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Related Concept Videos

Covalently Linked Protein Regulators02:04

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.
Covalently Linked Protein Regulators02:04

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.
The JAK-STAT Signaling Pathway01:20

The JAK-STAT Signaling Pathway

Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as  SH2...
Histone Modification02:32

Histone Modification

The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
Histone Modification02:32

Histone Modification

The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
Co-activators and Co-repressors02:04

Co-activators and Co-repressors

Gene transcription is regulated by the synergistic action of several proteins that form a complex at a gene regulatory site. This is observed in eukaryotes, where the regulation of gene expression is a complex process. Regulatory proteins in eukaryotes can broadly be classified into two types – regulators that bind directly to specific DNA sequences and co-regulators that associate with regulatory proteins but cannot directly bind to the DNA. These co-regulators are further divided into...

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Related Experiment Video

Updated: May 7, 2026

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity
09:45

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity

Published on: January 29, 2018

Acetylation and sumoylation control STAT5 activation antagonistically.

Oliver H Krämer1, Richard Moriggl

  • 1Center for Molecular Biomedicine; Institute for Biochemistry and Biophysics; Department of Biochemistry; Friedrich Schiller University of Jena; Jena, Germany.

JAK-STAT
|September 24, 2013
PubMed
Summary
This summary is machine-generated.

STAT5 protein sumoylation impairs tyrosine phosphorylation, disrupting lymphocyte signaling. Acetylation and sumoylation antagonistically regulate STAT5 activity, impacting immune cell function.

Keywords:
STAT5ASTAT5Bacetylationcrosstalksumoylationtyrosine phosphorylation

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Last Updated: May 7, 2026

In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity
09:45

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Published on: January 29, 2018

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Published on: November 2, 2017

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12:11

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

Published on: February 27, 2020

Area of Science:

  • Immunology
  • Molecular Biology
  • Cell Signaling

Background:

  • Signal transducer and activator of transcription 5 (STAT5) proteins are crucial for lymphocyte development and function.
  • STAT5 activation typically involves tyrosine phosphorylation, but other post-translational modifications are increasingly recognized.
  • These modifications include serine/threonine phosphorylation, acetylation, and sumoylation near the critical tyrosine residue.

Purpose of the Study:

  • To investigate the role of sumoylation in STAT5 signaling.
  • To examine the impact of impaired SUMO-specific protease 1 (SENP1) on STAT5 modification and function.
  • To explore the antagonistic relationship between STAT5 acetylation and sumoylation in controlling tyrosine phosphorylation.

Main Methods:

  • Analysis of STAT5 signaling in lymphocytes from SENP1 knockout (SENP1(-/-)) mice.
  • Assessment of STAT5 sumoylation and tyrosine phosphorylation levels.
  • Investigation of acetylation and sumoylation interplay on STAT5.

Main Results:

  • STAT5 is extensively sumoylated in lymphocytes from SENP1(-/-) mice.
  • Sumoylated STAT5 exhibits abolished tyrosine phosphorylation, indicating impaired signaling.
  • Acetylation and sumoylation of STAT5 were found to act antagonistically.

Conclusions:

  • SUMO-specific protease 1 (SENP1) is essential for normal STAT5 signaling in lymphocytes.
  • Sumoylation of STAT5 inhibits its tyrosine phosphorylation, thereby blocking STAT5-dependent signaling pathways.
  • The balance between STAT5 acetylation and sumoylation is critical for regulating STAT5 activation and function.