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

Open Access
Publisher Website
Google Scholar
Abstract
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.