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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...
Coat Assembly and GTPases01:33

Coat Assembly and GTPases

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.
Coat assembly depends on the local availability of phosphatidylinositol phosphates or PIPs and GTP-binding proteins. Adaptor proteins, which link the coat proteins to the membrane, bind to these PIPs and play a crucial role in controlling...
SNAREs and Membrane Fusion01:43

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...
Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
Rab Proteins01:14

Rab Proteins

Rab proteins constitute the largest family of monomeric GTPases, of which 70 members are present in humans. Rab proteins and their effectors regulate consecutive stages of vesicle transport such as vesicle transport, docking, and fusion to the correct recipient membrane.
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
GPCRs Regulate Adenylyl Cylase Activity01:09

GPCRs Regulate Adenylyl Cylase Activity

Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of cells.
Two...

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Related Experiment Video

Updated: Jul 4, 2026

Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time
08:33

Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time

Published on: March 11, 2021

Synaptic vesicle protein 2 binds adenine nucleotides.

Jia Yao1, Sandra M Bajjalieh

  • 1Department of Pharmacology, University of Washington, 1959 NE Pacific Street, Seattle, WA 98195, USA.

The Journal of Biological Chemistry
|June 6, 2008
PubMed
Summary

Synaptic vesicle protein 2 (SV2) binds adenine nucleotides, suggesting a link between cellular energy and regulated secretion. This finding reveals SV2

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • Synaptic vesicle protein 2 (SV2) is crucial for calcium-regulated secretion of hormones and neurotransmitters.
  • SV2 isoforms (SV2A, SV2B) are essential for maintaining the readily releasable pool of synaptic vesicles, indicating a role in vesicle priming.

Purpose of the Study:

  • To investigate the potential ATP-binding properties of SV2, given the presence of putative ATP-binding sites.
  • To explore the interaction of SV2A and SV2B with nucleotides and identify potential binding sites.

Main Methods:

  • Utilized a photoaffinity reagent (8-azido-ATP[gamma] biotin) to examine nucleotide binding to purified, recombinant SV2A and SV2B.
  • Tested binding in the presence and absence of various nucleotides to determine affinity and specificity.

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Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis
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Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis

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An Optical Assay for Synaptic Vesicle Recycling in Cultured Neurons Overexpressing Presynaptic Proteins
09:33

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

Published on: June 26, 2018

Related Experiment Videos

Last Updated: Jul 4, 2026

Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time
08:33

Measuring Nucleotide Binding to Intact, Functional Membrane Proteins in Real Time

Published on: March 11, 2021

Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis
08:09

Mapping the Binding Site of an Aptamer on ATP Using MicroScale Thermophoresis

Published on: January 7, 2017

An Optical Assay for Synaptic Vesicle Recycling in Cultured Neurons Overexpressing Presynaptic Proteins
09:33

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

Published on: June 26, 2018

Main Results:

  • SV2A and SV2B were confirmed to bind nucleotides, with a preference for adenine-containing nucleotides.
  • Two nucleotide-binding sites were identified within the cytoplasmic domains of SV2A, preceding transmembrane domains 1 and 7.

Conclusions:

  • SV2-mediated vesicle priming may be regulated by adenine nucleotides.
  • This nucleotide interaction provides a potential mechanism linking cellular energy status to regulated secretion processes.