A Reemerging Bright Soft X-Ray State of the Changing-look Active Galactic Nucleus 1ES 1927+654:A Multiwavelength View

1ES1927+654 is a nearby active galactic nucleus (AGN) that has shown an enigmatic outburst in optical/UV followed by X-rays, exhibiting strange variability patterns at timescales of months to years. Here we report the unusual X-ray, UV, and radio variability of the source in its postflare state (2022 January–2023 May). First, we detect an increase in the soft X-ray (0.3–2 keV) flux from 2022 May to 2023 May by almost a factor of 5, which we call the bright soft state. The hard X-ray 2–10 keV flux increased by a factor of 2, while the UV flux density did not show any significant changes (≤30%) in the same period. The integrated energy pumped into the soft and hard X-rays during this period of 11 months is ∼3.57 × 10 ^50 erg and 5.9 × 10 ^49 erg, respectively. From the energetics, it is evident that whatever is producing the soft excess (SE) is pumping out more energy than either the UV or hard X-ray source. Since the energy source presumably is ultimately the accretion of matter onto the supermassive black hole, the SE-emitting region must be receiving the majority of this energy. In addition, the source does not follow the typical disk–corona relation found in AGNs, neither in the initial flare (from 2017 to 2019) nor in the current bright soft state (2022–2023). We found that the core (<1 pc) radio emission at 5 GHz gradually increased until 2022 March, but showed a dip in 2022 August. The Güdel–Benz relation ( L _radio / L _X-ray ∼ 10 ^−5 ), however, is still within the expected range for radio-quiet AGNs, and further follow-up radio observations are currently being undertaken

Trap-State Dynamics in Visible-Light-Emitting ZnO:MgO Nanocrystals

Oleate-capped ZnO:MgO nanocrystals have been synthesized that are soluble in nonpolar solvents and which emit strongly in the visible region (450−600 nm) on excitation by UV radiation. The visible emission involves recombination of trap states of the nanocrystalline ZnO core and has a higher quantum yield than the band gap UV exciton emission. The spectrally resolved dynamics of the trap states have been investigated by time-resolved emission spectroscopy. The time-evolution of the photoluminescence spectra show that there are, in fact, two features in the visible emission whose relative importance and efficiencies vary with time. These features originate from recombination involving trapped electrons and holes, respectively, and with efficiencies that depend on the occupancy of the trap density of states

Spectrally Resolved Resonance Energy Transfer from ZnO:MgO Nanocrystals

Resonance energy transfer (RET) from the visible emission of core−shell ZnO:MgO nanocrystals to Nile Red chromophores, following band gap excitation in the UV, has been investigated for four different nanocrystal sizes. With use of steady state and time-resolved fluorescence spectroscopic measurements the wavelength dependent RET efficiencies have been determined. The RET process in ZnO:MgO nanocrystals occurs from emissions involving trap state recombination. There are two such processes with different RET efficiencies for the same particle size. This is shown to be a consequence of the fact that the recombination processes giving rise to the two emissions are located at different distances from the center of the particle so that the donor−acceptor distances for the two are different, even for the same particle size

The strong propensity of Cadherin‐23 for aggregation inhibits cell migration

Cadherin‐23 (Cdh23), a long‐chain non‐classical cadherin, exhibits strong homophilic and heterophilic binding. The physiological relevance of strong heterophilic binding with protocadherin‐15 at neuroepithelial tip links is well‐studied. However, the role of Cdh23 homodimers in physiology is less understood, despite its widespread expression at the cell boundaries of various human and mouse tissues, including kidney, muscle, testes, and heart. Here, we performed immunofluorescence studies that revealed that Cdh23 is present as distinct puncta at the cell–cell boundaries of cancer cells. Analysis of patient data and quantitative estimation of Cdh23 in human tissues (normal and tumor) also indicated that Cdh23 is down‐regulated via promoter methylation in lung adenocarcinoma (AD) and esophageal squamous cell carcinoma (SCC) cells; we also observed a clear inverse correlation between Cdh23 expression and cancer metastasis. Using HEK293T cells and four types of cancer cells differentially expressing Cdh23, we observed that cell migration was faster in cells with reduced levels of Cdh23 expression. The cell migration rate in cancer cells is further accelerated by the presence of excretory isoforms of Cdh23, which loosen its cell‐adhesion ability by competitive binding. Overall, our data indicate the role of Cdh23 as a suppressor of cell migration

Different roles of cadherins in the assembly and structural integrity of the desmosome complex.

International audience: Adhesion between cells is established by the formation of specialized intercellular junctional complexes, such as desmosomes. Desmosomes comprise two members of the cadherin superfamily of cell adhesion proteins, desmocollin (Dsc) and desmoglein (Dsg), but their combinatorial roles in desmosome assembly is not understood. To uncouple desmosome assembly from other cell-cell adhesion complexes, we used micro-patterned substrates of Dsc2aFc and/or Dsg2Fc and collagen IV; we show that Dsc2aFc, but not Dsg2Fc, was necessary and sufficient to recruit desmosome-specific desmoplakin into desmosome puncta and produce strong adhesive binding. Single Molecule Force Spectroscopy showed that monomeric Dsc2a, but not Dsg2, formed Ca(2+)-dependent homophilic bonds, and that Dsg2 formed Ca(2+)-independent heterophilic bonds with Dsc2a. A W2A mutation in Dsc2a inhibited Ca(2+)-dependent homophilic binding, similar to classical cadherins, and Dsc2aW2A, but not Dsg2W2A, was excluded from desmosomes in MDCK cells. These results indicate that Dsc2a, not Dsg2, is required for desmosome assembly via homophilic Ca(2+)- and W2/strand swap-dependent binding, and that Dsg2 may be involved later in regulating a switch to Ca(2+)-independent adhesion in mature desmosomes

Interdomain linkers tailor the stability of immunoglobulin repeats in polyproteins

International audienceLinkers in polyproteins are considered as mere spacers between two adjacent domains. However, a series of studies using single-molecule force spectroscopy have recently reported distinct thermodynamic stability of I27 in polyproteins with varying linkers and indicated the vital role of linkers in domain stability. A flexible glycine rich linker (-(GGG)n, n≥3) featured unfolding at lower forces than regularly used arg-ser (RS) based linker. Interdomain interactions among I27 domains in Gly-rich linkers were suggested to lead to reduced domain stability. However, the negative impact of inter domain interactions on domain stability is thermodynamically counter-intuitive and demanded thorough investigations. Here, using an array of ensemble equilibrium experiments and in-silico measurements with I27 singlet and doublets with two aforementioned linkers, we delineate that the inter-domain interactions in fact raise the stability of the polyprotein with RS linker. More surprisingly, a highly flexible Gly-rich linker has no interference on the stability of polyprotein. Overall, we conclude that flexible linkers are preferred in a polyprotein for maintaining domain's independence