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Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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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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ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
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The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
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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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Multiprotein signaling complexes are formed in a dynamic process involving protein-protein interactions at the cytoplasmic domain of transmembrane receptors or enzymatic and non-enzymatic proteins associated with the receptor. These complexes ensure the activation and propagation of intracellular signals that regulate cell functions.
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Related Experiment Video

Updated: Aug 30, 2025

Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes
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Emerging roles for G-quadruplexes in proteostasis.

Bryan B Guzman1, Ahyun Son2, Theodore J Litberg2

  • 1Department of Pharmacology, University of North Carolina at Chapel Hill, NC, USA.

The FEBS Journal
|August 26, 2022
PubMed
Summary

G-quadruplexes, unique nucleic acid structures, significantly impact protein folding, aggregation, and misfolding. This review explores their role in protein homeostasis and disease, highlighting key research questions.

Keywords:
ALSAlzheimeraggregationchaperonefragile Xproteostasisquadruplex

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Understanding nucleic acid-protein interactions is crucial for comprehending cellular processes.
  • G-quadruplexes, specific DNA and RNA structures, are increasingly recognized for their biological significance.
  • Dysregulation of protein homeostasis is linked to various diseases.

Purpose of the Study:

  • To review recent findings on G-quadruplexes' influence on protein aggregation and misfolding.
  • To examine the role of G-quadruplexes in protein homeostasis and disease pathogenesis.
  • To identify current knowledge gaps and future research directions in this field.

Main Methods:

  • Literature review of recent scientific reports and studies.
  • Analysis of experimental data on G-quadruplex-protein interactions.
  • Synthesis of information on G-quadruplexes' effects on protein folding, aggregation, and phase separation.

Main Results:

  • G-quadruplexes modulate protein aggregation, proteolysis, and phase separation.
  • These structures are implicated in the development of protein misfolding diseases.
  • Evidence suggests a critical role for G-quadruplexes in maintaining protein homeostasis.

Conclusions:

  • G-quadruplexes are key players in protein homeostasis and disease.
  • Further research is needed to fully elucidate the mechanisms of G-quadruplex-protein interactions.
  • Targeting G-quadruplexes may offer therapeutic strategies for protein misfolding diseases.