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Related Concept Videos

Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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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.
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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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Multivesicular bodies (MVBs) are mature endosomes that sort ubiquitinated proteins and then fuse with lysosomes to degrade the sorted proteins. Epidermal growth factor (EGF) and its receptor (EGFR) form a complex that can be internalized through endocytosis, sorted into an MVB, and later degraded.
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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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Related Experiment Video

Updated: Aug 4, 2025

Using Phage Display to Develop Ubiquitin Variant Modulators for E3 Ligases
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Using Phage Display to Develop Ubiquitin Variant Modulators for E3 Ligases

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Generation and Characterization of Engineered Ubiquitin Variants to Modulate the Ubiquitin Signaling Cascade.

Chen T Liang1, Olivia Roscow1, Wei Zhang2,3

  • 1Department of Molecular and Cellular Biology, College of Biological Science, University of Guelph, Guelph, Ontario N1G2W1, Canada.

Cold Spring Harbor Protocols
|March 30, 2023
PubMed
Summary

Researchers developed novel ubiquitin variants (UbVs) using protein engineering to modulate the ubiquitin system, offering potential new therapies for diseases like cancer by targeting ubiquitination pathways.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Drug Discovery

Background:

  • The ubiquitin signaling cascade is vital in cellular functions, and its dysregulation is linked to diseases such as cancer.
  • Targeting ubiquitination and deubiquitination pathways is a key strategy in developing new therapeutics.
  • Protein-based modulators offer specificity and potency for modulating ubiquitin signal transduction.

Approach:

  • Utilizing a structure-based combinatorial protein-engineering strategy to create ubiquitin variants (UbVs).
  • Employing phage display technology for the generation and selection of UbV libraries.
  • Developing and refining methods for UbV binder selection and library improvement.

Key Points:

  • Detailed review of the design and generation of phage-displayed UbV libraries.
  • Comprehensive overview of in vitro and cellular methodologies for characterizing UbV binders.
  • Highlighting recent applications of UbVs in developing potential therapeutic molecules.

Conclusions:

  • Ubiquitin variants (UbVs) represent a promising class of protein-based therapeutics.
  • The presented approaches facilitate the development of specific modulators for the ubiquitin-proteasome system.
  • UbV technology holds significant potential for future drug development targeting ubiquitin-related diseases.