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Anaphase Promoting Complex

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...

The Proteasome

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 Proteasome

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...

Covalently Linked Protein Regulators

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 Degradation

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...

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Related Experiment Video

Updated: May 19, 2026

Profiling Ubiquitin and Ubiquitin-like Dependent Post-translational Modifications and Identification of Significant Alterations

Profiling Ubiquitin and Ubiquitin-like Dependent Post-translational Modifications and Identification of Significant Alterations

Published on: November 7, 2019

Finally, polyubiquitinated PCNA gets recognized.

Michelle K Zeman¹, Karlene A Cimprich

¹Department of Chemical and Systems Biology, Stanford University, Stanford, CA 94305, USA.

|August 14, 2012

Summary

This summary is machine-generated.

The translocase ZRANB3/AH2 recognizes ubiquitinated PCNA to restart stalled DNA replication forks. This discovery is crucial for understanding DNA repair mechanisms and maintaining genome stability.

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Area of Science:

Molecular Biology
DNA Replication
Ubiquitination

Background:

DNA replication forks can stall due to various cellular stresses.
Stalled forks require efficient restart mechanisms to maintain genome integrity.
Ubiquitination of proliferating cell nuclear antigen (PCNA) is a key signal in DNA damage response.

Discussion:

The translocase ZRANB3/AH2 interacts with K63-linked polyubiquitinated PCNA.
This interaction is essential for the process of restarting stalled replication forks.
The findings highlight a conserved mechanism for fork stabilization and repair.

Key Insights:

ZRANB3/AH2 acts as a sensor for ubiquitinated PCNA.
The enzyme facilitates the resolution of replication stress.
This provides a molecular link between ubiquitination and replication fork restart.

Outlook:

Further investigation into ZRANB3/AH2 function in various cellular contexts.
Exploring therapeutic strategies targeting ZRANB3/AH2 in diseases associated with DNA repair defects.
Understanding the precise structural basis of ZRANB3/AH2 interaction with ubiquitinated PCNA.