FRX proteins bring new perspectives to nucleoporins' homeostasis.

FXR proteins are part of ribonucleoprotein granules controlling stability, translation, and cellular localization of target mRNAs. In the current issue, Agote-Aran et al extend the repertoire of FXR protein action and show that they are also involved in the transport of nuclear pore complex components to the nuclear envelope and thereby prevent cytoplasmic aggregation of these proteins.