and constrain grain growth. The resulting Ag2Se-CdSe nanocomposites exhibit a reproducible, stable figure of merit (zT) of 1.04 between 300 and 390 K. Beyond demonstrating high performance, we elucidate the interfacial chemical reactions that give rise to the observed microstructure and transport properties, providing a foundation for rationally engineering interfacial chemistry to tailor transport properties across diverse thermoelectric material systems.},
  author       = {Liu, Yu and Kleinhanns, Tobias and Horta, Sharona and Dutkiewicz, Ewelina and Lu, Shaoqing and Spadaro, Maria Chiara and Genç, Aziz and Chen, Lei and Lim, Khak Ho and Hong, Min and Arbiol, Jordi and Ibáñez, Maria},
  issn         = {1520-5126},
  journal      = {Journal of the American Chemical Society},
  number       = {35},
  pages        = {32199--32208},
  publisher    = {American Chemical Society},
  title        = {{Liquid-solid interface reactions drive enhanced thermoelectric performance in Ag2Se}},
  doi          = {10.1021/jacs.5c11435},
  volume       = {147},
  year         = {2025},
}

@article{19795,
  abstract     = {Super-resolution microscopy often entails long acquisition times of minutes to hours. Since drifts during the acquisition adversely affect data quality, active sample stabilization is commonly used for some of these techniques to reach their full potential. Although drifts in the lateral plane can often be corrected after acquisition, this is not always possible or may come with drawbacks. Therefore, it is appealing to stabilize sample position in three dimensions (3D) during acquisition. Various schemes for active sample stabilization have been demonstrated previously, with some reaching sub-nanometer stability in 3D. Here, we present a scheme for active drift correction that delivers the nanometer-scale 3D stability demanded by state-of-the-art super-resolution techniques and is straightforward to implement compared to previous schemes capable of reaching this level of stabilization precision. Using a refined algorithm that can handle various types of reference structure, without sparse signal peaks being mandatory, we stabilized sample position to ∼1 nm in 3D using objective lenses both with high and low numerical aperture. Our implementation requires only the addition of a simple widefield imaging path and we provide an open-source control software with graphical user interface to facilitate easy adoption of the module. Finally, we demonstrate how this has the potential to enhance data collection for diffraction-limited and super-resolution imaging techniques using single-molecule localization microscopy and cryo-confocal imaging as showcases.},
  author       = {Vorlaufer, Jakob and Semenov, Nikolai and Kreuzinger, Caroline and Javoor, Manjunath and Zens, Bettina and Agudelo Duenas, Nathalie and Tavakoli, Mojtaba and Suplata, Marek and Jahr, Wiebke and Lyudchik, Julia and Wartak, Andreas and Schur, Florian Km and Danzl, Johann G},
  issn         = {2667-0747},
  journal      = {Biophysical Reports},
  number       = {2},
  publisher    = {Elsevier},
  title        = {{Image-based 3D active sample stabilization on the nanometer scale for optical microscopy}},
  doi          = {10.1016/j.bpr.2025.100211},
  volume       = {5},
  year         = {2025},
}

@phdthesis{19722,
  author       = {Inumella, Syamala},
  isbn         = {978-3-99078-059-6},
  issn         = {2663-337X},
  pages        = {113},
  publisher    = {Institute of Science and Technology Austria},
  title        = {{Molecular mechanisms of microtubule reorganization in elongating root epidermal cells}},
  doi          = {10.15479/AT-ISTA-19722},
  year         = {2025},
}

@phdthesis{19395,
  abstract     = {Plant growth and development rely significantly on phytohormones, with auxin serving as a master regulator, orchestrating processes from embryogenesis to organogenesis, vascular patterning, and environmental adaptation. Since its conceptual proposition by Charles Darwin in 1880 as an endogenous chemical signal influencing phototropism in grass, auxin has captivated scientists seeking to understand how such a small molecule exerts a profound influence on plant development.
One particularly fascinating aspect of auxin function is its ability to self-organize its transport. Through a feedback mechanism between auxin perception and directional transport—primarily mediated by PIN auxin transporters—auxin establishes narrow transport channels. This phenomenon, known as auxin canalization, is fundamental to vascular formation, regeneration, and other key developmental processes. Despite advances in our understanding, driven by experimental studies and computational models, auxin canalization remains an enigma, with many unanswered questions.
Like other hormones, auxin functions through intricate signaling pathways. It operates through at least two distinct signaling mechanisms: the well-characterized canonical pathway and the less understood non-canonical pathway. While significant progress has been made in elucidating the canonical pathway, the non-canonical mechanisms remain less defined and require further investigation.
In this study, we revisit the non-canonical auxin signaling pathway mediated by the cell-surface complex Auxin Binding Protein 1-Transmembrane Kinase 1 (ABP1-TMK1), with a particular focus on its downstream phosphorylation events. We reveal that this auxin-mediated phosphorylation is conserved across the green lineage, underscoring its fundamental role in plant development. We explore key phosphorylation targets, particularly PIN2, which is essential for root gravitropism. To further understand TMK1’s role in diverse developmental processes, we identified and investigated its interactors as potential co-receptors or regulatory components within its signaling network.
Given the previously established role of ABP1-TMK1 in auxin canalization, we sought to further investigate this process and identified several TMK1 interactors also involved in this intricate mechanism.
These findings provide new insights into the complex regulation of auxin canalization, highlighting a broader and more interconnected signaling framework than previously understood.},
  author       = {Monzer, Aline},
  issn         = {2663-337X},
  pages        = {160},
  publisher    = {Institute of Science and Technology Austria},
  title        = {{Cell-Surface Auxin Signaling: Linking molecular pathways to plant development}},
  doi          = {10.15479/AT-ISTA-19395},
  year         = {2025},
}

@unpublished{19398,
  abstract     = {Receptor-like kinases (RLKs), particularly the Transmembrane Kinase (TMK) family, play essential roles in signaling and development, with TMKs being key components of auxin perception and downstream phosphorylation events. While TMKs’ involvement in auxin canalization, a process essential for vasculature formation and regeneration, has been established, nonetheless, the additional signaling and regulatory partners remain poorly understood. In this study, we identify and characterize seven leucine-rich repeat RLKs (TINT1–TINT7) as novel interactors of TMK1, revealing their diverse evolutionary, structural, and functional characteristics. Our results show that TINTs interact with TMK1 and highlight their roles in regulating various developmental processes. Majority of TINTs contributes, together with TMK1, to auxin canalization, with TINT5 linking TMK1 to other canalization component CAMEL. Beyond canalization, we also establish the role of TINT-TMK1 interactions in processes such as stomatal movement and the hypocotyl’s gravitropic response. These findings suggest that TINTs, through their interaction with TMK1, are integral components of various signaling networks, contributing to both auxin canalization and broader plant development.},
  author       = {Monzer, Aline and Mazur, Ewa and Rodriguez Solovey, Lesia and Gallei, Michelle C and Zou, Minxia and Smejkal, Michael and Cervenova, Ema and Friml, Jiří},
  booktitle    = {bioRxiv},
  publisher    = {Cold Spring Harbor Laboratory},
  title        = {{TMK interacting network of receptor like kinases for auxin canalization and beyond}},
  doi          = {10.1101/2025.02.28.640727},
  year         = {2025},
}