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Related Concept Videos

Regulated Protein Degradation02:58

Regulated Protein Degradation

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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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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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The Proteasome01:13

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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.
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Evaluation of Substrate Ubiquitylation by E3 Ubiquitin-ligase in Mammalian Cell Lysates
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Ubiquitin Ligases: Structure, Function, and Regulation.

Ning Zheng1, Nitzan Shabek1

  • 1Howard Hughes Medical Institute and Department of Pharmacology, University of Washington, Seattle, Washington 98195; email: nzheng@uw.edu , nshabek@uw.edu.

Annual Review of Biochemistry
|April 5, 2017
PubMed
Summary
This summary is machine-generated.

Ubiquitin E3 ligases are crucial for protein degradation in eukaryotes. Recent research reveals new E3 classes and substrate recognition mechanisms, paving the way for targeted disease therapies.

Keywords:
PTMagonistdegronposttranslational modificationubiquitin ligaseubiquitination

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Area of Science:

  • Biochemistry and Molecular Biology
  • Cellular Biology
  • Genetics

Background:

  • Ubiquitin E3 ligases are key enzymes in the ubiquitination cascade, targeting specific proteins for degradation.
  • RING and HECT E3 ligases have been extensively studied for their enzymatic activities and structures.
  • Understanding E3 ligase mechanisms is vital for comprehending cellular regulation.

Purpose of the Study:

  • To review recent advancements in the structure-function studies of ubiquitin E3 ligases.
  • To highlight novel classes of E3 ligases and their diverse substrate recognition mechanisms.
  • To discuss the therapeutic potential of targeting E3 ligases for human diseases.

Main Methods:

  • Literature review of recent structure-function studies on ubiquitin E3 ligases.
  • Synthesis of current knowledge on E3 ligase catalysis, activation, and regulation.
  • Analysis of emerging discoveries in E3 ligase classes and substrate binding.

Main Results:

  • Significant progress has been made in elucidating the mechanistic details of E3 ligase function.
  • New classes of E3 ligases and novel substrate recognition strategies have been identified.
  • The understanding of E3 ligase regulation has deepened considerably.

Conclusions:

  • Current research provides comprehensive insights into the diverse functions and regulation of ubiquitin E3 ligases.
  • The detailed knowledge of E3 ligase mechanisms supports the development of targeted therapeutics.
  • Targeting E3 ligases offers a promising strategy for treating various human diseases.