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Related Concept Videos

Directing Proteins to the Rough Endoplasmic Reticulum01:34

Directing Proteins to the Rough Endoplasmic Reticulum

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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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GPI Anchoring of Proteins in the ER Membrane01:29

GPI Anchoring of Proteins in the ER Membrane

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GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...
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Protein Modifications in the RER01:26

Protein Modifications in the RER

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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.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...
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Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

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After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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Tail-anchoring of Proteins in the ER Membrane01:45

Tail-anchoring of Proteins in the ER Membrane

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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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ER Retrieval Pathway01:45

ER Retrieval Pathway

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In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
The ER uses many checkpoints to prevent the entry of incorrectly folded or a resident protein as cargo onto a transport vesicle. These mechanisms...
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Related Experiment Video

Updated: Sep 29, 2025

Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells
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Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells

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γ-Resorcyclic Acid-Based AIEgens for Illuminating Endoplasmic Reticulum.

Jaypalsing Ingle1, Hiren Dedaniya1, Chaithra Mayya2

  • 1Discipline of Chemistry, Indian Institute of Technology Gandhinagar, 382355, Palaj, Gujarat, India.

Chemistry (Weinheim an Der Bergstrasse, Germany)
|March 18, 2022
PubMed
Summary

Researchers developed novel γ-resorcyclic acid-based molecules with aggregation-induced emission (AIE) properties. These molecules effectively visualize the endoplasmic reticulum (ER) in cancer and non-cancerous cells, aiding in disease research.

Keywords:
aggregation-induced emissionendoplasmic reticulumhydrazide-hydrazonesintramolecular dual H-bonding

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Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells
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Monitoring Endoplasmic Reticulum Calcium Homeostasis Using a Gaussia Luciferase SERCaMP
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Optimizing the Genetic Incorporation of Chemical Probes into GPCRs for Photo-crosslinking Mapping and Bioorthogonal Chemistry in Live Mammalian Cells
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Visualization of Endoplasmic Reticulum Subdomains in Cultured Cells
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Area of Science:

  • Chemical Biology
  • Cell Biology
  • Biophysical Chemistry

Background:

  • The endoplasmic reticulum (ER) is crucial for numerous biological processes, but its visualization remains challenging.
  • Understanding ER dynamics is vital for studying diseases like cancer.

Purpose of the Study:

  • To design and synthesize novel small molecules for endoplasmic reticulum (ER) visualization.
  • To investigate the aggregation-induced emission (AIE) properties of these molecules for cellular imaging.

Main Methods:

  • Synthesis of γ-resorcyclic acid-based small molecules.
  • Characterization of aggregation-induced emission (AIE) properties in aqueous media.
  • pH- and temperature-dependent fluorescence quenching studies.
  • Scanning electron microscopy for aggregation analysis.
  • Live-cell imaging in HeLa cervical cancer and RPE-1 human retinal epithelial cells.

Main Results:

  • Novel γ-resorcyclic acid-based molecules exhibited significant aggregation-induced emission (AIE) in water.
  • AIE properties were attributed to dual intramolecular hydrogen bonding and 2D self-assembly.
  • Successful sub-cellular visualization of the endoplasmic reticulum (ER) in both cancer and non-cancerous human cell lines within one hour.
  • pH and temperature studies confirmed the fluorescence quenching mechanism and aggregation behavior.

Conclusions:

  • Developed novel AIEgens based on γ-resorcyclic acid for ER imaging.
  • These molecules offer a promising tool for studying ER chemical biology, particularly in disease states.
  • Rapid and efficient ER illumination in live cells opens new avenues for biological research.