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Related Concept Videos

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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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.
With the help of motor proteins such...
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Fusion of Secretory Vesicles with the Plasma Membrane01:26

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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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SNAREs and Membrane Fusion01:43

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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.
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Overview of Protein Sorting and Transport01:45

Overview of Protein Sorting and Transport

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Eukaryotic cells have different membrane-bound organelles with distinct protein requirements. The process by which proteins are targeted to a specific organelle is called protein sorting.
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Clathrin Coated Vesicles01:12

Clathrin Coated Vesicles

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Clathrin-coated vesicles use endocytosis to transport receptors and lysosomal hydrolases from the Golgi to the lysosome in the late secretory pathway. Clathrin-mediated endocytosis was the first described endocytic process, and Clathrin-coated vesicles remain one of the most well-studied transport vesicles. The molecular machinery that generates clathrin-coated vesicles comprises over 50 proteins that precisely coordinate vesicle formation. Cell surface receptors concentrated in indented sites...
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Related Experiment Video

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Measuring Synaptic Vesicle Endocytosis in Cultured Hippocampal Neurons
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Synaptic vesicle morphology: a case of protein sorting?

Kumud R Poudel1, Jihong Bai1

  • 1Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, WA, USA; Department of Biochemistry, University of Washington, Seattle, WA, USA.

Current Opinion in Cell Biology
|February 18, 2014
PubMed
Summary

Synaptic vesicle (SV) morphology is maintained by adaptor proteins that sort cargo. Disruptions in these proteins alter SV size and architecture, impacting neurotransmitter storage and release.

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Biochemistry

Background:

  • Synaptic vesicles (SVs) store and release neurotransmitters at nerve terminals.
  • SV morphology is remarkably uniform despite continuous recycling via exocytosis and endocytosis.
  • Clathrin adaptor proteins are implicated in cargo sorting and SV morphology maintenance.

Purpose of the Study:

  • To review the relationship between adaptor proteins and synaptic vesicle size.
  • To highlight the impact of protein sorting on synaptic vesicle architecture.
  • To explore the regulatory network maintaining SV morphology.

Main Methods:

  • Literature review of studies on synaptic vesicle recycling and protein sorting.
  • Analysis of the roles of clathrin, adaptor proteins, and accessory proteins.
  • Examination of the influence of SV cargoes and lipid composition.

Main Results:

  • Disruption of clathrin adaptor proteins leads to impaired cargo sorting.
  • Alterations in protein sorting pathways affect synaptic vesicle morphology and size.
  • A complex network involving molecular players maintains SV architecture.

Conclusions:

  • Adaptor proteins are crucial for maintaining synaptic vesicle uniformity.
  • Protein sorting mechanisms significantly impact synaptic vesicle architecture.
  • A coordinated network of molecular components ensures stable SV morphology.