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International audience; mRNA translation is coupled to multiprotein complex assembly in the cytoplasm, or to protein delivery into intracellular compartments. Here, by combining systematic RNA immunoprecipitation and single molecule RNA imaging in yeast, we have provided a complete depiction of the co-translational events involved in the biogenesis of a large multiprotein assembly, the nuclear pore complex (NPC). We report that binary interactions between NPC subunits can be established during translation, in the cytoplasm. Strikingly, the nucleoporins Nup1/Nup2, together with a number of nuclear proteins, are instead translated at nuclear pores, through a mechanism involving interactions between their nascent N-termini and nuclear transport receptors. Uncoupling this co-translational recruitment further triggers the formation of cytoplasmic foci of unassembled polypeptides. Altogether, our data reveal that distinct, spatially-segregated modes of co-translational interactions foster the ordered assembly of NPC subunits, and that localized translation can ensure the proper delivery of proteins to the pore and the nucleus.