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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...
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...
Role of Matrix Metalloproteases in Degradation of ECM01:23

Role of Matrix Metalloproteases in Degradation of ECM

Matrix metalloproteases (MMPs) are enzymes involved in the hydrolysis of proteins and glycoproteins of the extracellular matrix. MMPs are essential for the migration and proliferation of cells through the dense matrix network, throughout embryonic development, and throughout morphogenesis. The first MMP activity discovered was a collagenase in a tadpole's tail undergoing metamorphosis. The active collagen deposition and modifications lead to the morphogenesis of tadpoles into the adult body.
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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

Function and regulation of SUMO proteases.

Christopher M Hickey1, Nicole R Wilson, Mark Hochstrasser

  • 1Department of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, Connecticut 06520, USA.

Nature Reviews. Molecular Cell Biology
|November 24, 2012
PubMed
Summary
This summary is machine-generated.

Protein desumoylation, regulated by SUMO proteases, is crucial for cellular functions. Recent discoveries reveal new SUMO protease classes, specificities, and roles, alongside connections to SUMO-targeted ubiquitin ligases (STUbLs).

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In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity
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Published on: January 29, 2018

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Localization of SUMO-modified Proteins Using Fluorescent Sumo-trapping Proteins
06:23

Localization of SUMO-modified Proteins Using Fluorescent Sumo-trapping Proteins

Published on: April 27, 2019

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Small ubiquitin-like modifier (SUMO) conjugation to proteins is a dynamic and regulated post-translational modification.
  • SUMO proteases are key enzymes that reverse SUMOylation, influencing critical cellular processes like transcription, cell division, and ribosome biogenesis.

Purpose of the Study:

  • To summarize recent advancements in the field of SUMO proteases.
  • To highlight novel discoveries in SUMO protease classes, specificity, and cellular functions.
  • To explore the emerging connections between SUMO proteases and SUMO-targeted ubiquitin ligases (STUbLs).

Main Methods:

  • Literature review of recent research on SUMO proteases.
  • Analysis of newly identified SUMO protease classes and their functions.
  • Investigation of the interplay between SUMO proteases and STUbLs.

Main Results:

  • Discovery of two novel classes of SUMO proteases.
  • Gained insights into the specificity of SUMO proteases for their substrates.
  • Revealed previously unrecognized functions of SUMO proteases in essential cellular pathways.
  • Established new links between SUMO proteases and STUbLs.

Conclusions:

  • The field of SUMO proteases is rapidly evolving with significant new discoveries.
  • SUMO proteases play diverse and critical roles in cellular regulation.
  • The integration of SUMOylation and ubiquitination pathways via STUbLs represents a key area for future research.