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Related Concept Videos

Regulated Protein Degradation02:58

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
Regulated Protein Degradation02:58

Regulated Protein Degradation

It is vital to regulate the activity of enzymatic as well as non-enzymatic proteins inside the cell. This can be achieved either through creating a balance between their rate of synthesis and degradation or regulating the intrinsic activity of the protein. Both these regulation mechanisms play an essential role in the normal functioning of cells.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
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.

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Related Experiment Video

Updated: May 8, 2026

SUMO-Binding Entities (SUBEs) as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer
08:29

SUMO-Binding Entities (SUBEs) as Tools for the Enrichment, Isolation, Identification, and Characterization of the SUMO Proteome in Liver Cancer

Published on: November 1, 2019

SUMO-targeted ubiquitin ligases.

Annie M Sriramachandran1, R Jürgen Dohmen

  • 1University of Cologne, Institute for Genetics, Zülpicher Straße 47a, D-50674 Cologne, Germany.

Biochimica Et Biophysica Acta
|September 11, 2013
PubMed
Summary
This summary is machine-generated.

Small ubiquitin-related modifier (SUMO) conjugation impacts protein function and stability. Novel SUMO-recognizing ubiquitin ligases (STUbLs) link SUMOylation to the ubiquitin-proteasome system, regulating modified proteins.

Keywords:
ArkadiaRnf4SIMSlx5Slx8Uls1

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Covalent posttranslational modification with SUMO (small ubiquitin-related modifier) regulates diverse protein functions in eukaryotic cells.
  • SUMOylation influences protein activity, interactions, localization, and stability.

Purpose of the Study:

  • To review recent insights into the properties and function of novel SUMO-recognizing ubiquitin ligases (STUbLs).
  • To discuss the role of STUbLs in regulating sumoylated proteins and their connection to the ubiquitin/proteasome system.

Main Methods:

  • Literature review of recent studies on SUMOylation and STUbL ligases.
  • Analysis of the functional interplay between SUMO modification and the ubiquitin-proteasome system.

Main Results:

  • Discovery of STUbLs (E3-S) that recognize sumoylated proteins.
  • STUbLs bridge SUMO modification with the ubiquitin/proteasome pathway.
  • These ligases play a key role in regulating the fate of sumoylated substrates.

Conclusions:

  • STUbLs represent a novel class of ubiquitin ligases with a crucial role in protein regulation.
  • Understanding STUbLs provides new insights into the integration of SUMOylation and ubiquitination pathways.
  • This connection is vital for cellular processes governed by the ubiquitin-proteasome system.