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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.
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
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,...
Phase II Reactions: Acetylation Reactions01:24

Phase II Reactions: Acetylation Reactions

Acetylation, a phase II biotransformation reaction, introduces an acetyl group to drugs or their metabolites. Acetyltransferase enzymes facilitate this reaction, which resembles α-amino acid conjugation due to the addition of a functional group to the drug molecule.
The substrates for acetylation are typically drugs or their metabolites with an amino, sulfonamide, or hydrazine functional group. Acetylation can occur at several points in the drug molecule, including primary, secondary, and...

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Related Experiment Video

Updated: May 22, 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

An acetylation switch regulates SUMO-dependent protein interaction networks.

Rebecca Ullmann1, Christopher D Chien, Maria Laura Avantaggiati

  • 1Institute of Biochemistry II, Goethe University School of Medicine, Theodor-Stern-Kai 7, D-60590 Frankfurt, Germany.

Molecular Cell
|May 15, 2012
PubMed
Summary

Acetylation of SUMO proteins controls cellular signaling by blocking interactions with SUMO-interaction motifs (SIMs). This acetylation switch regulates gene silencing and protein complex assembly, impacting SUMO-SIM dynamics.

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Related Experiment Videos

Last Updated: May 22, 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

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization
12:11

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

Published on: February 27, 2020

In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells
09:40

In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells

Published on: November 2, 2017

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • SUMOylation regulates cellular signaling via SUMO-interaction motifs (SIMs).
  • SIMs typically bind SUMO through hydrophobic interactions and charge complementarity.
  • The role of post-translational modifications at the SUMO-SIM interface is less understood.

Purpose of the Study:

  • To investigate the role of acetylation in regulating SUMO-SIM interactions.
  • To identify the impact of acetylation on SUMO-mediated cellular processes.

Main Methods:

  • Analysis of SUMO-SIM binding in the presence of acetylation.
  • Investigating the effect of acetylation on gene silencing mediated by SUMO and PIAS proteins.
  • Assessing the impact on PML nuclear body assembly and Daxx recruitment.

Main Results:

  • Acetylation neutralizes basic charges on SUMO, preventing binding to SIMs in PML, Daxx, and PIAS proteins.
  • Acetylation does not inhibit the interaction between RanBP2 and SUMO.
  • Acetylation by HDACs attenuates SUMO- and PIAS-mediated gene silencing and restrains Daxx recruitment to PML nuclear bodies.

Conclusions:

  • Acetylation acts as a key regulatory switch for SUMO-SIM interactions.
  • This mechanism controls the selectivity and dynamics of SUMOylation signaling.
  • Acetylation expands the regulatory network of SUMOylation in cellular processes like gene silencing and nuclear body formation.