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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.
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Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
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Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
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

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In Vitro Analysis of E3 Ubiquitin Ligase Function
06:06

In Vitro Analysis of E3 Ubiquitin Ligase Function

Published on: May 14, 2021

Animal HECT ubiquitin ligases: evolution and functional implications.

Ignacio Marín1

  • 1Instituto de Biomedicina de Valencia, Consejo Superior de Investigaciones Científicas (IBV-CSIC), Valencia, Spain. imarin@ibv.csic.es

BMC Evolutionary Biology
|February 24, 2010
PubMed
Summary

The classification of HECT ubiquitin ligases (HECT E3s) is revised, revealing 16 animal subfamilies that evolved early. This evolutionary history helps explain their roles in diseases like cancer.

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Area of Science:

  • Evolutionary biology
  • Molecular biology
  • Biochemistry

Background:

  • HECT ubiquitin ligases (HECT E3s) are crucial in the ubiquitin-proteasome system and implicated in human diseases.
  • Understanding HECT E3 evolution provides a framework for interpreting functional data.

Purpose of the Study:

  • To analyze the diversification patterns of HECT E3s since the emergence of animals.
  • To establish a robust classification and evolutionary framework for HECT E3s.

Main Methods:

  • Phylogenetic analyses of HECT E3 protein sequences.
  • Sequence and structural analyses of HECT E3 proteins.
  • Comparative genomics to identify gene losses and evolutionary origins.

Main Results:

  • The current classification of HECT E3s into three groups is inaccurate.
  • Phylogenetic analyses support 16 distinct animal HECT E3 subfamilies, most originating before or during early animal evolution.
  • Independent gene losses occurred in specific lineages, coinciding with losses in other E3 ligase families.
  • Some HECT E3s emerged before the cellular systems they regulate, suggesting independent co-option for similar functions.

Conclusions:

  • The complex evolutionary history of animal HECT E3s has been elucidated.
  • Results suggest specific model organisms for studying HECT E3s and propose new research directions.