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

2.6K
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...
2.6K
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

4.0K
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...
4.0K
The Unfolded Protein Response01:37

The Unfolded Protein Response

5.2K
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...
5.2K
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

4.0K
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...
4.0K
Protein Modifications in the RER01:26

Protein Modifications in the RER

5.7K
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...
5.7K
The Proteasome01:13

The Proteasome

1.2K
Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
1.2K

You might also read

Related Articles

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

Sort by
Same author

Coumarins link iron deficiency to TOR inhibition in plants.

Current biology : CB·2026
Same author

Nanoscale regulation of ROS signaling at the plasma membrane tunes the plant response to osmotic stress.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Mechanisms controlling the plasma membrane targeting and the nanodomain organization of the plant SPFH protein HIR2.

The Plant journal : for cell and molecular biology·2026
Same author

Two anchoring proteins control daughter apical complex assembly in <i>Toxoplasma gondii</i>.

bioRxiv : the preprint server for biology·2026
Same author

The CELL NUMBER REGULATOR SlFWL5 protein regulates aerial vegetative growth in tomato, by promoting cell expansion.

Journal of experimental botany·2025
Same author

AtSnRK2.4 Functions as an ABA-Responsive Protein Kinase in Arabidopsis.

Physiologia plantarum·2025

Related Experiment Video

Updated: Oct 2, 2025

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

Root Membrane Ubiquitinome under Short-Term Osmotic Stress.

Nathalie Berger1, Vincent Demolombe1, Sonia Hem1

  • 1BPMP, CNRS, INRAE, Institut Agro, University Montpellier, 34060 Montpellier, France.

International Journal of Molecular Sciences
|February 26, 2022
PubMed
Summary

Plant survival under osmotic stress depends on proteomic plasticity. This study identifies 719 ubiquitinated lysine residues in root membrane proteins, revealing ubiquitination

Keywords:
aquaporinmass spectrometryosmotic stressubiquitination

More Related Videos

Translating Ribosome Affinity Purification TRAP to Investigate Arabidopsis thaliana Root Development at a Cell Type-Specific Scale
09:41

Translating Ribosome Affinity Purification TRAP to Investigate Arabidopsis thaliana Root Development at a Cell Type-Specific Scale

Published on: May 14, 2020

12.3K
Phosphoproteomic Strategy for Profiling Osmotic Stress Signaling in Arabidopsis
05:47

Phosphoproteomic Strategy for Profiling Osmotic Stress Signaling in Arabidopsis

Published on: June 25, 2020

5.3K

Related Experiment Videos

Last Updated: Oct 2, 2025

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
Translating Ribosome Affinity Purification TRAP to Investigate Arabidopsis thaliana Root Development at a Cell Type-Specific Scale
09:41

Translating Ribosome Affinity Purification TRAP to Investigate Arabidopsis thaliana Root Development at a Cell Type-Specific Scale

Published on: May 14, 2020

12.3K
Phosphoproteomic Strategy for Profiling Osmotic Stress Signaling in Arabidopsis
05:47

Phosphoproteomic Strategy for Profiling Osmotic Stress Signaling in Arabidopsis

Published on: June 25, 2020

5.3K

Area of Science:

  • Plant Biology
  • Molecular Biology
  • Proteomics

Background:

  • Osmotic stress significantly impacts plant survival, necessitating proteomic adaptability.
  • Protein ubiquitination is a key post-translational modification regulating plant responses to osmotic stress.

Purpose of the Study:

  • To identify ubiquitinated lysine residues in Arabidopsis root membrane proteins under osmotic stress.
  • To elucidate the role of ubiquitination in membrane protein internalization and sorting during osmotic stress.
  • To investigate the function of E2 ubiquitin-conjugating enzymes (UBC32 and UBC34) in plant osmotic stress response.

Main Methods:

  • K-Ɛ-GG antibody enrichment coupled with high-resolution mass spectrometry.
  • Quantitative proteome and ubiquitinome analysis.
  • In silico analysis of ubiquitinated proteins and enzyme targeting.

Main Results:

  • Identified 719 ubiquitinated lysine (K-Ub) residues on 450 Arabidopsis root membrane proteins.
  • Ubiquitination is primarily involved in cargo protein internalization and sorting, not degradation, during short-term osmotic stress.
  • Acidic residues near K-Ub sites were identified, and UBC32/UBC34 were implicated in targeting membrane proteins under osmotic stress.

Conclusions:

  • Ubiquitination plays a crucial role in the internalization and sorting of root membrane proteins during osmotic stress.
  • UBC32 and UBC34 positively regulate primary root growth under osmotic stress, suggesting their importance in plant stress adaptation.