PEAK1 (pseudopodium enriched atypical kinase 1) is a catalytically inactive pseudokinase that functions as a critical scaffolding protein regulating cell adhesion, migration, and barrier function. In normal physiology, PEAK1 maintains intestinal tight junction integrity by interacting with ZO-1 and protecting it from autophagy-mediated degradation, with Src-mediated phosphorylation of Y724 promoting this stabilization 1. PEAK1 regulates cell migration through Src-mediated Y635 phosphorylation, which facilitates indirect binding to integrins via Tensin3 and enables convergence of integrin and growth factor signaling 2. In cancer, PEAK1 promotes oncogenic signaling through multiple mechanisms. It activates CAMK2 via PLCγ1/Ca2+ signaling in triple-negative breast cancer, with RA306 (CAMK2 inhibitor) showing therapeutic potential 3. PEAK1 upregulation correlates with poor prognosis across multiple cancer types, promoting epithelial-mesenchymal transition (EMT), invasion, and metastasis in breast, lung, and gastric cancers 4, 5, 6. In prostate cancer, PEAK1 mediates docetaxel resistance by promoting M2 macrophage polarization through HIF-1α/STAT3/NF-κB pathway activation 7. Emerging evidence suggests PEAK1 itself may be therapeutically targeted, as miRNA-enriched plant exosomes modulating PEAK1 expression alleviate colitis 8.