ENSA Protein, Human (Biotinylated, His)

ENSA protein, a pivotal phosphatase inhibitor, exerts precise control over protein phosphatase 2A (PP2A) during mitosis, specifically inhibiting its activity. Phosphorylation at Ser-67 during mitosis facilitates a specific interaction with PPP2R2D (PR55-delta), leading to the inactivation of PP2A. This orchestrated inactivation of PP2A is crucial for maintaining high cyclin-B1-CDK1 activity during the M phase, underscoring ENSA's regulatory role in cell cycle progression. Beyond its mitotic functions, ENSA also operates as a stimulator of insulin secretion by interacting with the sulfonylurea receptor (ABCC8), preventing sulfonylurea binding and reducing K(ATP) channel currents. Notably, ENSA's interactions with PPP2R2D and ABCC8 highlight its diverse roles in both cell cycle control and insulin secretion regulation, showcasing its significance in maintaining cellular homeostasis and functional integrity. Additionally, ENSA's interaction with SNCA, disrupted upon phosphorylation at Ser-109, further emphasizes its dynamic involvement in cellular processes.