# Paxillin’s nuclear switch: orchestrating gene splicing for brain plasticity

## TL;DR

Paxillin, a protein known for cell adhesion, now acts in the nucleus to control gene splicing during brain development.

## Contribution

Paxillin's nuclear role in regulating alternative splicing during synaptic refinement is newly identified.

## Key findings

- Paxillin's phosphorylation at serine 119 enables its nuclear translocation.
- Nuclear paxillin fine-tunes gene splicing programs in developing neurons.
- This process is critical for synaptic refinement during sensitive developmental periods.

## 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.

Recent work in The EMBO Journal uncovers the regulatory role of nuclear paxillin in alternative splicing for synaptic refinement during brain development.