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Related Concept Videos

ER Retrieval Pathway01:45

ER Retrieval Pathway

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In the secretory pathway, vesicles transport proteins from one cellular compartment to another in forward transport to deliver the protein to its correct location. Occasionally, misfolded proteins and incorrect proteins escape their original compartments, and a retrieval pathway is used to return the escaped proteins to their original compartment.
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Overview of Secretory Vesicles01:33

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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.
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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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Pinching-off of Coated Vesicles01:32

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Vesicle budding is orchestrated by distinct cytosolic proteins such as adaptor proteins, coat proteins, and GTPases. To initiate vesicle budding, membrane-bending proteins containing crescent-shaped BAR domains bind to the lipid heads in the bilayer and distort the membrane to form a protein-coated vesicle bud. Adaptors proteins such as AP2 for clathrin-coated vesicles can nucleate on the deformed membrane. Finally, coat proteins such as clathrin or COPI and COPII assemble into a coat forming...
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Vesicular Tubular Clusters01:45

Vesicular Tubular Clusters

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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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Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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Vesicles incorporate different coat protein subunits in different cell locations, which changes the properties of the coat, such as the shape and geometry of the transport vesicles. Thus, vesicle coat proteins also play a significant role in cargo selection.
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Related Experiment Video

Updated: Dec 3, 2025

Measuring Synaptic Vesicle Endocytosis in Cultured Hippocampal Neurons
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Measuring Synaptic Vesicle Endocytosis in Cultured Hippocampal Neurons

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PICK1 Controls Activity-Dependent Synaptic Vesicle Cargo Retrieval.

Xuan Ling Hilary Yong1, Michael A Cousin2, Victor Anggono1

  • 1Clem Jones Centre for Ageing Dementia Research, Queensland Brain Institute, The University of Queensland, Brisbane, QLD 4072, Australia.

Cell Reports
|October 28, 2020
PubMed
Summary
This summary is machine-generated.

Protein interacting with C-kinase 1 (PICK1) is essential for efficient synaptic vesicle recycling. Loss of PICK1 function slows endocytosis and disrupts synaptic protein localization, impacting glutamate release in central synapses.

Keywords:
AP-2BAR domainPDZ domainPICK1endocytosisglutamate releasesynaptic transmissionsynaptic vesicle recyclingsynaptic vesicle retrievalsynaptic vesicles

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Area of Science:

  • Neuroscience
  • Cell Biology
  • Synaptic Physiology

Background:

  • Efficient synaptic vesicle (SV) recycling is vital for sustained synaptic transmission.
  • Protein interacting with C-kinase 1 (PICK1) is known to regulate postsynaptic glutamate receptor trafficking.
  • PICK1's presynaptic role in SV recycling was previously uncharacterized.

Purpose of the Study:

  • To investigate the role of PICK1 in regulating presynaptic SV recycling.
  • To determine the molecular mechanisms underlying PICK1's function in SV endocytosis.

Main Methods:

  • Utilized primary hippocampal neurons.
  • Employing PICK1 loss-of-function and knockdown models.
  • Investigated SV protein localization and endocytosis kinetics during high-frequency stimulation.

Main Results:

  • PICK1 loss of function selectively slowed SV endocytosis kinetics.
  • PICK1 knockdown led to mislocalization of synaptophysin and vGlut1.
  • A functional PDZ domain and interaction with AP-2 were crucial for synaptophysin targeting and clustering.

Conclusions:

  • PICK1 is a key regulator of presynaptic SV recycling in central synapses.
  • PICK1's interaction with AP-2 is essential for efficient SV endocytosis and sustained glutamate release.