PRKCE Protein, Human (Active, sf9, GST)

PKCE, a calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase, plays pivotal roles in regulating diverse cellular processes associated with cytoskeletal proteins, including cell adhesion, motility, migration, and cell cycle control. In cardiac fibroblasts, PKCE mediates angiotensin-2-induced integrin beta-1 (ITGB1) activation, facilitating cell adhesion to the extracellular matrix. It phosphorylates MARCKS, leading to PTK2/FAK activation and subsequent cardiomyocyte spreading. In mesenchymal cells, PKCE governs the directional transport of ITGB1 by phosphorylating vimentin (VIM). In epithelial cells, it associates with and phosphorylates keratin-8 (KRT8), influencing desmoplakin targeting at desmosomes and regulating cell-cell contact. Additionally, PKCE phosphorylates IQGAP1, promoting epithelial cell detachment prior to migration. In various contexts, such as HGF-induced cell migration, wound healing, and cytokinesis, PKCE demonstrates its versatility in coordinating complex cellular events. It also plays crucial roles in cardiac myocytes, nerve growth factor (NGF)-induced neurite outgrowth, and immune responses. Notably, PKCE influences prostate cancer cell invasion through phosphorylation of STAT3 and participates in the LPS-induced immune response via TICAM2/TRAM activation. In differentiating erythroid progenitors, PKCE is regulated by EPO, providing protection against TNFSF10/TRAIL-mediated apoptosis. Additionally, PKCE is implicated in insulin-induced phosphorylation and activation of AKT1, as well as the modulation of AKT pathway activation in cumulus cells through NLRP5/MATER phosphorylation.