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

The Proteasome02:18

The Proteasome

7.7K
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...
7.7K
The Proteasome01:13

The Proteasome

1.6K
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...
1.6K
The Proteasome02:18

The Proteasome

3.9K
3.9K
The Proteasome Structure01:17

The Proteasome Structure

2.2K
The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
2.2K
Caspases01:24

Caspases

8.6K
Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside...
8.6K
Protein Import into the Peroxisomes01:27

Protein Import into the Peroxisomes

4.4K
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...
4.4K

You might also read

Related Articles

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

Sort by
Same author

Elementary vectors reveal minimal interactions in microbial communities.

Journal of the Royal Society, Interface·2026
Same author

PML as a neuroprotective guardian: Leveraging nuclear protein quality control to mitigate neurotoxicity of an ALS-associated NEK1 variant.

The FEBS journal·2026
Same author

Decomposable and Essentially Univariate Mass-Action Systems: Extensions of the Deficiency One Theorem.

Journal of nonlinear science·2026
Same author

Novel Netrin-1-Unc5b-Klf4 axis balances AT2 survival in experimental bronchopulmonary dysplasia.

American journal of respiratory cell and molecular biology·2026
Same author

Reprogramming of bacterial virulence by lysine acetylation.

Nature communications·2026
Same author

Urine Proteomics as a Source of Biological Information and Outcome Predictor in Living Kidney Transplantation.

Molecular & cellular proteomics : MCP·2026

Related Experiment Video

Updated: Apr 22, 2026

Quantitative FRET Förster Resonance Energy Transfer Analysis for SENP1 Protease Kinetics Determination
16:02

Quantitative FRET Förster Resonance Energy Transfer Analysis for SENP1 Protease Kinetics Determination

Published on: February 21, 2013

18.0K

SUMO-specific proteases/isopeptidases: SENPs and beyond.

Arnab Nayak, Stefan Müller

    Genome Biology
    |October 16, 2014
    PubMed
    Summary

    SUMO proteases, also known as SUMO isopeptidases, are enzymes crucial for cellular regulation. This review covers their evolution, structure, function, and links to human diseases.

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Cell Biology

    Background:

    • SUMOylation is a vital post-translational modification regulating protein function.
    • SUMO proteases (SUMO isopeptidases) are essential for reversing SUMOylation.
    • Dysregulation of SUMOylation and SUMO proteases is implicated in various pathologies.

    Purpose of the Study:

    • To provide a comprehensive overview of SUMO proteases.
    • To elucidate their evolutionary origins, structural characteristics, and cellular localization.
    • To discuss their diverse biological functions and relevance to human diseases.

    Main Methods:

    • Literature review and synthesis of existing research.
    • Comparative analysis of SUMO protease families across species.

    More Related Videos

    SUMO-Binding Entities SUBEs as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer
    08:29

    SUMO-Binding Entities SUBEs as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer

    Published on: November 1, 2019

    7.5K
    Cell Subtype-specific Analysis of Neuronal Membrane Proteasome in Somatosensory Neurons
    09:27

    Cell Subtype-specific Analysis of Neuronal Membrane Proteasome in Somatosensory Neurons

    Published on: October 10, 2025

    739

    Related Experiment Videos

    Last Updated: Apr 22, 2026

    Quantitative FRET Förster Resonance Energy Transfer Analysis for SENP1 Protease Kinetics Determination
    16:02

    Quantitative FRET Förster Resonance Energy Transfer Analysis for SENP1 Protease Kinetics Determination

    Published on: February 21, 2013

    18.0K
    SUMO-Binding Entities SUBEs as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer
    08:29

    SUMO-Binding Entities SUBEs as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer

    Published on: November 1, 2019

    7.5K
    Cell Subtype-specific Analysis of Neuronal Membrane Proteasome in Somatosensory Neurons
    09:27

    Cell Subtype-specific Analysis of Neuronal Membrane Proteasome in Somatosensory Neurons

    Published on: October 10, 2025

    739
  • Integration of structural, functional, and disease-related data.

    • Main Results:

    • SUMO proteases exhibit diverse evolutionary trajectories and structural folds.
    • They are localized in various subcellular compartments, including the nucleus and cytoplasm.
    • Their functions span gene expression, DNA repair, and signal transduction.

    Conclusions:

    • SUMO proteases play critical roles in maintaining cellular homeostasis.
    • Understanding their biology is key to developing therapeutic strategies for SUMOylation-related diseases.
    • Further research into SUMO protease mechanisms will uncover new biological insights.