Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

3.7K
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...
3.7K
ER Retrieval Pathway01:45

ER Retrieval Pathway

3.9K
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...
3.9K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

3.2K
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
3.2K
Mitochondrial Protein Sorting01:39

Mitochondrial Protein Sorting

4.4K
Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death.  Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
4.4K
Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

2.6K
Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial...
2.6K
ABC Transporters: Exporter01:31

ABC Transporters: Exporter

4.5K
ATP-binding cassette or ABC transporter is the largest superfamily of integral membrane proteins. The transporters have transmembrane-binding domains (TMDs) and nucleotide-binding domains (NBDs). The TMDs are specific to their substrates, whereas the NBDs are similar to engines that complete ATP hydrolysis to complete the substrate transport. They can be full transporters consisting of two TMDs and NBDs, half transporters with one TMD and NBD, while some encoded with a single TMD or NBD are...
4.5K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Consensus on Behavioral Strategies for Adults with Obesity from the Korean Society for the Study of Obesity.

Journal of obesity & metabolic syndrome·2026
Same author

Systematic review of clinical evidence for Kneipp medicine.

Wiener klinische Wochenschrift·2026
Same author

Authoritarian attitudes and the perceived scientific legitimacy of anthroposophic medicine: A survey of attitudes on complementary and alternative medicine in Austria.

PloS one·2026
Same author

A multidimensional eye-tracking assessment for estimating cognitive profiles in intellectual disability: A preliminary deep learning study.

Digital health·2026
Same author

Correction to "Next-Generation MDMA Analogue SDMA: Pharmacological and Metabolic Insights".

ACS chemical neuroscience·2026
Same author

People are approaching me: biased ensemble perception of biological motion in social anxiety.

Cognition & emotion·2026

Related Experiment Video

Updated: Aug 15, 2025

Purification of the Cystic Fibrosis Transmembrane Conductance Regulator Protein Expressed in Saccharomyces cerevisiae
15:12

Purification of the Cystic Fibrosis Transmembrane Conductance Regulator Protein Expressed in Saccharomyces cerevisiae

Published on: May 10, 2014

14.6K

Rescue of Misfolded Organic Cation Transporter 3 Variants.

Thomas J F Angenoorth1, Julian Maier1, Stevan Stankovic1

  • 1Institute of Pharmacology, Center for Physiology and Pharmacology, Medical University of Vienna, Währingerstraße 13A, 1090 Vienna, Austria.

Cells
|January 8, 2023
PubMed
Summary
This summary is machine-generated.

Chemical chaperones can restore function to misfolded organic cation transporter 3 (OCT3, SLC22A3) variants. Treatment with 4-phenylbutyric acid (4-PBA) increased membrane expression and transport capacity of OCT3 mutations.

Keywords:
17-DMAG4-PBAchemical chaperonecorticosteronepharmacochaperoningprogesteroneµ-pifithrin

More Related Videos

Functional Reconstitution and Channel Activity Measurements of Purified Wildtype and Mutant CFTR Protein
09:59

Functional Reconstitution and Channel Activity Measurements of Purified Wildtype and Mutant CFTR Protein

Published on: March 9, 2015

12.3K
Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
08:59

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

Published on: February 12, 2019

11.3K

Related Experiment Videos

Last Updated: Aug 15, 2025

Purification of the Cystic Fibrosis Transmembrane Conductance Regulator Protein Expressed in Saccharomyces cerevisiae
15:12

Purification of the Cystic Fibrosis Transmembrane Conductance Regulator Protein Expressed in Saccharomyces cerevisiae

Published on: May 10, 2014

14.6K
Functional Reconstitution and Channel Activity Measurements of Purified Wildtype and Mutant CFTR Protein
09:59

Functional Reconstitution and Channel Activity Measurements of Purified Wildtype and Mutant CFTR Protein

Published on: March 9, 2015

12.3K
Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
08:59

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase

Published on: February 12, 2019

11.3K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Pharmacology

Background:

  • Organic cation transporters (OCTs) like OCT3 (SLC22A3) are crucial for cellular uptake of various substances.
  • Novel mutations in OCT3 can lead to misfolding, ER retention, and impaired transport function.
  • Pharmacological chaperones have shown potential in restoring function to misfolded transporter variants in other families.

Purpose of the Study:

  • To investigate the effect of chemical chaperones on two ER-bound, misfolded OCT3 variants (D340G and R348W).
  • To determine if chaperone treatment can restore membrane expression and transport capacity of these OCT3 variants.

Main Methods:

  • Confocal and biochemical analyses were used to assess transporter expression.
  • Radiotracer uptake assays were performed to measure transporter function.
  • Cells expressing OCT3 variants were treated with the chemical chaperone 4-phenylbutyric acid (4-PBA).

Main Results:

  • 4-PBA treatment increased the membrane expression of both D340G and R348W OCT3 variants.
  • Transport capacity was significantly enhanced: 8-fold for D340G and 1.5-fold for R348W.
  • These results demonstrate a rescue effect of 4-PBA on folding-deficient OCT3 variants.

Conclusions:

  • Chemical chaperones, specifically 4-PBA, can partially restore function to misfolded OCT3 variants.
  • This study provides proof of principle for chaperone-mediated rescue of folding-deficient SLC22 transporters.
  • Further investigation is warranted to extend these findings to other SLC22 members associated with diseases.