Pim-1 translocates sorting nexin 6/TRAF4-associated factor 2 from cytoplasm to nucleus.

Pim-1, an oncogene product of serine/threonine kinase, has been found to play roles in apoptosis induction/suppression, cell-cycle progression and transcriptional regulation by phosphorylating the target proteins involved in these processes. The target proteins phosphorylated by Pim-1, including p100, Cdc25A, PAP-1 and heterochromatin protein 1, have been identified. The precise functions of Pim-1, however, are still poorly understood. In this study, we identified tumor necrosis factor receptor-associated factor 4-associated factor 2/sorting nexin 6 (TFAF2/SNX6) as a Pim-1-binding protein, and we found that TFAF2/SNX6 was phosphorylated and translocated from the cytoplasm to nucleus by Pim-1. This translocation of the protein was not affected by Pim-1-dependent phosphorylation. Since sorting nexins, including TFAF2/SNX6, have been reported to be located in the cytoplasm or membrane by association with several receptors of tyrosine- or serine/threonine-kinase, this is the first report of TFAF2/SNX6 being located in the nucleus after binding to Pim-1.