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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...
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...
Proteins: From Genes to Degradation02:11

Proteins: From Genes to Degradation

Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA molecules by RNA...
Proteins: From Genes to Degradation02:11

Proteins: From Genes to Degradation

Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick.  Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA molecules by RNA...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...

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Related Experiment Video

Updated: Jun 6, 2026

Quantifying Subcellular Ubiquitin-proteasome Activity in the Rodent Brain
09:25

Quantifying Subcellular Ubiquitin-proteasome Activity in the Rodent Brain

Published on: May 21, 2019

Protein degradation and memory formation.

Diasynou Fioravante1, John H Byrne

  • 1Department of Neurobiology and Anatomy, W.M. Keck Center for the Neurobiology of Learning and Memory, The University of Texas Medical School at Houston, Houston, TX 77030, USA.

Brain Research Bulletin
|November 17, 2010
PubMed
Summary
This summary is machine-generated.

Protein degradation and ubiquitination are crucial for long-term memory consolidation. This process converts short-term memories into enduring forms by altering neuronal properties and synaptic connections.

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cognitive Science

Background:

  • Long-term memory formation involves converting short-term memory traces into stable forms.
  • Memory consolidation is linked to protein synthesis altering neuronal biophysics and synaptic strength.

Purpose of the Study:

  • To discuss recent findings on the roles of protein degradation and ubiquitination in memory consolidation.
  • To explore the involvement of these processes in synaptic plasticity, learning, and memory.

Main Methods:

  • Review of recent scientific literature.
  • Analysis of studies investigating protein synthesis and degradation pathways.
  • Examination of ubiquitination's role in synaptic plasticity.

Main Results:

  • Protein degradation is essential for memory consolidation, alongside protein synthesis.
  • Ubiquitination plays a significant role in regulating synaptic plasticity.
  • These processes are integral to the molecular mechanisms underlying learning and memory.

Conclusions:

  • Both protein synthesis and degradation are required for effective memory consolidation.
  • Ubiquitination and protein degradation are critical molecular mechanisms for synaptic plasticity and memory formation.