DOCK7 functions as a guanine nucleotide exchange factor (GEF) that activates Rac1 and Rac3 small GTPases, playing critical roles in neuronal development and cellular migration. In neurons, DOCK7 is required for STMN1 phosphorylation during axon formation and neuronal polarization 1. Beyond neurodevelopment, DOCK7 regulates tissue fluidification through a planar polarized MYO6-DOCK7-RAC1 axis that promotes coordinated cell migration in epithelial tissues 2. DOCK7 has emerged as a significant player in cancer biology. Tumor-associated macrophage-derived extracellular vesicles containing DOCK7 promote colorectal cancer metastasis by activating RAC1, which upregulates ABCA1 and increases cholesterol efflux, enhancing cancer cell motility 3. In ovarian cancer, DOCK7 overexpression promotes replication stress resistance through ATR-dependent phosphorylation and RAC1/Cdc42 activation, sensitizing cells to chemotherapy when depleted 4. Conversely, in EGFR-amplified glioblastomas, ligand-activated EGFR suppresses invasion by inhibiting DOCK7-regulated Rho GTPase signaling through BIN3 upregulation 5. Clinically, biallelic DOCK7 mutations cause developmental and epileptic encephalopathy 23, characterized by early-onset seizures, intellectual disability, cortical blindness, and distinctive dysmorphic features including occipital lobe atrophy and pontine hypoplasia 6. DOCK7 genetic variants also associate with serum lipid level variation 7, and DOCK7 interacts with Nbeal2 in platelet α-granule biology 8.