DOK1 (docking protein 1) functions as an enzymatically inert adaptor protein that provides scaffolding for multimolecular signaling complexes and exhibits complex roles in cellular regulation. The protein shuttles between nucleus and cytoplasm through a CRM1-dependent nuclear export system, with subcellular localization regulated by tyrosine phosphorylation and external stimuli 1. DOK1 serves as a negative regulator in multiple signaling pathways, including natural killer cell activation where it reduces cell activation induced by NK-cell-activating receptors 2. The protein interacts with RasGAP through dual SH2 domain engagement, contributing to spatial-temporal regulation of Ras signaling 3. In cancer contexts, DOK1 exhibits paradoxical functions: it acts as a tumor suppressor that is frequently silenced by promoter hypermethylation in various human malignancies including head and neck cancers (93%) and lung cancers (81%) 4, yet it also promotes clear cell renal cell carcinoma progression through PI3K/AKT/GSK3β signaling 5. DOK1 participates in lysosomal repair through microlysophagy, where STK38-mediated phosphorylation enables VPS4 recruitment for ESCRT disassembly 6. Additionally, DOK1 modulates integrin β1 signaling and invadopodia formation in breast cancer invasion 7.