To avoid deleterious misfolding of proteins, the assembly of multiprotein complexes is tightly controlled and can either occur co-translationally in the cytoplasm or as a spatially restricted event by targetting ribosomes at particular subcellular locations. In an article recently published in Molecular Cell, Benoit Palancade’s team (Institut Jacques Monod) showed that both phenomenon are at play in the biogenesis of the nucleopore, one of the largest multiprotein complex in the cells. The “genetics networks” team from LCQB contributed to this work by conducting genome-wide analyses of the interactions between nucleoporins (key nucleopore subunits) during translation
