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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.
Protein degradation plays two important roles in the cells. It helps to protect cells from misfolded or damaged proteins before they lead to a...
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Tail-anchoring of Proteins in the ER Membrane01:45

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Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
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Export of Misfolded Proteins out of the ER01:32

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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...
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Covalently Linked Protein Regulators02:04

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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 the Unfolded Protein Response01:31

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Inositol-requiring kinase one or IRE1 is the most conserved eukaryotic unfolded protein response (UPR) receptor. It is a type I transmembrane protein kinase receptor with a distinctive site-specific RNase activity. As the binding mechanics of the misfolded proteins with the N-terminal domain of IRE-1 are unclear, three binding models — direct, indirect, and allosteric -- are proposed for receptor activation. Nevertheless, it is known that once a misfolded protein associates with IRE1, it...
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Enzyme-linked Receptors01:00

Enzyme-linked Receptors

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Enzyme-linked receptors are proteins that act as both receptor and enzyme, activating multiple intracellular signals. This is a large group of receptors that include the receptor tyrosine kinase (RTK) family. Many growth factors and hormones bind to and activate the RTKs.
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Related Experiment Video

Updated: Jul 5, 2025

A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues
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A Time-Efficient Fluorescence Spectroscopy-Based Assay for Evaluating Actin Polymerization Status in Rodent and Human Brain Tissues

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The E3 ubiquitin ligase TRIM9 regulates synaptic function and actin dynamics.

Laura E McCormick1, Elliot B Evans1, Natalie K Barker2,3

  • 1Department of Cell Biology and Physiology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599.

Biorxiv : the Preprint Server for Biology
|January 23, 2024
PubMed
Summary

The E3 ubiquitin ligase TRIM9 regulates dendritic spine development and function. TRIM9 is essential for synaptic responses to netrin, controlling cytoskeletal dynamics and neuronal firing rates.

Keywords:
TRIM9dendritic spinefilopodiasynapse

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In Vitro Analysis of E3 Ubiquitin Ligase Function
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Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • Neuronal development involves dynamic filopodia maturing into dendritic spines.
  • Extracellular cues influence spine morphology and synaptic function.
  • The E3 ubiquitin ligase TRIM9 previously regulated early neuronal development.

Approach:

  • TRIM9 localization to dendritic filopodia and spines was investigated.
  • The impact of TRIM9 loss on synaptic responses to netrin was assessed.
  • Proteomic analysis identified TRIM9's role in the postsynaptic density (PSD) and actin cytoskeleton.

Key Points:

  • TRIM9 localizes to the PSD in dendritic spines and is required for netrin response.
  • Loss of TRIM9 disrupts netrin-induced actin accumulation in spines.
  • TRIM9 deficiency alters PSD proteome and synaptic receptors.

Conclusions:

  • TRIM9 regulates cytoskeletal dynamics within dendritic spines.
  • TRIM9 is essential for synaptic netrin signaling and neuronal function.
  • TRIM9 controls netrin-dependent increases in neuronal firing rates.