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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...
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...
Abnormal Proliferation02:23

Abnormal Proliferation

Under normal conditions, most adult cells remain in a non-proliferative state unless stimulated by internal or external factors to replace lost cells. Abnormal cell proliferation is a condition in which the cell's growth exceeds and is uncoordinated with normal cells. In such situations, cell division persists in the same excessive manner even after cessation of the stimuli, leading to persistent tumors. The tumor arises from the damaged cells that replicate to pass the damage to the daughter...
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...

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Related Experiment Video

Updated: Jun 1, 2026

Purification of Ubiquitinated p53 Proteins from Mammalian Cells
10:55

Purification of Ubiquitinated p53 Proteins from Mammalian Cells

Published on: March 21, 2022

p53 regulation by ubiquitin.

Christopher L Brooks1, Wei Gu

  • 1Stemline Therapeutics, Inc., 1675 York Avenue, Suite 34-L, New York, NY 10128, USA. cbrooks@stemline.com

FEBS Letters
|June 1, 2011
PubMed
Summary

The ubiquitination pathway regulates protein function, including the p53 tumor suppressor, through ubiquitin modifications. Reversible deubiquitination adds another regulatory control layer to p53 activity.

Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • The ubiquitination pathway is a dynamic cellular process regulating protein degradation and function.
  • The p53 tumor suppressor and associated factors are modulated by ubiquitin and ubiquitin-like proteins.
  • These modifications are crucial for p53 protein stability, localization, and activity.

Purpose of the Study:

  • To review recent advances in understanding the ubiquitination pathway's role in p53 regulation.
  • To highlight the impact of deubiquitination enzymes on p53 function.
  • To elucidate the regulatory mechanisms controlling p53 through reversible ubiquitination.

Main Methods:

  • Literature review of recent studies on ubiquitination and p53.
  • Analysis of research on deubiquitination enzymes targeting p53.

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Detection of Protein Ubiquitination
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Detection of Protein Ubiquitination

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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

Published on: April 17, 2026

Related Experiment Videos

Last Updated: Jun 1, 2026

Purification of Ubiquitinated p53 Proteins from Mammalian Cells
10:55

Purification of Ubiquitinated p53 Proteins from Mammalian Cells

Published on: March 21, 2022

Detection of Protein Ubiquitination
09:00

Detection of Protein Ubiquitination

Published on: August 19, 2009

Comparative Strategies for Ubiquitination Detection in Mammalian Cell Lysates Using SMAD2/SMURF2 as a Model
09:00

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

Published on: April 17, 2026

  • Synthesis of information on the dynamic regulation of p53 by ubiquitin modifications.

    • Main Results:

    • Ubiquitination critically controls p53 degradation, localization, and activity.
    • Deubiquitination enzymes specifically remove ubiquitin from p53 and pathway factors.
    • The reversible nature of ubiquitination provides an additional regulatory layer for p53.

    Conclusions:

    • Ubiquitin modifications are central to p53 pathway regulation.
    • Deubiquitination offers a key mechanism for controlling p53 function.
    • Recent advances reveal a complex, dynamic regulatory network governing p53 activity.