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Related Concept Videos

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.
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...
Lipids as Anchors01:32

Lipids as Anchors

In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains the...
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.
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...

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Related Experiment Video

Updated: Jul 7, 2026

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
11:36

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

Published on: July 25, 2019

A ubiquitin-like system mediates protein lipidation.

Y Ichimura1, T Kirisako, T Takao

  • 1Department of Cell Biology, National Institute for Basic Biology, Okazaki, Japan.

Nature
|December 2, 2000
PubMed
Summary

Autophagy utilizes a novel protein lipidation process involving Apg8 (Autophagy-related protein 8) conjugation to phosphatidylethanolamine. This ubiquitination-like pathway is crucial for membrane dynamics during yeast autophagy.

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Last Updated: Jul 7, 2026

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
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Published on: July 25, 2019

Ubiquitin Chain Analysis by Parallel Reaction Monitoring
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Comparative Strategies for Ubiquitination Detection in Mammalian Cell Lysates Using SMAD2/SMURF2 as a Model
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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Autophagy is a vital cellular process for degrading proteins and organelles via lysosomes.
  • Apg8 (Autophagy-related protein 8) is essential for autophagy in yeast.
  • Apg8 undergoes C-terminal processing by Apg4 protease, resulting in a membrane-bound form.

Purpose of the Study:

  • To elucidate the mechanism of Apg8 modification and its role in autophagy.
  • To identify the pathway responsible for Apg8 conjugation to membranes.
  • To investigate the function of Apg8 lipidation in cellular membrane dynamics.

Main Methods:

  • Biochemical assays to study protein conjugation.
  • Analysis of ubiquitination-like pathways involving E1 and E2 enzymes.
  • Investigating the role of Apg7 and Apg3 in Apg8 modification.

Main Results:

  • Apg8 is covalently conjugated to phosphatidylethanolamine via an amide bond.
  • This lipidation is mediated by a ubiquitination-like system involving Apg7 and Apg3.
  • Apg7 activates both Apg12 and Apg8, directing them to specific E2 enzymes.

Conclusions:

  • A novel protein lipidation mechanism for Apg8 has been identified.
  • This Apg8-phosphatidylethanolamine conjugation is essential for membrane dynamics in autophagy.
  • The ubiquitination-like system plays a critical role in regulating autophagy.