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Related Concept Videos

The Proteasome01:13

The Proteasome

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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.
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...
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The Proteasome Structure01:17

The Proteasome Structure

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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...
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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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Regulation of Nuclear Protein Sorting01:45

Regulation of Nuclear Protein Sorting

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Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...
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Protein Complex Assembly

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Quantifying Subcellular Ubiquitin-proteasome Activity in the Rodent Brain
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Proteasome cap particle regulates synapses.

Fulya Türker1, Seth S Margolis1,2

  • 1Department of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD, USA.

Science (New York, N.Y.)
|May 25, 2023
PubMed
Summary
This summary is machine-generated.

The free 19S proteasome cap particle

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Biology

Background:

  • Synaptic transmission is crucial for neuronal communication.
  • The ubiquitin-proteasome system regulates protein turnover.
  • The 19S proteasome cap particle plays a role in protein degradation.

Purpose of the Study:

  • To investigate the role of the free 19S proteasome cap particle in synaptic transmission.
  • To explore the deubiquitylation activity of the free 19S proteasome cap particle at synapses.

Main Methods:

  • Biochemical assays to measure deubiquitylation activity.
  • Electrophysiological recordings to assess synaptic transmission.
  • Immunofluorescence and Western blotting to detect protein localization and levels.

Main Results:

  • The free 19S proteasome cap particle exhibits deubiquitylation activity at synapses.
  • This deubiquitylation activity modulates synaptic transmission.
  • Specific deubiquitylation targets at the synapse were identified.

Conclusions:

  • Free 19S proteasome cap particle-mediated deubiquitylation is a novel regulator of synaptic function.
  • Targeting this pathway may offer therapeutic strategies for neurological disorders.