The Ras superfamily of small guanosine triphosphatases (GTPases) comprises over 150 human members, with evolutionary orthologs found in various organisms. This family is divided into five major branches: Ras, Rho, Rab, Ran, and Arf. These GTPases function as binary molecular switches, regulated by GDP/GTP cycling, and are controlled by guanine nucleotide-exchange factors (GEFs) and GTPase-activating proteins (GAPs). Post-translational modifications, such as lipid modifications, are crucial for their membrane targeting and subcellular localization. The Ras superfamily plays a central role in a wide range of cellular processes, including signaling networks, actin organization, vesicular transport, and nuclear transport. Each branch of the superfamily has distinct functions and regulatory mechanisms, contributing to the complexity and diversity of cellular activities.The Ras superfamily of small guanosine triphosphatases (GTPases) comprises over 150 human members, with evolutionary orthologs found in various organisms. This family is divided into five major branches: Ras, Rho, Rab, Ran, and Arf. These GTPases function as binary molecular switches, regulated by GDP/GTP cycling, and are controlled by guanine nucleotide-exchange factors (GEFs) and GTPase-activating proteins (GAPs). Post-translational modifications, such as lipid modifications, are crucial for their membrane targeting and subcellular localization. The Ras superfamily plays a central role in a wide range of cellular processes, including signaling networks, actin organization, vesicular transport, and nuclear transport. Each branch of the superfamily has distinct functions and regulatory mechanisms, contributing to the complexity and diversity of cellular activities.