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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...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
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...
Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
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...

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Related Experiment Video

Updated: May 10, 2026

In Vitro Analysis of E3 Ubiquitin Ligase Function
06:06

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

The Hydra small ubiquitin-like modifier.

Umair Khan1, Prajwalini Mehere, Senthilkumar Deivasigamani

  • 1Biology, Indian Institute of Science Education and Research, Pune, India.

Genesis (New York, N.Y. : 2000)
|June 20, 2013
PubMed
Summary
This summary is machine-generated.

Scientists characterized SUMO (Small Ubiquitin-like Modifier) cycle components in Hydra, a regenerating cnidarian. They found SUMO proteases are conserved from Hydra to flies, aiding SUMO maturation and deconjugation.

Keywords:
SUMOSentrinUlppolypprotease

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Developmental Biology

Background:

  • Small Ubiquitin-like Modifier (SUMO) is a crucial post-translational modifier involved in diverse cellular functions across eukaryotes.
  • SUMOylation machinery, including SUMO proteins and SUMO proteases, is generally conserved in eukaryotic organisms.
  • Hydra, a cnidarian, possesses remarkable regenerative capabilities, making it a model organism to study conserved biological processes.

Purpose of the Study:

  • To characterize the SUMOylation pathway components in Hydra, focusing on SUMO and SUMO proteases.
  • To investigate the functional conservation of SUMO proteases in processing immature SUMO.
  • To establish tools for in vivo monitoring and target identification of the SUMO cycle in Hydra.

Main Methods:

  • Bioinformatic analysis, gene cloning, and biochemical characterization of Hydra SUMO and SUMO protease.
  • Comparative analysis of SUMO protease activity across species (Hydra to flies).
  • Generation of a transgenic Hydra expressing a SUMO-GFP fusion protein for in vivo studies.

Main Results:

  • Identification and characterization of key SUMOylation pathway components in Hydra.
  • Demonstration of conserved SUMO processing activity by Hydra SUMO proteases, similar to those in flies.
  • Successful generation of a transgenic Hydra model for SUMO cycle research.

Conclusions:

  • The core SUMOylation machinery, particularly SUMO proteases, exhibits evolutionary conservation from cnidarians to insects.
  • This study provides foundational insights into the SUMOylation pathway in a basal metazoan.
  • The developed transgenic Hydra model offers a novel system for future investigations into SUMOylation in regeneration and development.