Related Experiment Video
Updated: Aug 6, 2026

07:30
Measuring Synaptic Vesicle Endocytosis in Cultured Hippocampal Neurons
Published on: September 4, 2017
The calcineurin-dynamin 1 complex as a calcium sensor for synaptic vesicle endocytosis
M M Lai1, J J Hong, A M Ruggiero
1Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
The Journal of Biological Chemistry
|September 3, 1999
Summary
Researchers discovered calcineurin and dynamin 1 form a calcium-dependent complex, acting as a calcium sensor to facilitate synaptic vesicle endocytosis.
Area of Science:
- Neuroscience
- Cell Biology
- Biochemistry
Background:
- Synaptic vesicle exocytosis is calcium-dependent, utilizing synaptotagmin as the calcium sensor.
- The calcium dependence of synaptic vesicle endocytosis has been proposed, but a specific sensor remained unidentified.
Purpose of the Study:
- To identify a calcium-sensing mechanism involved in synaptic vesicle endocytosis.
- To investigate the role of calcineurin and dynamin 1 in calcium-dependent endocytosis.
Main Methods:
- Investigated the physical association between calcineurin and dynamin 1.
- Quantified the calcium dependence of the calcineurin-dynamin 1 interaction using EC50 values.
- Assessed the impact of disrupting this interaction on clathrin-mediated endocytosis.
Main Results:
- A calcium-dependent physical association was identified between calcineurin and dynamin 1.
- The calcineurin-dynamin 1 interaction exhibits a calcium dependency with an EC50 between 0.1-0.4 microM.
- Disruption of the calcineurin-dynamin 1 complex formation inhibited clathrin-mediated endocytosis.
Conclusions:
- The calcium-dependent formation of the calcineurin-dynamin 1 complex serves as a novel calcium sensor for synaptic endocytosis.
- This complex, when localized with other endocytic proteins, facilitates the calcium-sensing process during synaptic vesicle recycling.
More Related Videos
Related Concept Videos
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...
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...
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...
SNAREs and Membrane Fusion
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.
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
SNAREs exist in pairs that symmetrically interact and catalyze the fusion of the lipid bilayers in vesicle and target organelle. v-SNARE in the vesicle membrane are single polypeptide chains that bind to a complementary t-SNARE, composed of 2...
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...
Calmodulin-dependent Signaling
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...

