PKN1 is a serine/threonine protein kinase that regulates multiple cellular processes including cytoskeletal dynamics, cell migration, and transcriptional activity. As a Rho effector, PKN1 phosphorylates cytoskeletal proteins such as vimentin and neurofilament proteins, inhibiting their polymerization and regulating the actin cytoskeleton organization [UniProt Function]. PKN1 also phosphorylates tau protein at multiple sites, reducing microtubule binding and disrupting tubulin assembly [UniProt Function]. In transcriptional regulation, PKN1 acts as a coactivator of androgen receptor-dependent gene expression by phosphorylating histone H3 at threonine 11, marking chr19 for transcriptional activation [UniProt Function]. Clinically, PKN1 is significantly elevated in gliomas and correlates with histopathological grade 1. PKN1 knockdown in glioblastoma cells inhibits proliferation, invasion, and migration while promoting apoptosis through downregulation of YAP, a Hippo pathway effector 1. PKN1 upregulation conversely enhances malignant characteristics and YAP expression 1. The selective estrogen receptor modulator raloxifene effectively targets PKN1 to inhibit glioblastoma cell proliferation and sensitizes cells to temozolomide chemotherapy 1, suggesting PKN1 inhibition as a potential therapeutic strategy for gliomas. These findings establish PKN1 as a promising therapeutic target in cancer biology.