Original story from the University of Basel (Switzerland). Nuclear pore complexes are more dynamic than previously thought, reshaping our understanding of a vital transport process in cells. An international study led by the University of Basel (Switzerland) has discovered that nuclear pore complexes (NPC) – tiny gateways in the nuclear membrane – are not rigid or gel-like as once thought. Their interiors are dynamically organized, constantly moving and rearranging. The findings reshape our understanding of a vital transport process in cells and have implications for diseases and potential therapies. Imagine the cell’s nucleus as a bank vault protected by a highly sophisticated security system: the NPC. Only proteins carrying the correct ‘key’ – specialized transport factors – are granted exclusive access. This selective control over what enters and exits the nucleus is essential for ensuring proper communication between the genome protected inside it and the cellular machinery outside. Infographic: Investigating biomechanics with atomic force microscopy In this infographic, we dive into how AFM works, the technical features one must consider and how it can be implemented for biomechanical investigation. Nanoscience leads to new biological insights Despite its importance, the NPC’s inner workings have remained a mystery. Its transport channel is lined with highly flexible protein ‘threads’ – the FG nucleoporins (FG Nups) – that create a selective barrier whose ultra-fine organization has eluded even the most powerful electron microscopes. Because the FG Nups can form gel-like assemblies outside of cells, older models have compared the NPC’s function to a rigid…
