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Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

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....

Epigenetic Regulation

Epigenetic Regulation

Epigenetic changes alter the physical structure of the DNA without changing the genetic sequence and often regulate whether genes are turned on or off. This regulation ensures that each cell produces only proteins necessary for its function. For example, proteins that promote bone growth are not produced in muscle cells. Epigenetic mechanisms play an essential role in healthy development. Conversely, precisely regulated epigenetic mechanisms are disrupted in diseases like cancer.
X-chromosome...

Epigenetic Regulation

Epigenetic Regulation

Epigenetic mechanisms play an essential role in healthy development. Conversely, precisely regulated epigenetic mechanisms are disrupted in diseases like cancer.

Epigenetic Regulation

Epigenetic Regulation

Protein Folding Quality Check in the RER

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...

Oligosaccharide Assembly

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...

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Toxicological Assays for Testing Effects of an Epigenetic Drug on Development, Fecundity and Survivorship of Malaria Mosquitoes

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Published on: January 16, 2015

O-GlcNAcylation regulates EZH2 protein stability and function.

Chi-Shuen Chu¹, Pei-Wen Lo, Yi-Hsien Yeh

¹Genomics Research Center, Academia Sinica, Taipei 115, Taiwan.

Proceedings of the National Academy of Sciences of the United States of America

|January 30, 2014

Summary

This summary is machine-generated.

O-linked N-acetylglucosamine (GlcNAc) transferase (OGT) stabilizes the EZH2 protein via O-GlcNAcylation, which is crucial for forming the H3K27me3 epigenetic mark that silences genes.

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Published on: September 20, 2018

Area of Science:

Epigenetics
Molecular Biology
Biochemistry

Background:

O-linked N-acetylglucosamine (GlcNAc) transferase (OGT) regulates gene transcription and epigenetics.
Dysregulation of OGT is linked to diseases like cancer, but mechanisms are unclear.
Histone 3 trimethylation at K27 (H3K27me3) marks silenced chromatin and is catalyzed by EZH2 within PRC2.

Purpose of the Study:

To investigate the role of OGT in H3K27me3 formation and its connection to EZH2.
To elucidate the mechanism by which OGT influences EZH2 activity and PRC2 complex integrity.
To identify potential tumor suppressor genes regulated by the OGT-EZH2 pathway.

Main Methods:

OGT depletion via knockdown.
Analysis of H3K27me3 levels and other histone modifications.
Assessment of EZH2 protein stability and PRC2 complex integrity.
Co-immunoprecipitation and cosedimentation assays to detect OGT-EZH2/PRC2 interactions.
Site-directed mutagenesis to identify EZH2 O-GlcNAcylation site.
Microarray and ChIP analysis.

Main Results:

OGT depletion significantly reduced H3K27me3 levels.
OGT knockdown decreased EZH2 protein stability and disrupted PRC2 integrity.
OGT directly interacts with EZH2/PRC2.
Serine 75 (S75) was identified as the O-GlcNAcylation site on EZH2; S75A mutation reduced EZH2 stability.
A subset of tumor suppressor genes was found to be repressed by the OGT-EZH2 axis.

Conclusions:

OGT-mediated O-GlcNAcylation of EZH2 at S75 stabilizes EZH2.
This stabilization is essential for H3K27me3 formation and gene silencing.
OGT plays a critical epigenetic role in regulating histone methylation through EZH2 stabilization.