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Related Concept Videos

Fusion of Secretory Vesicles with the Plasma Membrane01:26

Fusion of Secretory Vesicles with the Plasma Membrane

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...
Chemical Synapses01:26

Chemical Synapses

Chemical synapses are specialized sites between two neurons or between a neuron and a non-neuronal cell like a muscle, glandular or sensory cell.
Because chemical synapses depend on the release of neurotransmitter molecules from synaptic vesicles to pass on their signal, there is an approximately one millisecond delay between when the axon potential reaches the presynaptic terminal and when the neurotransmitter leads to opening of postsynaptic ion channels. Additionally, this signaling is...
Chemical Synapses01:26

Chemical Synapses

Chemical synapses are specialized sites between two neurons or between a neuron and a non-neuronal cell like a muscle, glandular or sensory cell.
Because chemical synapses depend on the release of neurotransmitter molecules from synaptic vesicles to pass on their signal, there is an approximately one millisecond delay between when the axon potential reaches the presynaptic terminal and when the neurotransmitter leads to opening of postsynaptic ion channels. Additionally, this signaling is...
Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

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...
Synaptic Signaling01:12

Synaptic Signaling

Neurons communicate at synapses, or junctions, to excite or inhibit the activity of other neurons or target cells, such as muscles. Synapses may be chemical or electrical.
Synaptic Signaling01:09

Synaptic Signaling

Neurons communicate at synapses, or junctions, to excite or inhibit the activity of other neurons or target cells, such as muscles. Synapses may be chemical or electrical.
Most synapses are chemical, meaning an electrical impulse or action potential spurs the release of chemical messengers called neurotransmitters. The neuron sending the signal is called the presynaptic neuron, and the neuron receiving the signal is the postsynaptic neuron.
The presynaptic neuron fires an action potential that...

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Related Experiment Video

Updated: Jun 24, 2026

Measuring Synaptic Vesicle Endocytosis in Cultured Hippocampal Neurons
07:30

Measuring Synaptic Vesicle Endocytosis in Cultured Hippocampal Neurons

Published on: September 4, 2017

Synaptic vesicle recycling at CNS snapses without AP-2.

Sung Hyun Kim1, Timothy A Ryan

  • 1Department of Biochemistry, Weill Cornell Medical College, New York, New York 10065, USA.

The Journal of Neuroscience : the Official Journal of the Society for Neuroscience
|March 27, 2009
PubMed
Summary

Synaptic vesicle (SV) protein recycling is essential for neurotransmission. Adaptor complex AP-2 is crucial for endocytosis, but AP-1 can compensate, ensuring SV proteins are still internalized.

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • Synaptic vesicles (SVs) internalize transmembrane proteins after neurotransmitter release.
  • Mechanisms for SV protein reassembly into vesicles post-exocytosis are unclear.
  • Adaptor complex AP-2 is a key clathrin-associated protein for plasma membrane cargo recognition.

Purpose of the Study:

  • Investigate the role of adaptor complex AP-2 in synaptic vesicle endocytosis.
  • Determine if AP-2 is essential for the internalization of SV transmembrane proteins.
  • Explore compensatory mechanisms for SV protein recycling in the absence of AP-2.

Main Methods:

  • Utilized shRNA-mediated knockdown to reduce AP-2 complex levels in primary neurons.
  • Employed simultaneous expression of shRNA and pHluorin-tagged SV components.
  • Assessed endocytosis kinetics and sensitivity to ARF-GEF inhibitor BFA.

Main Results:

  • AP-2 complex reduction by ~96% significantly slowed, but did not block, endocytosis of major SV proteins.
  • Adaptor complex AP-1 substituted for AP-2, leading to BFA-sensitive internalization kinetics.
  • Simultaneous removal of AP-1 and AP-2 resulted in slowed but functional endocytosis.

Conclusions:

  • Synaptic vesicle proteins are endocytosed even without AP-2.
  • AP-1 can functionally compensate for AP-2 in SV protein recycling.
  • Synaptic vesicle recycling remains operational despite the absence of AP-2.