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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.
Ras is a...
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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:
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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...
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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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Protein Modifications in the RER01:26

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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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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...
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Updated: Oct 25, 2025

Fully Processed Recombinant KRAS4b: Isolating and Characterizing the Farnesylated and Methylated Protein
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Post-translational modification of RAS proteins.

Sharon L Campbell1, Mark R Philips2

  • 1University of North Carolina School of Medicine, USA.

Current Opinion in Structural Biology
|August 8, 2021
PubMed
Summary

RAS proteins, crucial in cancer, are regulated by more than just nucleotide binding. Post-translational modifications (PTMs) add another layer of control, offering potential new drug targets for cancer therapy.

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CancerGTPasePost-translational modificationRASSignaling

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Area of Science:

  • Molecular Biology
  • Oncology
  • Biochemistry

Background:

  • RAS genes are frequently mutated in cancer, acting as key oncogenes.
  • RAS proteins function as molecular switches, regulating cellular growth pathways.
  • Historically, RAS regulation was thought to be solely dependent on GTP/GDP binding.

Purpose of the Study:

  • To explore the role of post-translational modifications (PTMs) in RAS protein regulation.
  • To understand the functional consequences and physiological relevance of RAS PTMs.
  • To identify potential drug discovery targets among enzymes catalyzing RAS PTMs.

Main Methods:

  • This study focuses on the biological implications of RAS protein modifications.
  • Investigates the enzymatic regulation of RAS signaling pathways.
  • Literature review and analysis of current research on RAS PTMs.

Main Results:

  • RAS proteins are subject to a wide range of post-translational modifications.
  • These PTMs represent a significant, yet not fully understood, layer of RAS regulation.
  • Enzymes involved in PTMs are promising targets for therapeutic intervention in cancers driven by RAS mutations.

Conclusions:

  • RAS protein regulation extends beyond nucleotide binding to include PTMs.
  • Understanding RAS PTMs is critical for deciphering their role in cancer.
  • Targeting enzymes that modify RAS proteins offers a promising avenue for novel cancer therapies.