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

Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

2.7K
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...
2.7K
The Unfolded Protein Response01:37

The Unfolded Protein Response

5.3K
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...
5.3K
Role of ER in the Secretory Pathway01:17

Role of ER in the Secretory Pathway

6.0K
Eukaryotic cells have a special pathway that enables communication between various intracellular membrane-bound compartments and also with the extracellular environment. This pathway is termed as the secretory pathway.
Components of the secretory pathway
About a third of proteins synthesized in the cell are sorted via the secretory route. They shuffle between different compartments in membrane-bound vesicles until they reach their final destination. The main intracellular compartments involved...
6.0K
Stringent Response in E. coli01:23

Stringent Response in E. coli

79
Bacterial growth is closely tied to nutrient availability, with cells proliferating exponentially under favorable conditions and entering a stationary phase when resources become scarce. This transition is mediated by a regulatory mechanism known as the stringent response, which allows bacteria to adapt to nutrient deprivation by modulating gene expression and metabolic activity.During nutrient scarcity, intracellular amino acid levels decline. It results in the accumulation of uncharged tRNAs...
79
Other Stress Responses in Bacteria01:30

Other Stress Responses in Bacteria

105
Bacteria have global regulatory systems that control several types of stress mechanisms. These include Pho regulon and the heat shock response, which are essential systems for environmental adaptation, such as nutrient limitation and proteotoxic stress. The Pho regulon and the heat shock response exemplify bacterial resilience, enabling rapid adaptation to fluctuating environmental conditions.Pho RegulonBacteria require phosphorus for essential cellular processes, including nucleic acid...
105
Post-translational Translocation of Proteins to the RER01:27

Post-translational Translocation of Proteins to the RER

6.2K
A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...
6.2K

You might also read

Related Articles

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

Sort by
Same author

Selective Oxidation of Benzyl Alcohol in Water With Cobalt-Exchanged Zeolite-NaY Catalyst.

ChemPlusChem·2026
Same author

<b>The rarely encountered jewel beetle, <i>Buprestis splendens</i> Fabricius, 1775: First Korean record of the subgenus <i>Cypriacis</i> (Coleoptera: Buprestidae) with molecular insights</b>.

Zootaxa·2026
Same author

E2T: EEG-to-Trajectory Transformer for Motor Imagery-Based Fully-DoF Motion Prediction.

IEEE transactions on neural systems and rehabilitation engineering : a publication of the IEEE Engineering in Medicine and Biology Society·2026
Same author

Body mass index levels and changes before and after dementia diagnosis and risk of all-cause mortality: a nationwide cohort study.

Alzheimer's research & therapy·2026
Same author

N<sup>6</sup>-adenosine methylation enhances nuclear mRNA export through METTL3 and NUP93.

Nature cell biology·2026
Same author

Vitamin D-Mediated Immunoregulation in Degenerative Diseases: Insights into Cardiovascular, Neurodegenerative and Musculoskeletal Disorders.

Nutrients·2026

Related Experiment Video

Updated: Oct 12, 2025

Author Spotlight: Exploring the Role of Unfolded Protein Response in HIV-1 Replication and Infectivity
10:12

Author Spotlight: Exploring the Role of Unfolded Protein Response in HIV-1 Replication and Infectivity

Published on: June 14, 2024

2.2K

Endoplasmic reticulum stress increases LECT2 expression via ATF4.

Chan Yoon Park1, Seul Ki Lee2, Jimin Kim2

  • 1Department of Physiology, University of Ulsan College of Medicine, Seoul, South Korea; Department of Food & Nutrition, College of Health Science, The University of Suwon, Hwaseong-si, Gyeonggi-do, South Korea.

Biochemical and Biophysical Research Communications
|November 22, 2021
PubMed
Summary

Endoplasmic reticulum (ER) stress increases leukocyte cell-derived chemotaxin-2 (LECT2) in non-alcoholic fatty liver disease. Activating transcription factor 4 (ATF4) mediates this upregulation, linking ER stress to LECT2 in liver disease.

Keywords:
ATF4ER stressHepatokineLECT2NAFLDObesity

More Related Videos

Measurements of Physiological Stress Responses in C. Elegans
10:36

Measurements of Physiological Stress Responses in C. Elegans

Published on: May 21, 2020

14.3K
Author Spotlight: Polysome Profiling Protocol for Studying Translational Regulation in Arabidopsis Under Heat Stress
08:39

Author Spotlight: Polysome Profiling Protocol for Studying Translational Regulation in Arabidopsis Under Heat Stress

Published on: October 11, 2024

1.8K

Related Experiment Videos

Last Updated: Oct 12, 2025

Author Spotlight: Exploring the Role of Unfolded Protein Response in HIV-1 Replication and Infectivity
10:12

Author Spotlight: Exploring the Role of Unfolded Protein Response in HIV-1 Replication and Infectivity

Published on: June 14, 2024

2.2K
Measurements of Physiological Stress Responses in C. Elegans
10:36

Measurements of Physiological Stress Responses in C. Elegans

Published on: May 21, 2020

14.3K
Author Spotlight: Polysome Profiling Protocol for Studying Translational Regulation in Arabidopsis Under Heat Stress
08:39

Author Spotlight: Polysome Profiling Protocol for Studying Translational Regulation in Arabidopsis Under Heat Stress

Published on: October 11, 2024

1.8K

Area of Science:

  • Hepatology
  • Molecular Biology
  • Cellular Stress Response

Background:

  • Non-alcoholic fatty liver disease (NAFLD) is linked to obesity, insulin resistance, and endoplasmic reticulum (ER) stress.
  • Elevated circulating leukocyte cell-derived chemotaxin-2 (LECT2) is observed in NAFLD, but the underlying mechanism remains unclear.

Purpose of the Study:

  • To investigate the relationship between ER stress/unfolded protein response (UPR) signaling and LECT2 secretion in NAFLD.
  • To elucidate the role of activating transcription factor 4 (ATF4) in ER stress-induced LECT2 expression.

Main Methods:

  • Utilized HepG2 cells treated with ER stress inducers and chemical chaperones.
  • Performed gene knockdown and overexpression of UPR pathway proteins.
  • Conducted ChIP assays to assess ATF4 binding to the LECT2 promoter.
  • Measured hepatic LECT2 and ATF4 expression in diet-induced obese mice.

Main Results:

  • ER stressors increased LECT2 expression in HepG2 cells, an effect mitigated by a chemical chaperone.
  • Knockdown of ATF4 suppressed ER stress-induced LECT2, while ATF4 overexpression enhanced it.
  • ATF4 was found to bind to the LECT2 promoter, with binding enhanced by ER stress.
  • Concomitant elevation of LECT2 and ATF4 expression was observed in the steatotic livers of obese mice.

Conclusions:

  • Activation of ER stress/UPR signaling induces LECT2 expression in steatotic liver.
  • ATF4 plays a crucial role in mediating the transcriptional upregulation of LECT2 in response to ER stress.