Kiss-and-run, collapse and 'readily retrievable' vesicles
Silvio O Rizzoli1, Reinhard Jahn
1Department of Neurobiology, Max-Planck-Institute for Biophysical Chemistry, 37077 Göttingen, Germany.
Traffic (Copenhagen, Denmark)
|July 25, 2007
Summary
Synaptic vesicle recycling occurs via kiss-and-run or full fusion. Both models demonstrate high fidelity, with readily retrievable vesicles enabling fast endocytosis for full fusion, minimizing efficiency differences.
Area of Science:
- Neuroscience
- Cell Biology
- Biochemistry
Background:
- Synaptic vesicle recycling is crucial for neurotransmission.
- Two models, kiss-and-run and full fusion, are debated for vesicle recycling mechanisms.
- Kiss-and-run was hypothesized to be faster and more faithful than full fusion.
Purpose of the Study:
- To review recent evidence supporting both synaptic vesicle recycling models.
- To compare the efficiency and fidelity of kiss-and-run versus full fusion.
- To elucidate the role of readily retrievable vesicles in synaptic vesicle recycling.
Main Methods:
- Literature review of experimental evidence for synaptic vesicle recycling models.
- Analysis of data comparing kiss-and-run and full fusion mechanisms.
- Conceptual analysis of vesicle fusion pore dynamics and endocytosis.
Main Results:
- Both kiss-and-run and full fusion mechanisms support high-fidelity vesicle recycling.
- Full fusion, aided by readily retrievable vesicles, can trigger rapid endocytosis.
- Efficiency differences between the two models are less pronounced than previously thought.
Conclusions:
- Both kiss-and-run and full fusion are viable and high-fidelity mechanisms for synaptic vesicle recycling.
- The presence of readily retrievable vesicles enhances the speed of full fusion-mediated endocytosis.
- The debate on the efficiency of synaptic vesicle recycling models is nuanced by the interplay of different mechanisms.
Related Concept Videos
Pinching-off of Coated Vesicles
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...
Clathrin Coated Vesicles
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...
COP Coated Vesicles
Membrane-enclosed structures called vesicles transport proteins and lipids across the cell. The vesicles derive their cargo from the plasma membrane, Golgi, ER, or endosome. Coated vesicles are spherical, protein-coated carriers with a 50–100 nm diameter that mediate bidirectional transport between the ER and the Golgi. The distribution of proteins between the ER and Golgi complex is dynamic and is maintained by different coated vesicles. Their formation is driven by the assembly of different...
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...
With the help of motor proteins such...
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...
In 1993, Jim Rothman proposed that the antiparallel pairing of vesicular and transmembrane SNAREs, or...
Overview of Secretory Vesicles
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...
Various proteins regulate the aggregation of molecules inside the secretory vesicles. Chromogranins...


