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Related Concept Videos

Protein Translocation Machinery on the ER Membrane01:28

Protein Translocation Machinery on the ER Membrane

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The translocon complex situated on the ER membrane is the main gateway for the protein secretory pathway. It facilitates the transport of nascent peptides into the ER lumen and their insertion into the ER membrane.
Sec61 protein conducting channel
In eukaryotes, the translocon complex comprises a core heterotrimeric translocator channel called the Sec61 complex. This channel includes three transmembrane proteins, Sec61α, Sec61β, and Sec61γ, and is the largest subunit of the...
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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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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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The Endoplasmic Reticulum01:43

The Endoplasmic Reticulum

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The endoplasmic reticulum or ER makes up for more than half of the membranes in a cell and accounts for 10% of total cell volume. It is also the primary protein and lipid synthesis factory for most cell organelles, such as the Golgi apparatus, lysosomes, secretory vesicles, and the plasma membrane. Despite being the most extensive and functionally complex subcellular organelle, ER was the last to be discovered. After years of deliberation, Keith Porter and George Palade in the year 1954,...
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Assembly of the Lipid Bilayer in the ER01:28

Assembly of the Lipid Bilayer in the ER

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Biological membranes are more than just a barrier separating cell cytoplasm from the outside environment. They are highly dynamic and help maintain the integrity and physiological stability of the cells as well as membrane-bound organelles. Membranes also play vital roles in cell-to-cell and intracellular communication.
A large chunk of any biological membrane is composed of phospholipids. These lipids have a heterogeneous distribution across different subcellular organelles and even between...
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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.
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Related Experiment Video

Updated: May 22, 2025

Direct Imaging of ER Calcium with Targeted-Esterase Induced Dye Loading TED
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Direct Imaging of ER Calcium with Targeted-Esterase Induced Dye Loading TED

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Molecules Targeting EriCF1 Increase Streptococcus mutans Fluoride Sensitivity.

Q Weng1,2, J Liu1,2, S Yao2

  • 1Department of Preventive Dentistry, Shanghai Stomatological Hospital & School of Stomatology, Fudan University, Shanghai, China.

Journal of Dental Research
|March 13, 2025
PubMed
Summary
This summary is machine-generated.

New compounds targeting fluoride exporters in Streptococcus mutans enhance fluoride

Keywords:
antimicrobials/antimicrobial resistancebacteriabacterial virulencecariesmicrobiologypreventive dentistry

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Last Updated: May 22, 2025

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Area of Science:

  • Microbiology
  • Biochemistry
  • Dental Research

Background:

  • Dental caries is a major global oral health issue.
  • Fluoride prevents caries but is insufficient against Streptococcus mutans.
  • Streptococcus mutans has a fluoride detoxification mechanism involving exporters.

Purpose of the Study:

  • Identify the functional fluoride exporter in Streptococcus mutans.
  • Develop novel compounds to enhance fluoride's antibacterial efficacy.
  • Investigate new therapeutic strategies for dental caries prevention.

Main Methods:

  • Constructed gene deletion, overexpression, and complemented strains of S. mutans UA159.
  • Assessed fluoride sensitivity, intracellular fluoride levels, and cell membrane permeability.
  • Used molecular docking to identify diphenylurea derivatives targeting the fluoride exporter.
  • Performed chequerboard broth microdilution assays and in vivo studies.

Main Results:

  • EriC^F1 identified as the major functional fluoride exporter in S. mutans.
  • Three diphenylurea derivatives synergistically enhanced sodium fluoride's antibacterial effect by impeding fluoride efflux.
  • Compounds 9 and 15 combined with sodium fluoride significantly reduced S. mutans cariogenicity in vivo with good biocompatibility.

Conclusions:

  • Fluoride exporters in S. mutans are potential targets for caries prevention.
  • Diphenylurea derivatives targeting EriC^F1 offer a promising therapeutic approach when combined with fluoride.
  • This strategy provides novel measures for effective dental caries prevention.