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Related Concept Videos

Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

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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.
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Vesicular Tubular Clusters01:45

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After budding out from the ER membrane, some COPII vesicles lose their coat and fuse with one another to form larger vesicles and interconnected tubules called vesicular tubular clusters or VTCs. These clusters constitute a compartment at the ER-Golgi interface known as ERGIC (Endoplasmic Reticulum Golgi Intermediate Compartment). The ERGIC is a mobile membrane-bound cargo transport system that sorts proteins secreted from ER and delivers them to the Golgi.
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Overview of Secretory Vesicles01:33

Overview of Secretory Vesicles

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Secretory vesicles, also known as dense core vesicles (DCVs), are membrane-bound vesicles that transport secretory proteins, such as hormones or neurotransmitters. Regulated secretory vesicles transport proteins from the trans-Golgi network to the exterior of the cell. Proteins present in regulated secretory vesicles are required to be rapidly exocytosed in large amounts upon a specific stimulus.
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...
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Nuclear Export01:42

Nuclear Export

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The nucleus restricts several proteins within and allows others to pass. The restricted proteins possess a nuclear retention sequence or NRS, anchoring them to the nuclear lamins and preventing their transport to the cytosol. The non-restricted proteins, after their synthesis, are transported to their site of action, such as the cytosol or other organelles, with the help of nuclear export signals or NES.
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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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Transport Across the Golgi01:26

Transport Across the Golgi

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While it is unclear how molecules move between adjacent Golgi cisternae, it is apparent that the molecules move from cis- cisterna, the entry face, to the trans- cisterna, the exit face. Experiments initially suggested vesicles that bud from one cisterna and fuse with the next cisterna to transport proteins between the cisternae. This vesicular transport model describes the Golgi apparatus as a relatively static structure with a unique enzyme composition in each cisterna. Molecules are...
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Quantitative Approaches for Scoring in vivo Neuronal Aggregate and Organelle Extrusion in Large Exopher Vesicles in C. elegans
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Neurons Export Extracellular Vesicles Enriched in Cysteine String Protein and Misfolded Protein Cargo.

Jingti Deng1, Carolina Koutras1, Julien Donnelier1

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Cysteine string protein alpha (CSPα) facilitates the removal of toxic proteins from neurons via extracellular vesicles (EVs), maintaining synaptic proteostasis and offering a potential therapeutic target for neurodegenerative diseases.

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • Synaptic transmission fidelity relies on protein machinery integrity.
  • Misfolded proteins accumulate, causing neuronal dysfunction.
  • Cysteine string protein alpha (CSPα) is crucial for synaptic proteostasis.

Purpose of the Study:

  • Investigate the role of CSPα in neuronal extracellular vesicle (EV) function.
  • Determine if CSPα mediates the export of disease-associated misfolded proteins.
  • Explore CSPα as a therapeutic target for neurodegenerative diseases.

Main Methods:

  • Studied CSPα presence in exported neuronal vesicles.
  • Co-expressed CSPα with disease-associated proteins (72Q huntingtin, SOD-1G93A).
  • Analyzed protein export via EVs and the effect of resveratrol.

Main Results:

  • Neurons export CSPα in extracellular vesicles (EVs).
  • CSPα facilitates the export of misfolded 72Q huntingtin and SOD-1G93A via EVs.
  • Resveratrol reduces CSPα-mediated export of 72Q huntingtin.

Conclusions:

  • CSPα-mediated EV export removes toxic proteins, maintaining synaptic proteostasis.
  • CSPα plays a key role in clearing misfolded proteins at the synapse.
  • CSPα is a potential therapeutic target for neurodegenerative conditions.