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Cysteine-based regulation of redox-sensitive Ras small GTPases

Samantha Messina1, Giovanna De Simone1, Paolo Ascenzi1

  • 1Department of Science, Roma Tre University, Viale Guglielmo Marconi 446, I-00146, Roma, Italy.

Redox Biology
|August 7, 2019
PubMed

Insights

Reactive oxygen and nitrogen species (ROS and RNS) regulate Ras proteins, crucial in cancer development. Cysteine oxidation in Ras impacts its function, offering potential therapeutic targets for cancer and other diseases.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Oncology

Background:

  • Ras small GTPases (HRAS, NRAS, KRAS) are key regulators of cellular processes and frequently mutated in human cancers.
  • Ras proteins are redox-sensitive, with their function modulated by reactive oxygen and nitrogen species (ROS and RNS).

Purpose of the Study:

  • To review the pathophysiological role of cysteine redox regulation in Ras proteins.
  • To highlight the involvement of Ras redox biology in cancer, heart, and brain diseases.

Main Methods:

  • Literature review focusing on Ras protein structure, function, and redox-sensitive cysteine residues.
  • Analysis of the impact of ROS/RNS on Ras protein stability, activity, localization, and interactions.
  • Examination of oncogenic mutations affecting Ras cysteine residues as potential drug targets.

Main Results:

  • The NKCD motif (Asn116-Lys117-Cys118-Asp119) is critical for Ras redox sensitivity, with Cys118 oxidation affecting protein properties.
  • Additional cysteine residues (80, 181, 184, 186) also contribute to Ras modulation.
  • Specific oncogenic mutations (Gly12Cys, Gly13Cys) create new oxidative centers, presenting actionable therapeutic opportunities.

Conclusions:

  • Cysteine redox regulation is a critical mechanism influencing Ras protein function in health and disease.
  • Targeting Ras cysteine oxidation holds promise for novel therapeutic strategies in oncology and other diseases.
Keywords:
Cysteine 118Ras small GTPasesRedox-signalling

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