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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...
Assembly of Complex Microtubule Structures01:32

Assembly of Complex Microtubule Structures

Complex microtubule structures are present in resting cells and in dividing cells. In resting cells, they are responsible for maintaining the cellular architecture, tracks for intracellular transport, positioning of organelles, assembly of cilia and flagella. They mediate the bipolar spindle assembly for chromosomal segregation and positioning of the cell division plate in dividing cells. The formation of microtubule complex structures depends on the cell type, cell stage, and cell function.
The Proteasome Structure01:17

The Proteasome Structure

The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

Proteins and neurotransmitters in secretory vesicles can be released from a cell upon vesicle docking, priming, and fusion with the plasma membrane. Vesicles are docked and primed in preparation for the quick exocytosis of their contents in response to a stimulus. The fusion process is mainly carried out by a SNAP Receptor or SNARE complex, consisting of synaptobrevin, syntaxin-1, and SNAP-25.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...

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Related Experiment Video

Updated: May 13, 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

Breaking it down: the ubiquitin proteasome system in neuronal morphogenesis.

Andrew M Hamilton1, Karen Zito

  • 1Center for Neuroscience, University of California Davis, 1544 Newton Court, Davis, CA 95618, USA. anhamilton@ucdavis.edu

Neural Plasticity
|March 12, 2013
PubMed
Summary

The ubiquitin-proteasome system (UPS) regulates diverse neuronal functions. This study highlights the UPS

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Genetic Manipulation of Cerebellar Granule Neurons In Vitro and In Vivo to Study Neuronal Morphology and Migration

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In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
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Last Updated: May 13, 2026

Quantifying Subcellular Ubiquitin-proteasome Activity in the Rodent Brain
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Genetic Manipulation of Cerebellar Granule Neurons In Vitro and In Vivo to Study Neuronal Morphology and Migration
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Genetic Manipulation of Cerebellar Granule Neurons In Vitro and In Vivo to Study Neuronal Morphology and Migration

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In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones
11:36

In Vitro Ubiquitination and Deubiquitination Assays of Nucleosomal Histones

Published on: July 25, 2019

Area of Science:

  • Neuroscience
  • Cell Biology
  • Biochemistry

Background:

  • The ubiquitin-proteasome system (UPS) is crucial for protein degradation and cellular process regulation.
  • Ubiquitination impacts protein function, localization, and endocytosis beyond degradation.
  • The UPS is vital in neurons for maintaining synaptic protein homeostasis.

Purpose of the Study:

  • To review recent advances in understanding the UPS' role in neuronal development.
  • To focus on the UPS' regulation of axon, dendrite, and dendritic spine morphogenesis.
  • To emphasize the involvement of E3 ubiquitin ligases and their targets.

Main Methods:

  • Literature review of recent studies on the UPS in neuronal morphogenesis.
  • Analysis of research focusing on E3 ubiquitin ligases and their substrates.
  • Synthesis of findings on ubiquitination's impact on neuronal structure development.

Main Results:

  • The UPS regulates key neuronal functions including synaptic strength and plasticity.
  • Specific E3 ubiquitin ligases and their targets are critical for axon and dendrite development.
  • Ubiquitination controls the morphogenesis of neuronal structures like dendritic spines.

Conclusions:

  • The UPS is a central regulator of neuronal morphogenesis.
  • E3 ubiquitin ligases are key players in directing neuronal structure formation.
  • Further research into the UPS' role in neurodevelopment is warranted.