Rap1 belongs to the Ras subgroup of small GTP-binding proteins. Whereas its early history has focused on its biochemical homology to Ras and the alleged functional antagonism between these two small GTPases, recent cellular evidence suggests that endogenous Rap1 plays a unique, Ras-independent role in eukaryotic cells. Activated by virtually all receptor types and second messengers, Rap1 controls adhesion-related functions such as phagocytosis, cell-cell contacts and functional activation of integrins through inside-out signalling. Whereas the precise mechanism by which its downstream effectors exert these diverse functions is unknown, Rap1 seems to fulfil the evolutionarily conserved function of patterning the eukaryotic cell, thus enabling it to respond to its environment, in particular through cytoskeletal remodelling.