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

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.
Protein Modifications in the RER01:26

Protein Modifications in the RER

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 sequences.
Protein Import into the Peroxisomes01:27

Protein Import into the Peroxisomes

Cells contain membrane-bound organelles called peroxisomes that oxidize organic molecules by transferring hydrogen atoms to oxygen, producing hydrogen peroxide. Peroxisomes enzymatically convert the released hydrogen peroxide into water and oxygen.
Peroxisomal Protein Import:
Peroxisomes lack the genetic machinery required to code for their own proteins. Hence, most peroxisomal membrane, lumenal and transmembrane proteins are synthesized in the cytoplasm or ER and transported to the peroxisome...
The Proteasome01:13

The Proteasome

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 (ubiquitin...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst 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. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...

You might also read

Related Articles

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

Sort by
Same author

Topical eye treatment with JGRi1, a protein/protein interaction inhibitor, mitigates retinal degeneration.

Cell death & disease·2026
Same author

Oxidative Stress Signaling and Regenerative Responses in a Larval Zebrafish Model of Retinal Light Damage.

Antioxidants (Basel, Switzerland)·2026
Same author

Chronic fasudil treatment induces benzodiazepine-like tolerance via modulation of GABA-A receptor γ2 subunit expression and impairs contextual fear memory in mice.

Pharmacological reports : PR·2026
Same author

Retraction Notice to "The Protective Effect of Superoxide Dismutase Mimetic M40401 on Balloon Injury-Related Neointima Formation: Role of the Lectin-Like Oxidized Low-Density Lipoprotein Receptor-1" J Pharmacol Exp Ther 311 (2004) 44-50.

The Journal of pharmacology and experimental therapeutics·2026
Same author

Hormetic Effects of Curcumin in RPE Cells: SIRT1 and Caspase-3 Inactivation with Implications for AMD.

International journal of molecular sciences·2025
Same author

Agenzia Italiana del Farmaco (AIFA): Developments and Strategy in a Transitioning European HTA Landscape.

Journal of market access & health policy·2025

Related Experiment Video

Updated: May 7, 2026

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
10:24

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

SUMO: a (oxidative) stressed protein.

Marco Feligioni1, Robert Nisticò

  • 1Laboratory of Pharmacology of Synaptic Plasticity, EBRI "Rita Levi-Montalcini" Foundation, Via del Fosso di Fiorano 64/65, 00143, Rome, Italy, m.feligioni@ebri.it.

Neuromolecular Medicine
|September 21, 2013
PubMed
Summary
This summary is machine-generated.

Oxidative stress impacts cellular redox homeostasis, altering protein SUMOylation. This study highlights SUMOylation

More Related Videos

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
07:16

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Published on: June 21, 2021

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity
09:45

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity

Published on: January 29, 2018

Related Experiment Videos

Last Updated: May 7, 2026

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
10:24

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
07:16

Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation

Published on: June 21, 2021

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity
09:45

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity

Published on: January 29, 2018

Area of Science:

  • Biochemistry
  • Cellular Biology
  • Pathology

Background:

  • Cellular metabolism generates redox species, crucial in normal physiology and pathological states like neurodegenerative diseases.
  • Imbalances in redox homeostasis trigger molecular changes, notably posttranslational protein modifications (PTMs).
  • Protein SUMOylation is a key PTM sensitive to oxidative stress and redox species levels.

Purpose of the Study:

  • To review updated evidence on the role of SUMOylation in various pathological conditions.
  • To elucidate the involvement of c-Jun N-terminal kinase (JNK) and the small ubiquitin modifier (SUMO) pathway crosstalk.
  • To underscore SUMOylation as a critical regulator under oxidative stress.

Main Methods:

  • Literature review of studies investigating SUMOylation and oxidative stress.
  • Analysis of molecular mechanisms linking redox homeostasis and PTMs.
  • Examination of the interplay between JNK signaling and SUMOylation pathways.

Main Results:

  • SUMOylation efficiency is modulated by oxidative species in a dose- and time-dependent manner.
  • SUMOylation plays a significant role in protein regulation (activation, localization, aggregation, expression) during cellular stress.
  • Evidence confirms SUMOylation's involvement in multiple pathological conditions.

Conclusions:

  • SUMOylation acts as a sensitive indicator of cellular redox state.
  • The crosstalk between JNK and SUMOylation pathways is critical in redox-related pathologies.
  • Understanding SUMOylation dynamics offers insights into disease mechanisms and potential therapeutic targets.