The Ras Superfamily of Small GTPases: The Unlocked Secrets
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The Ras superfamily of small GTPases is composed of more than 150 members, which share a conserved structure and biochemical
properties, acting as binary molecular switches turned on by binding GTP and off by hydrolyzing GTP to GDP. However, despite
considerable structural and biochemical similarities, these proteins play multiple and divergent roles, being versatile and
key regulators of virtually all fundamental cellular processes. Conversely, their dysfunction plays a crucial role in the
pathogenesis of serious human diseases, including cancer and developmental syndromes.
Fuelled by the original identification in 1982 of mutationally activated and transforming human Ras genes in human cancer
cell lines, a variety of powerful experimental techniques have been intensively focused on discovering and studying structure,
biochemistry, and biology of Ras and Ras-related small GTPases, leading to fundamental research breakthroughs into identification
and structural and functional characterization of a huge number of Ras superfamily members, as well as of their multiple regulators
and effectors.
In this review we provide a general overview of the major milestones that eventually allowed to unlock the secret treasure
chest of this large and important superfamily of proteins.
