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Related Concept Videos

The Ras Gene02:38

The Ras Gene

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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.
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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Related Experiment Video

Updated: Sep 4, 2025

Fully Processed Recombinant KRAS4b: Isolating and Characterizing the Farnesylated and Methylated Protein
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A Proteomic Approach Identifies Isoform-Specific and Nucleotide-Dependent RAS Interactions.

Seth P Miller1, George Maio1, Xiaoyu Zhang1

  • 1Department of Chemistry and Chemical Biology, Cornell University, Ithaca, New York, USA.

Molecular & Cellular Proteomics : MCP
|July 15, 2022
PubMed
Summary

This study reveals distinct protein interactions for each RAS protein isoform, uncovering new potential cancer drug targets. These findings help clarify the specific roles of RAS isoforms in cancer development and treatment.

Keywords:
CARM1GTPaseHRASKRASRADILRAScancerinteractomeproteomicssenescence

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Area of Science:

  • Oncology
  • Molecular Biology
  • Proteomics

Background:

  • RAS proteins (KRAS4A, KRAS4B, HRAS, NRAS) are frequently mutated in human cancers.
  • Despite known overlapping functions, RAS isoforms exhibit preferential activation in tumors, suggesting isoform-specific roles.

Purpose of the Study:

  • To comparatively analyze and quantitatively determine the isoform-specific and nucleotide-dependent interactomes of the four RAS isoforms.
  • To identify novel effector proteins and therapeutic targets for RAS-driven cancers.

Main Methods:

  • Quantitative proteomics was employed to generate comprehensive interactome maps for each RAS isoform.
  • Wild-type and constitutively active mutant RAS isoforms were analyzed to identify differences in protein interactions.

Main Results:

  • Numerous isoform-specific interacting proteins were identified, including HRAS-specific CARM1 and CHK1, and KRAS-specific PIP4K2C and IPO7.
  • Potential novel RAS effector proteins, such as RADIL, were discovered.
  • The HRAS-specific protein CARM1 was found to play a role in HRAS-induced senescence, with its inhibition selectively affecting HRAS-transformed cells.

Conclusions:

  • The study identified new isoform-specific and nucleotide-dependent RAS interactors.
  • These findings provide insights into the distinct functions of RAS isoforms and offer potential therapeutic strategies for targeting RAS-driven cancers.