Our laboratory is interested in the structural and functional characterization of macromolecular assemblies, with special emphasis on the large protein complex that regulates transport between the nucleus and the cytoplasm in eukaryotic cells: the nuclear pore complex (NPC). Apart from its main role as mediator of nucleocytoplasmic transport, the NPC is also a key platform for the regulation of many essential nuclear processes, such as chromatin organization, gene expression, or DNA repair. It is thus not surprising that defects affecting the NPC function are directly related to severe human diseases, like several types of cancers and neurological disorders. To understand how the NPC performs its roles we use a combination of approaches, including biochemical, proteomic, cell and structural biology methods, that are finally combined into integrative structure-function maps to reveal the basic molecular mechanisms underlying the NPC function.