CD47 is a multifunctional cell surface glycoprotein that serves as a critical immune checkpoint regulator. The protein functions primarily as a 'don't eat me' signal by binding to SIRPα on myeloid cells, particularly macrophages, thereby inhibiting phagocytosis 1. This CD47/SIRPα axis is frequently exploited by cancer cells, which overexpress CD47 to evade immune surveillance and phagocytic clearance 2. Beyond its role in immune evasion, CD47 acts as a receptor for thrombospondin-1 and modulates various cellular processes including cell adhesion, angiogenesis, and apoptosis. In pancreatic islets, CD47 is expressed by β cells and other islet cell types, with islets secreting substantial amounts of thrombospondin-1 3. The protein undergoes post-translational regulation through deubiquitination by USP2, which stabilizes CD47 expression 4. Therapeutically, anti-CD47 antibodies are being investigated for cancer treatment, though their efficacy requires Fc-FcγR interactions for optimal antitumor activity 5. Interestingly, CD47 blockade can enhance T cell-mediated tumor destruction through dendritic cell cross-priming rather than direct macrophage activation 6. CD47 also localizes to specialized subcellular domains called TIGER domains, where it can establish functionally relevant protein-protein interactions 7.