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

Abstract

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. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.