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

Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

9.8K
Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
9.8K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

14.4K
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...
14.4K
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

4.1K
4.1K
Phosphorylation01:02

Phosphorylation

53.2K
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...
53.2K
Proteomics01:33

Proteomics

9.0K
A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term...
9.0K

You might also read

Related Articles

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

Sort by
Same author

A Genetically Encoded Fluorescent Sensor for Protein Arginine Phosphorylation.

ACS sensors·2026
Same author

Proteomic Profiling of Oxidative Stress Response Proteins with a Methionine Sulfoxide-Inspired Activity-Based Probe.

JACS Au·2026
Same author

Three-dimensional spatiotemporal analysis for the assessment of retinal capillary perfusion using a clinical OCT system.

Scientific reports·2025
Same author

Intracristal space proteome mapping using super-resolution proximity labeling with isotope-coded probes.

Nature communications·2025
Same author

Polarization-diversity optical coherence tomography analysis of pentosan polysulfate sodium-associated maculopathy.

Canadian journal of ophthalmology. Journal canadien d'ophtalmologie·2025
Same author

Chemoproteomic identification of phosphohistidine acceptors: posttranslational activity regulation of a key glycolytic enzyme.

Chemical science·2025

Related Experiment Video

Updated: Dec 4, 2025

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

5.5K

Quest for the Crypto-phosphoproteome.

Seungmin Ahn1, Hoyoung Jung1, Jung-Min Kee1

  • 1Department of Chemistry, Ulsan National Institute of Science and Technology (UNIST), Ulsan, 44919, Korea.

Chembiochem : a European Journal of Chemical Biology
|October 23, 2020
PubMed
Summary
This summary is machine-generated.

Researchers are exploring the crypto-phosphoproteome, a challenging subset of protein phosphorylations. Understanding these elusive sites requires overcoming current technological hurdles for deeper insights into post-translational modifications.

Keywords:
binding domainskinasesphosphatasesphosphoproteomeprotein phosphorylation

More Related Videos

Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae
15:41

Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae

Published on: October 12, 2009

10.4K
A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
10:17

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

2.7K

Related Experiment Videos

Last Updated: Dec 4, 2025

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

5.5K
Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae
15:41

Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae

Published on: October 12, 2009

10.4K
A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors
10:17

A Mass Spectrometry-Based Approach to Identify Phosphoprotein Phosphatases and their Interactors

Published on: April 29, 2022

2.7K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • Protein phosphorylation is a critical post-translational modification (PTM).
  • Phosphoproteomics has advanced significantly, yet some phosphosites remain underexplored.
  • A subset of less chemically stable phosphosites, termed the crypto-phosphoproteome, presents unique challenges.

Purpose of the Study:

  • To summarize current knowledge on the crypto-phosphoproteome.
  • To identify technological gaps hindering the study of elusive protein phosphorylations.
  • To guide future research directions in this underexplored area.

Main Methods:

  • Review of existing phosphoproteomics techniques.
  • Analysis of limitations in current methodologies for unstable phosphosites.
  • Identification of key challenges in studying the crypto-phosphoproteome.

Main Results:

  • The crypto-phosphoproteome represents a significant, yet underexplored, fraction of protein phosphorylation.
  • Current phosphoproteomics technologies face limitations in detecting and characterizing chemically unstable phosphosites.
  • Specific technological advancements are needed to fully elucidate the crypto-phosphoproteome.

Conclusions:

  • Further research into the crypto-phosphoproteome is essential for a comprehensive understanding of protein phosphorylation.
  • Overcoming technological challenges is crucial for advancing the field.
  • Future studies should focus on developing novel methods to access these elusive phosphosites.