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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.
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...
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...
Regulation of the Unfolded Protein Response01:31

Regulation of the Unfolded Protein Response

Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
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: Jun 23, 2026

Detection of Protein Ubiquitination
09:00

Detection of Protein Ubiquitination

Published on: August 19, 2009

IAPs, RINGs and ubiquitylation.

David L Vaux1, John Silke

  • 1The Walter and Eliza Hall Institute, 1G Royal Parade, Parkville, Victoria 3050, Australia. vaux@wehi.edu.au

Nature Reviews. Molecular Cell Biology
|April 2, 2005
PubMed
Summary
This summary is machine-generated.

Inhibitor of apoptosis (IAP) proteins regulate cellular processes through baculoviral IAP repeat motifs and RING domains. Their functions, including ubiquitylation and self-degradation, are complex and increasingly understood.

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Last Updated: Jun 23, 2026

Detection of Protein Ubiquitination
09:00

Detection of Protein Ubiquitination

Published on: August 19, 2009

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry
11:54

Detection of Protein Ubiquitination Sites by Peptide Enrichment and Mass Spectrometry

Published on: March 23, 2020

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:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • Inhibitor of apoptosis (IAP) proteins are key regulators of cell death and survival.
  • IAPs possess baculoviral IAP repeat (BIR) motifs for protein interactions and RING domains for ubiquitin ligase activity.

Purpose of the Study:

  • To explore the multifaceted roles of IAP proteins in cellular regulation.
  • To understand the mechanisms of IAP-mediated ubiquitylation and its complex outcomes.
  • To investigate the regulation of IAP proteins themselves through ubiquitin-mediated degradation.

Main Methods:

  • Analysis of protein-protein interactions mediated by BIR motifs.
  • Biochemical assays to study E2 enzyme recruitment and ubiquitylation.
  • Investigation of ubiquitin-mediated degradation pathways affecting IAPs.

Main Results:

  • IAPs interact with diverse proteins via BIR motifs.
  • IAPs catalyze ubiquitylation of numerous targets, with complex downstream effects.
  • IAPs are subject to ubiquitin-mediated degradation, indicating intricate regulatory feedback loops.

Conclusions:

  • IAP proteins play a complex and dynamic role in cellular signaling.
  • Ubiquitylation is a critical mechanism controlling both IAP targets and IAPs themselves.
  • Further research into IAP ubiquitylation promises deeper insights into cell fate determination.