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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...
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

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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...
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.
Anaphase Promoting Complex00:50

Anaphase Promoting Complex

The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...

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Methods to Assess Subcellular Compartments of Muscle in C. elegans
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Published on: November 13, 2014

Ubiquitin-mediated pathways in C. elegans.

Edward T Kipreos1

  • 1Department of Cellular Biology, University of Georgia, Athens, GA 30602-2607, USA. ekipreos@cb.uga.edu

Wormbook : the Online Review of C. Elegans Biology
|December 1, 2007
PubMed
Summary
This summary is machine-generated.

This study reviews ubiquitin pathways in C. elegans, detailing components and their roles in development. Research highlights how ubiquitin conjugation regulates protein degradation and cellular functions.

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Last Updated: Jul 9, 2026

Methods to Assess Subcellular Compartments of Muscle in C. elegans
10:13

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Published on: November 13, 2014

In Vivo Quantification of Protein Turnover in Aging C. Elegans using Photoconvertible Dendra2
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In Vitro Analysis of E3 Ubiquitin Ligase Function
06:06

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

Area of Science:

  • Molecular Biology
  • Cell Biology
  • Developmental Biology

Background:

  • Ubiquitin, a conserved polypeptide, tags proteins for degradation or functional modification via the ubiquitin-proteasome system.
  • This system is crucial for dynamic cellular processes and involves ubiquitin-activating enzymes, ubiquitin-conjugating enzymes, and ubiquitin-protein ligases.

Purpose of the Study:

  • To provide a comprehensive overview of ubiquitin-mediated pathways in the nematode Caenorhabditis elegans.
  • To describe known components of the ubiquitin system and their molecular, cellular, and developmental functions.

Main Methods:

  • Utilized forward genetics, reverse genetics, and genome-wide RNA interference (RNAi) screens.
  • Conducted detailed analyses of ubiquitin-protein ligase classes to identify substrates and regulated pathways.

Main Results:

  • Identified one ubiquitin-activating enzyme, twenty putative ubiquitin-conjugating enzymes, and numerous ubiquitin-protein ligases in C. elegans.
  • Characterized loss-of-function phenotypes for most ubiquitin pathway components.
  • Determined substrates and molecular pathways regulated by specific ubiquitin-protein ligases.

Conclusions:

  • C. elegans serves as a model organism for studying ubiquitin pathway functions in development.
  • Research has elucidated the roles of various ubiquitin pathway components in cellular processes and organismal development.