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Related Concept Videos

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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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Rab GTPases act in a regulated cascade during membrane fusion, helping the lipid bilayers mix. The Rab family of proteins are active when bound to GTP, and inactive when bound to GDP. Hence, they act as guanine nucleotide-dependent molecular switches. Rab-GTP recognizes and binds to long or short-range tethering proteins to capture the target vesicle. These tethers coordinate with SNAREs on the vesicle and the target membrane to assemble the trans SNARE complex that locks the mixing bilayers.
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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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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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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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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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Related Experiment Video

Updated: Nov 10, 2025

An Optical Assay for Synaptic Vesicle Recycling in Cultured Neurons Overexpressing Presynaptic Proteins
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An Optical Assay for Synaptic Vesicle Recycling in Cultured Neurons Overexpressing Presynaptic Proteins

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Rab2 regulates presynaptic precursor vesicle biogenesis at the trans-Golgi.

Torsten W B Götz1, Dmytro Puchkov2, Veronika Lysiuk1

  • 1Freie Universität Berlin, Institute for Biology and Genetics, Berlin, Germany.

The Journal of Cell Biology
|April 6, 2021
PubMed
Summary
This summary is machine-generated.

Small GTPase Rab2 is crucial for presynaptic protein transport. Its deficiency causes protein buildup in the cell body and impaired neurotransmission due to disrupted Golgi export.

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Last Updated: Nov 10, 2025

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Measuring Synaptic Vesicle Endocytosis in Cultured Hippocampal Neurons
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Area of Science:

  • Neuroscience
  • Cell Biology
  • Molecular Biology

Background:

  • Efficient transport of presynaptic components from neuronal cell bodies to terminals is vital for synaptogenesis and neurotransmission.
  • The molecular mechanisms governing the assembly of these presynaptic precursors within the cell body are not fully understood.

Purpose of the Study:

  • To investigate the role of the small GTPase Rab2 in the somatic assembly and transport of presynaptic proteins.
  • To elucidate the molecular pathway controlling the export of active zone and synaptic vesicle proteins from the trans-Golgi network.

Main Methods:

  • Utilized genetic mutants of the small GTPase Rab2 in a neuronal model.
  • Analyzed the localization of active zone and synaptic vesicle proteins using cell biology techniques.
  • Performed biochemical fractionation to characterize ectopic protein accumulations.
  • Investigated the genetic relationship between Rab2 and Arl8.

Main Results:

  • Rab2 mutants exhibited accumulation of active zone and synaptic vesicle proteins in the neuronal cell body at the trans-Golgi.
  • Synaptic terminals in Rab2 mutants were depleted of these essential presynaptic proteins, leading to neurotransmission deficits.
  • Ectopic accumulations comprised heterogeneous vesicles and tubules, with distinct segregation of active zone/synaptic vesicle proteins and LAMP1.
  • Rab2 was found to act upstream of Arl8, a lysosomal adaptor involved in axonal precursor export.

Conclusions:

  • A Golgi-associated pathway for presynaptic precursor biogenesis has been identified.
  • This pathway relies on a Rab2-dependent protein export and sorting mechanism at the trans-Golgi.
  • Rab2 plays a critical role in regulating the transport of essential synaptic components, impacting overall neurotransmission.