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

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...
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...
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...
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.
Drug Metabolism: Phase II Reactions01:14

Drug Metabolism: Phase II Reactions

Phase II reactions are essential for the detoxification and elimination of drugs from the body. These reactions involve the conjugation of parent drugs or their phase I metabolites with endogenous molecules, resulting in more hydrophilic drug conjugates. The primary conjugation reactions in this phase are sulfation and glucuronidation. Both sulfation and glucuronidation typically produce biologically inactive metabolites. However, in some cases involving prodrugs, active metabolites may be...
Phase II Reactions: Sulfation and Conjugation with α-Amino Acids01:19

Phase II Reactions: Sulfation and Conjugation with α-Amino Acids

Sulfation and α-amino acid conjugation are two critical biotransformation reactions in drug metabolism. Sulfation, a phase II biotransformation reaction, involves adding a polar sulfate group to a drug, enhancing its water solubility and promoting excretion. This process can either co-occur with or occur independently of glucuronidation. Nonmicrosomal sulfotransferase enzymes catalyze the process. The reaction involves 3'-phosphoadenosine-5'-phosphosulfate or PAPS coenzyme activation, sulfur...

You might also read

Related Articles

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

Sort by
Same author

Engineering Cathepsin S Selective Chemical Probes and Antibody-Drug Conjugates through Substrate Profiling with Unnatural Amino Acids.

Journal of medicinal chemistry·2026
Same author

Synthesis and Characterization of ULK1/2 Kinase Inhibitors That Inhibit Autophagy and Upregulate Expression of Major Histocompatibility Complex I for the Treatment of Non-Small Cell Lung Cancer.

ACS chemical biology·2026
Same author

TOF-probe-based mass cytometry reveals individual protease activity as an important driver of immune cell differentiation and function.

Cell reports·2026
Same author

Identification and Exploration of a Series of SARS-Cov‑2 M<sup>Pro</sup> Cyano-Based Inhibitors Revealing Ortho-Substitution Effects within the P3 Biphenyl Group.

ACS medicinal chemistry letters·2025
Same author

A Robust Fluorogenic Substrate for Chikungunya Virus Protease (nsP2) Activity.

bioRxiv : the preprint server for biology·2025
Same author

Engineering unnatural amino acids in peptide linkers enables cathepsin-selective antibody-drug conjugates for HER2-positive breast cancer.

Journal of controlled release : official journal of the Controlled Release Society·2025
Same journal

ALKBH4 Promotes Osteogenesis via Epigenetic Regulation of BMP2-Wnt/β-Catenin Signaling in Cervical Spine OPLL.

IUBMB life·2026
Same journal

Single-Sequence Deep Learning Delivers Crystal-Quality Models of Covalent K-Ras G12 Hotspot Complexes.

IUBMB life·2026
Same journal

Mechanism of PCSK9-Mediated Macrophage Activation via the CAP1/NF-κB Pathway in CAWS-Induced Kawasaki Disease Vasculitis.

IUBMB life·2026
Same journal

Hormesis and the Golden Ratio: Toward a Universal Estimator of Adaptive Capacity.

IUBMB life·2026
Same journal

MicroRNAs in HPV-Associated Carcinogenesis: Potential Biomarkers in Oropharyngeal and Cervical Cancers.

IUBMB life·2026
Same journal

PGAM1 Orchestrates Cell Cycle Progression, Glycolytic Reprogramming, and Immunosuppressive Microenvironment in Triple-Negative Breast Cancer.

IUBMB life·2026
See all related articles

Related Experiment Video

Updated: Jul 3, 2026

Quantitative FRET (F&#246;rster 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

DeSUMOylating enzymes--SENPs.

Marcin Drag1, Guy S Salvesen

  • 1Program in Apoptosis and Cell Death Research, Burnham Institute for Medical Research, La Jolla, CA 92037, USA. mdrag@burnham.org

IUBMB Life
|July 31, 2008
PubMed
Summary
This summary is machine-generated.

Protein modification by small ubiquitin-like modifiers (SUMO) is reversible. Sentrin-specific proteases (SENPs) remove SUMO from substrates and process immature SUMO forms, playing crucial roles in cellular regulation.

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

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: Jul 3, 2026

Quantitative FRET (F&#246;rster 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

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

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
  • Molecular Biology
  • Cellular Regulation

Background:

  • Protein modification by ubiquitin and SUMO (small ubiquitin-like modifiers) is a dynamic and reversible process.
  • Deubiquitinating enzymes remove ubiquitin, while proteases called sentrin-specific proteases (SENPs) remove SUMO from substrates.
  • SENPs possess both isopeptidase activity (removing SUMO) and endopeptidase activity (processing immature SUMO).

Purpose of the Study:

  • To review recent advancements in understanding human SENPs.
  • To elucidate the diverse roles and substrates of human SENPs.
  • To highlight the conserved characteristics of the SENP family.

Main Methods:

  • Review of recent scientific literature on human SENPs.
  • Analysis of SENP family characteristics, including conserved catalytic mechanisms and scaffold.
  • Examination of SENP activity on SUMO and Nedd8 conjugated proteins and precursors.

Main Results:

  • SENPs are crucial proteases involved in SUMO removal and maturation.
  • Human SENPs share conserved features, including membership in peptidase Clan CE.
  • SENPs act on both SUMO and Nedd8 pathways, affecting protein conjugation.

Conclusions:

  • SENPs are essential regulators of SUMOylation and related pathways.
  • Understanding human SENPs is key to comprehending cellular signaling and protein homeostasis.
  • Further research on SENPs and their substrates will reveal deeper insights into biological processes.