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Related Concept Videos

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...
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...
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...
Phosphodiester Linkages01:01

Phosphodiester Linkages

Overview
Phosphodiester bond forms when a phosphoric acid molecule (H3PO4) links with two hydroxyl groups (–OH) of two other molecules, forming two ester bonds. Two water molecules are released in this process. The phosphodiester bond is commonly found in nucleic acids (DNA and RNA) and plays a critical role in their structure and function.
Phosphodiester Bonds Link Nucleotides Together
DNA and RNA are polynucleotides or long chains of nucleotides that are linked together. A nucleotide is...
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...

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Related Experiment Video

Updated: Jun 4, 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

Phosphoryl-EZH-ion.

Giuseppina Caretti1, Daniela Palacios, Vittorio Sartorelli

  • 1Department of Biomolecular Sciences and Biotechnology, University of Milan, 20133 Milan, Italy.

Cell Stem Cell
|March 3, 2011
PubMed
Summary
This summary is machine-generated.

Polycomb group (PcG) proteins control gene expression in stem cells, but how they target genes is unclear. EZH2, a key component of PRC2, acts as a nuclear phosphoprotein connecting cell signals to epigenetic changes.

More Related Videos

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Related Experiment Videos

Last Updated: Jun 4, 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

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Area of Science:

  • Epigenetics
  • Molecular Biology
  • Stem Cell Biology

Background:

  • Polycomb group (PcG) proteins are crucial regulators of gene expression in stem cells.
  • The precise mechanisms of PcG protein gene targeting and regulation are not fully understood.
  • EZH2, the enzymatic subunit of Polycomb Repressive Complex 2 (PRC2), has emerged as a key player.

Purpose of the Study:

  • To elucidate the role of EZH2 in PcG protein-mediated gene regulation.
  • To investigate how EZH2 links cellular signals to epigenetic modifications.
  • To understand the targeting mechanisms of PcG proteins in stem cells.

Main Methods:

  • Investigating the function of EZH2 in gene expression.
  • Analyzing the interaction of EZH2 with other proteins.
  • Studying the epigenetic modifications associated with EZH2 activity.

Main Results:

  • EZH2 functions as a nuclear phosphoprotein.
  • EZH2 connects cell-cycle-intrinsic and extracellular signals to epigenetic signatures.
  • Evidence suggests EZH2 is central to PcG protein targeting and regulation.

Conclusions:

  • EZH2 plays a critical role in PcG-mediated gene silencing.
  • EZH2 integrates cellular signaling pathways with epigenetic control of gene expression.
  • Further research into EZH2 mechanisms will illuminate stem cell regulation.