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Related Concept Videos

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

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...
Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

After folding, the ER assesses the quality of secretory and membrane proteins. The correctly folded proteins are cleared by the calnexin cycle for transport to their final destination, while misfolded proteins are held back in the ER lumen. The ER chaperones attempt to unfold and refold the misfolded proteins but sometimes fail to achieve the correct native conformation. Such terminally misfolded proteins are then exported to the cytosol by ER-associated degradation or ERAD pathway for...
Intralumenal Vesicles and Multivesicular Bodies01:38

Intralumenal Vesicles and Multivesicular Bodies

Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...
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.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

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Ubiquitin Chain Analysis by Parallel Reaction Monitoring
08:33

Ubiquitin Chain Analysis by Parallel Reaction Monitoring

Published on: June 17, 2020

Constructing and decoding unconventional ubiquitin chains.

Christian Behrends1, J Wade Harper

  • 1Institute of Biochemistry II, Goethe University School of Medicine, Frankfurt, Germany.

Nature Structural & Molecular Biology
|May 5, 2011
PubMed
Summary
This summary is machine-generated.

Ubiquitin chains regulate cell signaling. This review explores Lys11-linked and linear (Met1-linked) ubiquitin chains, detailing their assembly and roles in immunity and cell division.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Background:

  • The ubiquitin system extensively utilizes diverse chain linkages to control cellular signaling networks.
  • Lys48-linked and Lys63-linked ubiquitin chains are well-characterized for their roles in protein degradation and molecular assembly, respectively.
  • Understanding unconventional ubiquitin chain linkages is crucial for deciphering complex cellular processes.

Purpose of the Study:

  • To review recent advancements in understanding the machinery and mechanisms controlling the assembly of Lys11-linked and linear (Met1-linked) ubiquitin chains.
  • To describe current models for the functional roles of these unconventional ubiquitin chains in cellular signaling.
  • To highlight the importance of these linkages in immune signaling and cell-cycle control.

Main Methods:

  • Literature review of recent research on ubiquitin chain assembly and function.
  • Summarization of experimental findings elucidating the mechanisms of Lys11-linked and linear ubiquitin chain formation.
  • Analysis of current models for the biological roles of these specific ubiquitin chain types.

Main Results:

  • Recent studies have begun to elucidate the specific enzymes and pathways involved in forming Lys11-linked and linear ubiquitin chains.
  • Emerging evidence suggests distinct roles for these unconventional chains in regulating immune responses and cell cycle progression.
  • The decoding of these unique chain linkages by specific binding proteins is an active area of investigation.

Conclusions:

  • Lys11-linked and linear ubiquitin chains represent critical, yet less understood, regulatory mechanisms within the ubiquitin system.
  • Further research into the assembly and function of these chains will provide deeper insights into immune signaling and cell-cycle control.
  • The discovery of diverse ubiquitin chain linkages expands our understanding of post-translational modifications and their impact on cellular networks.