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The Ras Superfamily of Small GTPases: The Unlocked Secrets

  • Luca Goitre
  • Eliana Trapani
  • Lorenza Trabalzini
  • Saverio Francesco Retta
Part of the Methods in Molecular Biology book series (MIMB, volume 1120)

Abstract

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.

Key words

Small GTPases Ras superfamily Posttranslational modifications of Ras GTPases Subcellular dynamics of Ras GTPases Function and regulation of Ras GTPases Signaling of Ras GTPases 

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Copyright information

© Springer Science+Business Media, LLC 2014

Authors and Affiliations

  • Luca Goitre
    • 1
  • Eliana Trapani
    • 1
  • Lorenza Trabalzini
    • 2
  • Saverio Francesco Retta
    • 1
  1. 1.Department of Clinical and Biological SciencesUniversity of TorinoTorinoItaly
  2. 2.Department of Biotechnology, Chemistry, and PharmacyUniversity of SienaSienaItaly

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