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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...
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 Proteasome Structure01:17

The Proteasome Structure

The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...

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Related Experiment Video

Updated: May 10, 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

CUE'd up for Monoubiquitin.

Christopher D Lima1

  • 1Department of Biochemistry, Structural Biology Program, Weill Medical College of Cornell University, New York, NY 10021, USA.

Cell
|June 6, 2003
PubMed
Summary
This summary is machine-generated.

Researchers have determined the first structures of CUE domains bound to monoubiquitin using NMR and X-ray crystallography. These findings reveal how CUE domains recognize ubiquitin, showing diverse interaction surfaces and domain variations.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Recognition

Background:

  • CUE domains are ubiquitin-binding modules implicated in various cellular processes.
  • Understanding the structural basis of ubiquitin recognition by CUE domains is crucial for deciphering their function.

Discussion:

  • The study presents the first high-resolution structures of CUE domain-monoubiquitin complexes.
  • Two distinct structural studies, one using NMR and another X-ray crystallography, provide complementary insights.
  • Structural comparisons reveal that CUE domains utilize different surfaces to interact with monoubiquitin.

Key Insights:

  • The obtained structures elucidate the molecular mechanisms of ubiquitin recognition by CUE domains.
  • Evidence suggests a heterogeneity in CUE domain interaction surfaces, implying functional diversity.
  • This work provides a structural foundation for understanding the specificity and adaptability of CUE-mediated signaling.

Outlook:

  • Further structural and functional studies are needed to explore the full spectrum of CUE domain-ubiquitin interactions.
  • Investigating how variations in CUE domain surfaces influence cellular localization and downstream signaling pathways.
  • Exploring the therapeutic potential of targeting CUE domain-ubiquitin interactions in disease contexts.