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Related Concept Videos

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...
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...
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 Proteasome Structure01:17

The Proteasome Structure

The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...

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In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination
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Ubiquitin proteolytic system: focus on SUMO.

Van G Wilson1, Phillip R Heaton

  • 1Department of Microbial & Molecular Pathogenesis, College of Medicine, Texas A&M Health Science Center, College Station, TX 77843-1114, USA. wilson@medicine.tamhsc.edu

Expert Review of Proteomics
|February 20, 2008
PubMed
Summary
This summary is machine-generated.

Small ubiquitin-like modifier (SUMO) proteins are crucial ubiquitin family modifiers. Proteomics reveals more SUMO targets and interactions, promising new insights into cellular regulation and SUMO-ubiquitin cross-talk.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Biochemistry

Background:

  • Small ubiquitin-like modifier (SUMO) proteins are key post-translational modifiers.
  • SUMOs function similarly to ubiquitin, attaching covalently to lysine residues on substrate proteins.
  • The ubiquitin super family includes SUMO proteins, vital for cellular processes.

Purpose of the Study:

  • To highlight the impact of proteomics on understanding SUMOylation.
  • To discuss the future potential of proteomic techniques in SUMO research.
  • To explore the interplay between SUMOylation and ubiquitination.

Main Methods:

  • Application of proteomics to identify SUMOylation targets.
  • Development of refined proteomic techniques for global SUMOylation analysis.
  • Investigating cross-talk mechanisms between SUMOylation and ubiquitination pathways.

Main Results:

  • Proteomics has significantly expanded the known targets and sites of SUMOylation.
  • Global analysis of sumoylated proteins offers new insights into SUMO functions.
  • Evidence suggests significant cross-talk and coordination between SUMOylation and ubiquitination.

Conclusions:

  • Advanced proteomic methods will drive major discoveries in SUMOylation research.
  • Understanding SUMOylation dynamics is critical for cellular environmental responses.
  • Coordinated SUMOylation and ubiquitination are essential for regulating fundamental cellular events.