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Related Concept Videos

Regulation of the Unfolded Protein Response01:31

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Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
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Cis-regulatory sequences are short fragments of non-coding DNA that are present on the same chromosomes as the genes that they regulate. These fragments serve as binding sites for transcriptional regulators, proteins that are responsible for controlling gene transcription and differential gene expression across cell types in eukaryotes. Cis-regulatory sequences can be close to the gene of interest or thousands of bases away in the DNA sequence; however, those sequences that are further away are...
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Exon Recombination02:32

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The evolution of new genes is critical for speciation. Exon recombination, also known as exon shuffling or domain shuffling, is an important means of new gene formation. It is observed across vertebrates, invertebrates, and in some plants such as potatoes and sunflowers. During exon recombination, exons from the same or different genes recombine and produce new exon-intron combinations, which might evolve into new genes. 
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The gene expression in cells is regulated at different stages: (i) transcription, (ii) RNA processing, (iii) RNA localization, and (iv) translation. Transcriptional regulation is mediated by regulatory proteins such as transcription factors, activators, or repressors—these control gene expression by initiating or inhibiting the transcription of genes. Once a precursor or pre-mRNA is produced, it undergoes post-transcriptional modification, including 5' capping, splicing, and the...
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Nuclear receptors, or NRs, are unique transcription factors that regulate gene transcription and affect the cellular pathways involved in reproduction, development, or metabolism. Their ability to be stimulated by small lipophilic ligands and control vital cellular processes makes them ideal drug targets. Nearly 10-15% of currently prescribed drugs target these receptors.
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Related Experiment Video

Updated: Jun 20, 2025

Monitoring On-Target Signaling Responses in Larval Zebrafish - Z-REX Unmasks Precise Mechanisms of Electrophilic Drugs and Metabolites
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Understanding P-Rex regulation: structural breakthroughs and emerging perspectives.

Gareth D Jones1, Andrew M Ellisdon1

  • 1Cancer Program, Biomedicine Discovery Institute, Monash University, Clayton 3800, Victoria, Australia.

Biochemical Society Transactions
|July 18, 2024
PubMed
Summary

This review details the structural basis of P-Rex1 autoinhibition and activation by PI(3,4,5)P3 and Gβγ. It also explores how mutations in P-Rex2 drive cancer progression by destabilizing autoinhibition.

Keywords:
G-proteinsGTPasesRacguanine nucleotide exchange factorphosphatidylinositolstructural biology

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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Rho GTPases are crucial regulators of cellular processes.
  • Guanine nucleotide exchange factors (GEFs) control Rho GTPase activity.
  • Diffuse B-cell Lymphoma (Dbl) GEFs are the largest GEF family, featuring a conserved Dbl homology domain.

Purpose of the Study:

  • To review the structural basis of P-Rex1 autoinhibition and synergistic activation.
  • To explore regulatory mechanisms of P-Rex GEFs, including PI(3,4,5)P3 and Gβγ binding.
  • To infer the role of P-Rex2 mutations in cancer progression.

Main Methods:

  • Structural analysis of P-Rex proteins.
  • Review of existing literature on P-Rex regulation.
  • Inference of cancer-associated mutation effects based on structural data.

Main Results:

  • P-Rex1 autoinhibition and activation by PI(3,4,5)P3 and Gβγ are structurally characterized.
  • Phosphorylation and P-Rex2-PTEN complex formation add layers of P-Rex regulation.
  • Cancer-associated P-Rex2 mutations likely destabilize autoinhibition and evade PTEN inhibition, increasing GEF activity.

Conclusions:

  • Understanding P-Rex structure and regulation is key to deciphering its role in cellular processes.
  • Dysregulated P-Rex activity, particularly P-Rex2, contributes to cancer metastasis.
  • Further research is needed to fully elucidate P-Rex phosphorylation and P-Rex2-PTEN complex mechanisms.