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Related Concept Videos

SNAREs and Membrane Fusion01:43

SNAREs and Membrane Fusion

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Once a transport vesicle has recognized its target organelle, the vesicular membrane needs to fuse with the target membrane to unload the cargo. Transmembrane proteins called SNAREs present on organelle membranes and their vesicles, mediate vesicle fusion.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
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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.
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
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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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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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Nuclear Protein Sorting01:34

Nuclear Protein Sorting

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Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
Proteins targeted to the nucleus carry nuclear localization signals or NLS recognized by import receptors in the cytosol. Similarly, proteins with nuclear export signals are recognized by export receptors. Import and export receptors are...
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Export of Misfolded Proteins out of the ER01:32

Export of Misfolded Proteins out of the ER

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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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Related Experiment Video

Updated: Oct 15, 2025

Studying Pre-formed Fibril Induced &#945;-Synuclein Accumulation in Primary Embryonic Mouse Midbrain Dopamine Neurons
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Studying Pre-formed Fibril Induced α-Synuclein Accumulation in Primary Embryonic Mouse Midbrain Dopamine Neurons

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SNARE Proteins Mediate α-Synuclein Secretion via Multiple Vesicular Pathways.

Xiaofang Zhao1,2, Yuan Guan1,3, Fengwei Liu1

  • 1Beijing Institute of Brain Disorders, Laboratory of Brain Disorders, Ministry of Science and Technology, Collaborative Innovation Center for Brain Disorders, Capital Medical University, Beijing, 100069, China.

Molecular Neurobiology
|October 27, 2021
PubMed
Summary

Pathological alpha-synuclein (α-syn) secretion, key to synucleinopathies, is SNARE-dependent. It involves multiple vesicles, including autophagosomes and lysosomes, and is regulated by the autophagy-lysosome pathway.

Keywords:
AutophagosomeEndosomeExocytosisLysosomeSNAREα-Synuclein

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Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation
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Technique for Intranasal Administration of &#945;-Synuclein Aggregates
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Technique for Intranasal Administration of α-Synuclein Aggregates

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Exogenous Administration of Microsomes-associated Alpha-synuclein Aggregates to Primary Neurons As a Powerful Cell Model of Fibrils Formation
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Technique for Intranasal Administration of &#945;-Synuclein Aggregates
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Technique for Intranasal Administration of α-Synuclein Aggregates

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • Cell-to-cell transmission of pathological alpha-synuclein (α-syn) is crucial for synucleinopathies.
  • α-syn secretion is Ca2+-dependent and uses unconventional exocytosis.
  • The specific SNARE proteins and vesicles involved in α-syn secretion are not fully understood.

Purpose of the Study:

  • To elucidate the SNARE protein requirements for α-syn secretion.
  • To identify the vesicular pathways mediating α-syn secretion.
  • To investigate the role of the autophagy-lysosome pathway in α-syn secretion.

Main Methods:

  • Systematic knockdown of Q-SNAREs and R-SNAREs in SH-SY5Y cells.
  • Super-resolution microscopy in rat primary cortical neurons.
  • Co-localization studies with LC3 and analysis of autophagy-lysosome pathway regulation.

Main Results:

  • α-syn secretion is SNARE-dependent, primarily involving syntaxin 4 (STX4) and synaptosomal-associated protein 23 (SNAP23).
  • Vesicle-associated membrane proteins 3, 7, and 8 (VAMP3, VAMP7, VAMP8) are involved in α-syn secretion.
  • α-syn localizes to endosomes, lysosomes, and autophagosomes, with strong co-localization with LC3, indicating a link to autophagy.

Conclusions:

  • α-syn secretion is SNARE-dependent and utilizes multiple vesicular pathways.
  • The autophagy-lysosome pathway significantly regulates α-syn secretion.
  • These findings provide insights into the molecular mechanisms of α-syn propagation in synucleinopathies.