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

8.4K
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....
8.4K
Phosphorylation01:02

Phosphorylation

53.3K
The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
53.3K
Protein Modifications in the RER01:26

Protein Modifications in the RER

6.5K
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...
6.5K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

14.5K
Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
14.5K
Amino acids03:42

Amino acids

102.7K
Amino acids are the monomers that comprise proteins. Each amino acid has the same fundamental structure, which consists of a central carbon atom, or the alpha (α) carbon, bonded to an amino group (NH2), a carboxyl group (COOH), and to a hydrogen atom. Every amino acid also has another atom or group of atoms bonded to the central atom known as the R group. There are 20 common amino acids present in proteins, each with a different R group. Variation in the amino acid sequence is responsible for...
102.7K
Phase II Reactions: Acetylation Reactions01:24

Phase II Reactions: Acetylation Reactions

617
Acetylation, a phase II biotransformation reaction, introduces an acetyl group to drugs or their metabolites. Acetyltransferase enzymes facilitate this reaction, which resembles α-amino acid conjugation due to the addition of a functional group to the drug molecule.
The substrates for acetylation are typically drugs or their metabolites with an amino, sulfonamide, or hydrazine functional group. Acetylation can occur at several points in the drug molecule, including primary, secondary, and...
617

You might also read

Related Articles

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

Sort by
Same author

Fibroblastic aspartoacylase suppresses TGFβ-mediated responses and cancer progression.

Nature communications·2026
Same author

UBB as an early-stage potential biomarker for breast cancer via modulation of the ubiquitination pathway.

Scientific reports·2026
Same author

Epidermal deletion of Kindlin-1 drives matrix changes in the mouse skin and altered responses to ultraviolet radiation.

Journal of dermatological science·2026
Same author

Bacterial metataxonomic analysis of the Algerian traditional dried-salted meat 'El Kaddid' and characterization of its lactic acid bacteria.

Antonie van Leeuwenhoek·2026
Same author

<i>Staphylococcus caseorum</i> sp. nov., a new species isolated from Spanish traditional, blue-veined Cabrales cheese.

International journal of systematic and evolutionary microbiology·2026
Same author

Tissue-specific fibroblast lipid cues impose the rate of epithelial cancer invasion.

Nature metabolism·2026

Related Experiment Video

Updated: Dec 12, 2025

LERLIC-MS/MS for In-depth Characterization and Quantification of Glutamine and Asparagine Deamidation in Shotgun Proteomics
08:01

LERLIC-MS/MS for In-depth Characterization and Quantification of Glutamine and Asparagine Deamidation in Shotgun Proteomics

Published on: April 9, 2017

8.4K

Asparagine Hydroxylation is a Reversible Post-translational Modification.

Javier Rodriguez1, Cameron D Haydinger2, Daniel J Peet2

  • 1Cancer Research UK Edinburgh Centre, University of Edinburgh, Edinburgh, UK; Systems Biology Ireland, University College Dublin, Dublin, Ireland.

Molecular & Cellular Proteomics : MCP
|August 8, 2020
PubMed
Summary

Cellular machinery can reverse asparagine hydroxylation, a previously irreversible protein modification. This finding reveals dynamic regulation of protein function, challenging existing biological dogma.

Keywords:
Post-translational modificationsSILACaffinity proteomicsfactor-inhibiting-HIFhydroxylationmass spectrometrysignal transduction

More Related Videos

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

7.2K
A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
11:08

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

Published on: December 9, 2017

7.3K

Related Experiment Videos

Last Updated: Dec 12, 2025

LERLIC-MS/MS for In-depth Characterization and Quantification of Glutamine and Asparagine Deamidation in Shotgun Proteomics
08:01

LERLIC-MS/MS for In-depth Characterization and Quantification of Glutamine and Asparagine Deamidation in Shotgun Proteomics

Published on: April 9, 2017

8.4K
Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

7.2K
A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli
11:08

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

Published on: December 9, 2017

7.3K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Post-Translational Modifications

Background:

  • Amino acid hydroxylation is a crucial post-translational modification regulating protein function.
  • Currently, hydroxylation is considered irreversible, requiring protein degradation and resynthesis for modification reversal.

Purpose of the Study:

  • To investigate the reversibility of Factor Inhibiting Hypoxia-inducible factor (FIH)-mediated asparagine hydroxylation.
  • To determine if cellular machinery can reverse asparagine hydroxylation on intact proteins.

Main Methods:

  • Experimental investigation of FIH-mediated asparagine hydroxylation.
  • Analysis of protein modification reversal in cellular systems.

Main Results:

  • Evidence presented for the reversal of FIH-mediated asparagine hydroxylation on intact proteins.
  • Demonstration of cellular machinery's capability to reverse this specific post-translational modification.

Conclusions:

  • Asparagine hydroxylation is a dynamic and flexible post-translational modification.
  • This reversibility positions asparagine hydroxylation alongside other key regulatory modifications like phosphorylation and methylation.