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The Ras Gene

The Ras Gene

The Ras-gene-encoded proteins are regulators of signaling pathways controlling cell proliferation, differentiation, or cell survival. The Ras-gene family in humans constitutes three primary members—the HRas, NRas, and KRas. These genes code for four functionally distinct yet closely related proteins—the HRas, NRas, KRas4A, and KRas4B. The involvement of mutant Ras genes in human cancer was first discovered in 1982 and is among the most common causes of human tumorigenesis.
Ras is a superfamily...

Small GTPases - Ras and Rho

Small GTPases - Ras and Rho

Ras and Rho are small monomeric GTPases that act downstream of receptor tyrosine kinase (RTK) and regulate various cellular processes. These GTPases switch between active and inactive states by binding to guanine nucleotides.
Three regulatory proteins control their activity:

The Ras Gene

The Ras Gene

The Ras-gene-encoded proteins are regulators of signaling pathways controlling cell proliferation, differentiation, or cell survival. The Ras-gene family in humans constitutes three primary members—the HRas, NRas, and KRas. These genes code for four functionally distinct yet closely related proteins—the HRas, NRas, KRas4A, and KRas4B. The involvement of mutant Ras genes in human cancer was first discovered in 1982 and is among the most common causes of human tumorigenesis.
Ras is a superfamily...

MAPK Signaling Cascades

MAPK Signaling Cascades

Mitogen-activated protein kinase, or MAPK pathway, activates three sequential kinases to regulate cellular responses such as proliferation, differentiation, survival, and apoptosis. The canonical MAPK pathway starts with a mitogen or growth factor binding to an RTK. The activated RTKs stimulate Ras, which recruits Raf or MAP3 Kinase (MAPKKK), the first kinase of the MAPK signaling cascade. Raf further phosphorylates and activates MEK or MAP2 Kinases (MAPKK), which in turn phosphorylates MAP...

Abnormal Proliferation

Abnormal Proliferation

Under normal conditions, most adult cells remain in a non-proliferative state unless stimulated by internal or external factors to replace lost cells. Abnormal cell proliferation is a condition in which the cell's growth exceeds and is uncoordinated with normal cells. In such situations, cell division persists in the same excessive manner even after cessation of the stimuli, leading to persistent tumors. The tumor arises from the damaged cells that replicate to pass the damage to the daughter...

PI3K/mTOR/AKT Signaling Pathway

PI3K/mTOR/AKT Signaling Pathway

The mammalian target of rapamycin (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1 (mTORC1) and mTOR complex 2 (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast, mTORC2 consists of a rapamycin-insensitive companion...

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Related Experiment Video

Updated: May 17, 2026

Fully Processed Recombinant KRAS4b: Isolating and Characterizing the Farnesylated and Methylated Protein

Fully Processed Recombinant KRAS4b: Isolating and Characterizing the Farnesylated and Methylated Protein

Published on: January 16, 2020

Glutathiolated Ras: characterization and implications for Ras activation.

G Aaron Hobbs¹, Marcelo G Bonini, Harsha P Gunawardena

¹Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC 27599, USA.

Free Radical Biology & Medicine

|November 6, 2012

Summary

Ras GTPases are regulated by redox agents. Glutathione modification of Ras at cysteine 118 alters guanine nucleotide binding and activity only through a radical-mediated mechanism, protecting Ras from further activation.

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Last Updated: May 17, 2026

Fully Processed Recombinant KRAS4b: Isolating and Characterizing the Farnesylated and Methylated Protein

Fully Processed Recombinant KRAS4b: Isolating and Characterizing the Farnesylated and Methylated Protein

Published on: January 16, 2020

Characterize Disease-related Mutants of RAF Family Kinases by Using a Set of Practical and Feasible Methods

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Published on: July 17, 2019

Spectrophotometric Screening for Potential Inhibitors of Cytosolic Glutathione S-Transferases

Spectrophotometric Screening for Potential Inhibitors of Cytosolic Glutathione S-Transferases

Published on: October 10, 2020

Area of Science:

Molecular biology
Cellular signaling
Redox biology

Background:

Ras GTPases are key regulators of cellular processes, cycling between active and inactive states.
Ras activity is modulated by agents affecting guanine nucleotide binding and hydrolysis rates.
Redox agents like nitrogen dioxide can activate Ras by facilitating GDP dissociation.

Purpose of the Study:

To investigate the mechanism by which glutathione (GSH) modifies Ras and affects its guanine nucleotide binding properties.
To elucidate the role of cysteine 118 in Ras modification by glutathione.

Main Methods:

Nuclear Magnetic Resonance (NMR) spectroscopy
Top-down and bottom-up mass spectrometry
Biochemical analyses of glutathiolated H-Ras

Main Results:

Oxidized glutathione specifically glutathiolates H-Ras at cysteine 118.
Glutathiolation itself does not alter Ras structure or biochemical properties.
Changes in Ras guanine nucleotide binding and activity occur via a radical-mediated mechanism involving cysteine 118, not direct glutathiolation.
Ras glutathiolation protects against further free radical-mediated activation.

Conclusions:

Ras glutathiolation's effect on activity is dependent on a radical-mediated mechanism, not direct modification.
Cysteine 118 is crucial for radical-induced changes in Ras function.
Glutathiolation acts as a protective mechanism against excessive Ras activation by free radicals.