VPS26C is a core component of the Retriever complex, a trimeric assembly that includes VPS35L and VPS29, which functions as a major endosomal recycling machinery distinct from the retromer pathway 1. VPS26C integrates with the CCC complex (containing COMMD1-10, CCDC22, and CCDC93) to form the Commander complex, a 16-protein assembly critical for endosomal cargo recycling 2. Mechanistically, VPS26C participates in recycling diverse transmembrane proteins from endosomes back to the cell surface through interaction with the cargo adaptor SNX17, which binds to a conserved interface between VPS35L and VPS26C subunits 3. This interaction is regulated by cargo-binding and membrane phosphatidylinositol-3-phosphate recognition, enabling selective cargo recruitment 4. VPS26C mutations are associated with Ritscher-Schinzel syndrome, reflecting its essential role in endosomal trafficking 2. Beyond integrin and signaling receptor recycling, the Commander complex containing VPS26C has been implicated in cell cycle regulation, immune response, and cilium assembly 5. Cancer-associated mutations in VPS26C disrupt complex formation and impair membrane protein homeostasis 6, underscoring its clinical relevance in disease pathogenesis.