Extracellular signal-regulated kinase 2 (ERK2) mediates phosphorylation and inactivation of nuclear interaction partner of anaplastic lymphoma kinase (NIPA) at G₂/M

Background: NIPA is involved in timing mitotic entry and is inactivated by phosphorylation. The kinase responsible for NIPA phosphorylation at G ₂/M is unknown. Results: We show that cell cycle-dependent phosphorylation of NIPA is mediated by ERK2. Conclusion: NIPA is identified as one of the very few ERK2-specific substrates at the G₂/M transition. Significance: This demonstrates divergent functions of ERK1 and ERK2 in cell cycle regulation.