Acetylation of Prrp K150 regulates the subcellular localization

Posttranslational modifications of proteins have profound effects on many aspects of their function and have received much attention due to the importance of these processes in epigenetic regulation. In this study, we report that deleted azoospermia associated protein 1 (DAZAP1)/proline-rich RNA binding protein (Prrp), a multifunctional RNA binding protein which is essential for spermatogenesis and normal cell growth, is acetylated at Lysine 150 within its RNA binding domain. The acetylation is predominantly observed in nuclear Prrp, and the nonacetylated form is in cytoplasm. Considering that Prrp is a shuttling protein, we suggest that the acetylation cycle at Prrp K150 regulates nucleocytoplasmic transport in cells.

► Acetylation cycle is a regulatory switch which determines the direction of nucleocytoplasmic transport.
► Prrp at Lysine 150 is acetylated in nucleus, but not in cytoplasm.
► The acetylation defective mutant cannot enter nucleus.
► The acetylation at Prrp K150 is required to return nucleus.