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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...
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 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 Unfolded Protein Response01:37

The Unfolded Protein Response

The ER is the hub of protein synthesis in a cell. It has robust systems to quality control protein folding and also for degradation of terminally misfolded proteins. Under normal conditions, a small proportion of misfolded proteins that cannot be salvaged need to be transported to the cytoplasm by the ER-associated degradation or ERAD pathways. However, if the ERAD cannot handle the misfolded proteins, the cell activates the unfolded protein response or UPR to adjust the protein folding...
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...

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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

IAPS and ubiquitylation.

Rebecca Feltham1, Nufail Khan, John Silke

  • 1Department of Biochemistry, La Trobe University, Victoria, Australia.

IUBMB Life
|February 25, 2012
PubMed
Summary
This summary is machine-generated.

Inhibitors of apoptosis (IAP) proteins regulate cell death and survival by orchestrating ubiquitin modifications. This review focuses on the crucial interplay between IAPs and ubiquitin in controlling cell signaling pathways.

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Comparative Strategies for Ubiquitination Detection in Mammalian Cell Lysates Using SMAD2/SMURF2 as a Model
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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:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Inhibitors of apoptosis (IAP) proteins are critical negative regulators of programmed cell death.
  • IAP proteins possess a RING domain, classifying them as ubiquitin ligases that control cell survival.
  • Aberrant IAP protein levels are linked to tumor progression.

Purpose of the Study:

  • To review the intricate relationship between IAP proteins and ubiquitin modification.
  • To highlight the significance of this interaction in regulating IAPs, their substrates, and cell death/survival pathways.

Main Methods:

  • Literature review focusing on the interplay between IAPs and ubiquitin.
  • Analysis of ubiquitinylation mechanisms and their role in IAP function.
  • Discussion of IAP-mediated regulation of cell signaling.

Main Results:

  • Ubiquitin modification is a fundamental cellular process with diverse signaling outcomes.
  • IAP proteins, as E3 ubiquitin ligases, provide substrate specificity and control cellular fate.
  • The interplay between IAPs and ubiquitin is central to regulating cell death and survival.

Conclusions:

  • Understanding the IAP-ubiquitin relationship is vital for comprehending cell survival and death.
  • This interaction offers potential therapeutic targets for cancer and other diseases.
  • Further research into IAP-mediated ubiquitinylation can elucidate complex signaling networks.