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

Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

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...
Phosphorylation01:02

Phosphorylation

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...
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...
Transducer Mechanism: Enzyme-Linked Receptors01:27

Transducer Mechanism: Enzyme-Linked Receptors

Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:
Phosphoinositides and PIPs01:42

Phosphoinositides and PIPs

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...

You might also read

Related Articles

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

Sort by
Same author

Elimusertib enhances cytotoxic effects of conventional chemotherapy and sensitizes to radiation in preclinical Ewing sarcoma models.

Scientific reports·2026
Same author

Lipid Pocket Binders Impose Allosteric Changes of Protein Dynamics Around the Active Site of the Protein Kinase p38α.

Angewandte Chemie (International ed. in English)·2026
Same author

Lessons from Structural Biology for Understanding Drug Resistance in Gastrointestinal Stromal Tumors (GIST).

Journal of medicinal chemistry·2026
Same author

Targeting KRAS<sup>G13C</sup> with cyclic linker based inhibitors to explore warhead orientation.

Scientific reports·2025
Same author

Phase II Trial of Ponatinib in Patients with Metastatic Gastrointestinal Stromal Tumor following Failure or Intolerance of Prior Therapy with Imatinib (POETIG Trial).

Clinical cancer research : an official journal of the American Association for Cancer Research·2025
Same author

Computational Design of Lysine Targeting Covalent Binders Using Rosetta.

Journal of chemical information and modeling·2025
Same journal

Transport specificity of FpvA and FpvB for pyoverdine-antibiotic conjugates in Pseudomonas aeruginosa.

Bioorganic & medicinal chemistry·2026
Same journal

Design and engineering of μO-conotoxin MfVIA mutants to enhance Na<sub>V</sub>1.8 inhibition and analgesic efficacy in inflammatory pain.

Bioorganic & medicinal chemistry·2026
Same journal

Recent advances in Camptothecin-derived antibody-drug conjugates.

Bioorganic & medicinal chemistry·2026
Same journal

CDK4/6-targeted therapy: From clinical inhibitors to emerging strategies to overcome resistance.

Bioorganic & medicinal chemistry·2026
Same journal

Coumarin-sulfonamide hybrids as PKM2 activators induce metabolic reprogramming and suppress ovarian cancer cell growth.

Bioorganic & medicinal chemistry·2026
Same journal

Recent advances in the development of small-molecule drugs based on covalent reversible inhibitors.

Bioorganic & medicinal chemistry·2026
See all related articles

Related Experiment Video

Updated: Jun 3, 2026

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

Using small molecules to target protein phosphatases.

Viktor V Vintonyak1, Herbert Waldmann, Daniel Rauh

  • 1Max-Planck-Institute of Molecular Physiology, Otto-Hahn-Strasse 11, D-44227 Dortmund, Germany.

Bioorganic & Medicinal Chemistry
|March 23, 2011
PubMed
Summary
This summary is machine-generated.

Protein phosphatases regulate crucial biological processes. Developing selective inhibitors for these enzymes is vital for treating diseases like cancer, but faces challenges in selectivity and pharmacokinetics.

More Related Videos

Development and Application of Rapamycin-regulated Tyrosine Phosphatases
06:56

Development and Application of Rapamycin-regulated Tyrosine Phosphatases

Published on: September 6, 2024

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein
11:23

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Published on: June 30, 2019

Related Experiment Videos

Last Updated: Jun 3, 2026

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

Development and Application of Rapamycin-regulated Tyrosine Phosphatases
06:56

Development and Application of Rapamycin-regulated Tyrosine Phosphatases

Published on: September 6, 2024

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein
11:23

Characterization at the Molecular Level using Robust Biochemical Approaches of a New Kinase Protein

Published on: June 30, 2019

Area of Science:

  • Biochemistry and Molecular Biology
  • Drug Discovery and Development

Background:

  • Protein phosphorylation/dephosphorylation is a key regulatory mechanism in biological systems.
  • Dysregulation of protein kinases and phosphatases is linked to diseases including cancer, diabetes, and neurodegenerative disorders.
  • These enzymes are attractive targets for therapeutic intervention.

Purpose of the Study:

  • To explore strategies for identifying and developing inhibitors against clinically relevant protein phosphatases.
  • To provide an overview of the current landscape, challenges, and limitations in phosphatase inhibitor development.

Main Methods:

  • Review of current research strategies for phosphatase inhibitor discovery.
  • Analysis of challenges in achieving selectivity and favorable pharmacokinetics for phosphatase inhibitors.

Main Results:

  • Inhibition of phosphorylation is a significant strategy in targeted therapies.
  • Development of clinically viable phosphatase inhibitors faces substantial hurdles.
  • Limited selectivity and unfavorable pharmacokinetics are major bottlenecks.

Conclusions:

  • Understanding the importance and limitations of targeting protein phosphatases is crucial for advancing drug discovery.
  • Further research is needed to overcome current challenges in developing effective phosphatase inhibitors.