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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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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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Histone Modification02:32

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The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
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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.
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The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
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Related Experiment Video

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Purification of Tubulin with Controlled Posttranslational Modifications and Isotypes from Limited Sources by Polymerization-Depolymerization Cycles
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Posttranslational Modifications of RAS Proteins.

Ian Ahearn1, Mo Zhou1, Mark R Philips1

  • 1Department of Medicine, Perlmutter Cancer Center, New York University School of Medicine, New York, New York 10016.

Cold Spring Harbor Perspectives in Medicine
|January 10, 2018
PubMed
Summary

RAS proteins regulate cell growth and are key in cancer. This review focuses on their posttranslational modifications (PTMs), which are crucial for RAS activity and potential drug targets.

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Area of Science:

  • Molecular Biology
  • Oncogenesis
  • Biochemistry

Background:

  • The three human RAS genes encode four proteins critical for cell signaling.
  • RAS proteins function as molecular switches regulating growth and differentiation pathways.
  • Aberrant RAS signaling is a hallmark of many human cancers, driving oncogenesis.

Purpose of the Study:

  • To review the posttranslational modifications (PTMs) of RAS proteins.
  • To highlight the enzymes involved in RAS PTMs as potential therapeutic targets.
  • To provide a comprehensive overview of RAS PTMs in the context of cancer biology.

Main Methods:

  • Literature review of studies on RAS protein modifications.
  • Analysis of enzymatic pathways governing RAS PTMs.
  • Synthesis of current knowledge on RAS PTMs and their functional consequences.

Main Results:

  • RAS proteins undergo diverse PTMs, including farnesylation, geranylgeranylation, palmitoylation, and others.
  • These PTMs are essential for RAS membrane localization and effector interactions.
  • Specific enzymes catalyzing PTMs represent promising targets for developing anti-RAS therapies.

Conclusions:

  • Posttranslational modifications are critical regulators of RAS protein function and signaling.
  • Targeting enzymes responsible for RAS PTMs offers a viable strategy for anti-cancer drug development.
  • Understanding RAS PTMs is fundamental for advancing oncogenesis research and therapeutic interventions.