Error free translation of the genetic code to proteins is key to cellular growth and proliferation. This essential task is carried by the ribosome. While the structure of the mature ribosome is giving insights into the mechanism of translation, our knowledge regarding the assembly, quality control and intracellular targeting of this universal machine is rapidly emerging. We combine diverse functional approaches in the model organism budding yeast with structural biology (Cryo-EM and NMR) and mass spectrometry technologies (SWATH-MS and XL-MS) to reveal three aspects of eukaryotic ribosome assembly:

1. Mechanisms that link nucleocytoplasmic transport with the ribosome assembly pathway.
2. Mechanisms that regulate compositional dynamics of assembly factors on maturing pre-ribosomes.
3. Quality control steps that permit only correctly assembled pre-ribosomes for translation.

Understanding eukaryotic ribosome assembly will uncover the molecular basis for globally altered proteomes that are implicated in a growing list of Ribosomopathies- human diseases linked to impaired ribosome assembly and function. This knowledge will also set a strong basis for the targeted development of a new class of inhibitors that may challenge antibiotic resistant bacteria, fungi and parasites.