Function
PIAS1 functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and acting as a SUMO-tethering factor. It plays a crucial role in transcriptional coregulation across various cellular pathways, including the STAT pathway, the p53 pathway, and the steroid hormone signaling pathway. In vitro, PIAS1 binds to A/T-rich DNA. The effects of this transcriptional coregulation, whether transactivation or silencing, may vary depending on the specific biological context. PIAS1 sumoylates PML (at Lys-65 and Lys-160) and PML-RAR, promoting their ubiquitin-mediated degradation. PIAS1-mediated sumoylation of PML facilitates its interaction with CSNK2A1/CK2, which in turn promotes PML phosphorylation and degradation. PIAS1 enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. PIAS1 plays a dynamic role in adipogenesis by promoting the SUMOylation and degradation of CEBPB.