The annexin superfamily consists of 13 calcium or calcium and phospholipid binding proteins with high biological and structural homology. Annexin-1 (ANXA1) is the first characterized member of the annexin family of proteins and is able to bind to cellular membranes in a calcium-dependent manner, promoting membrane fusion and endocytosis. Annexin A1 has anti-inflammatory properties and inhibits phospholipase A2 activity. Annexin A1 can accumulate on internalized vesicles after EGF-stimulated endocytosis and may be required for a late stage in inward vesiculation. Phosphorylation by PKC, EGFR, and Chak1 results in inhibition of annexin A1 function. Annexin A1 has also been identified as one of the 'eat-me' signals on apoptotic cells that are to be recognized and ingested by phagocytes. Annexin A1, as an endogenous anti-inflammatory mediator, has roles in many diverse cellular functions, such as membrane aggregation, inflammation, phagocytosis, proliferation, apoptosis, and tumorigenesis and cancer development.