ABSTRACT
The mechanism of protein post-translational modifications in regulation of cell mitosis and genomic stability is always a hot issue in biological researches. The present review introduced the functional activity of de-SUMOylase SENP3 in sister chromatin dissociation at mitosis, and demonstrated a new molecular mechanism of cross-talk regulation between protein SUMOylation and phosphorylation in maintaining genomic stability.
ABSTRACT
Small ubiquitin-like modifier protein (SUMO) modification is a highly dynamic process, catalyzed by SUMO-specific activating (E1), conjugating (E2) and ligating (E3) enzymes, and reversed by a family of SUMO-specific proteases (SENPs). There are six members of the human SENP family, and each SENP has different cellular locations and substrate specificities. However, the precise roles of SENPs in cellular processes have not been elucidated to date. This brief review will focus on recent advances pertaining to the identified targets of SENP1 and its potential role in prostate cancer.