Terahertz cavity magnon polaritons

Hybrid light-matter coupled states, or polaritons, in magnetic materials have attracted significant attention due to their potential for enabling novel applications in spintronics and quantum information processing. However, most studies to date have been carried out for ferromagnetic materials with magnon excitations at gigahertz frequencies. Here, we have investigated strong resonant photon-magnon coupling at frequencies above 1 terahertz for the first time in a prototypical room-temperature antiferromagnetic insulator, NiO, inside a Fabry-P\'erot cavity. The cavity was formed by the crystal itself when it was thinned down to an optimized thickness. By using terahertz time-domain spectroscopy in high magnetic fields up to 25 T, we swept the magnon frequency through Fabry-P\'erot cavity modes and observed photon-magnon anticrossing behavior, demonstrating clear vacuum Rabi splittings exceeding the polariton linewidths. These results show that NiO is a promising platform for exploring antiferromagnetic spintronics and cavity magnonics in the terahertz frequency range

Tensin3 interaction with talin drives the formation of fibronectin-associated fibrillar adhesions

The formation of healthy tissue involves continuous remodeling of the extracellular matrix (ECM). Whilst it is known that this requires integrin-associated cell-ECM adhesion sites (CMAs) and actomyosin-mediated forces, the underlying mechanisms remain unclear. Here, we examine how tensin3 contributes to the formation of fibrillar adhesions (FBs) and fibronectin fibrillogenesis. Using BioID mass spectrometry and a mitochondrial targeting assay, we establish that tensin3 associates with the mechanosensors such as talin and vinculin. We show that the talin R11 rod domain binds directly to a helical motif within the central intrinsically disordered region (IDR) of tensin3, whilst vinculin binds indirectly to tensin3 via talin. Using CRISPR knock-out cells in combination with defined tensin3 mutations, we show (i) that tensin3 is critical for the formation of α5β1-integrin FBs and for fibronectin fibrillogenesis, and (ii) the talin/tensin3 interaction drives this process, with vinculin acting to potentiate it