Abstract
Paxillin, long known as a cytoplasmic scaffold protein involved in cell adhesion and migration, emerges in a new role as a nuclear regulator of alternative splicing in developing neurons. In this issue of The EMBO Journal, Chu and colleagues reveal that activity-dependent phosphorylation of paxillin at serine 119 promotes its nuclear translocation, enabling it to fine-tune gene splicing programs critical for synaptic refinement during sensitive periods of brain development.