NEDD1 is a centrosomal protein essential for microtubule nucleation and mitotic spindle assembly. Structurally, NEDD1 contains conserved WD40 repeats and forms a tetrameric α-helical assembly at its C-terminus that directly binds the γ-tubulin ring complex (γ-TuRC) 1. This interaction recruits and anchors γ-TuRC to centrosomes and the mitotic spindle, enabling microtubule nucleation 2. NEDD1 depletion causes loss of γ-TuRC from centrosomes and failure of spindle assembly 2. Beyond canonical nucleation, NEDD1 bridges augmin and γ-TuRC during branching microtubule nucleation; this bridging function requires CDK1 and PLK1-dependent phosphorylation and involves NEDD1's intrinsic microtubule affinity 3. PLK4-mediated phosphorylation of NEDD1 at S325 initiates centriole biogenesis by promoting SAS-6 recruitment 4. Centrosomal glutamylation recruits NEDD1 via electrostatic interactions, ensuring proper microtubule nucleation and ciliogenesis 5. Clinically, NEDD1 is significantly overexpressed in hepatocellular carcinoma, correlating with poor prognosis and reduced immunotherapy response 6. These findings establish NEDD1 as a critical hub regulating multiple aspects of centrosome biology and identify it as a potential therapeutic target in cancer.