Related Experiment Video
Updated: Aug 2, 2026

09:24
High-Resolution Quantitative Immunogold Analysis of Membrane Receptors at Retinal Ribbon Synapses
Published on: February 18, 2016
A conserved mechanism of synaptogyrin localization
1Department of Anatomy and Neurobiology, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
Molecular Biology of the Cell
|August 22, 2001
Summary
Synaptogyrin (SNG-1) proteins are localized to neuronal synapses. Specific C-terminal and cytoplasmic loop domains are crucial for this synaptic targeting, and these mechanisms appear conserved across species.
Area of Science:
- Neuroscience
- Cell Biology
- Molecular Biology
Background:
- Synaptogyrins are proteins involved in synaptic function.
- Understanding their precise localization mechanisms is key to synaptic vesicle trafficking.
Purpose of the Study:
- To investigate the in vivo localization of synaptogyrin family members.
- To identify the specific molecular domains responsible for synaptic targeting of synaptogyrin.
Main Methods:
- Utilized green fluorescent protein (GFP)-tagged Caenorhabditis elegans synaptogyrin (SNG-1) for in vivo studies.
- Performed deletion and mutational analyses to pinpoint localization signals.
- Conducted chimeric studies to test the sufficiency of identified domains.
- Examined localization in both C. elegans and cultured mammalian (hippocampal) neurons.
Main Results:
- Synaptogyrin (SNG-1) is localized to neurons and synapses in C. elegans.
- A 38 amino acid C-terminal sequence and a specific arginine in a cytoplasmic loop are essential for SNG-1 synaptic localization.
- These domains can redirect a non-neuronal synaptogyrin (cellugyrin) to synaptic vesicles.
- Rat synaptogyrin also shows synaptic localization in both C. elegans and hippocampal neurons, with the C-terminal domain being critical.
Conclusions:
- Identified key domains within synaptogyrin required for synaptic localization.
- Demonstrated that these localization signals are conserved from invertebrates to vertebrates.
- Suggests conserved molecular mechanisms govern synaptogyrin targeting to synaptic vesicles.
Related Concept Videos
Conserved Binding Sites
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally analyses the...
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...
Golgi Matrix Proteins
Golgi matrix proteins are a group of highly dynamic proteins that maintain the stacked structure of Golgi. These proteins adapt to rapid morphological changes of the Golgi during the cell cycle. During cell division, mild proteolysis removes these connections resulting in Golgi unstacking. In The daughter cells, these proteins help reassemble the unstacked Golgi.
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
One of the first identified Golgi matrix proteins was GM130, a rod-like protein located in the cis-Golgi. Subsequently, many Golgi...
Transport Across the Golgi
While it is unclear how molecules move between adjacent Golgi cisternae, it is apparent that the molecules move from cis- cisterna, the entry face, to the trans- cisterna, the exit face. Experiments initially suggested vesicles that bud from one cisterna and fuse with the next cisterna to transport proteins between the cisternae. This vesicular transport model describes the Golgi apparatus as a relatively static structure with a unique enzyme composition in each cisterna. Molecules are...
Chemical Synapses
Chemical synapses are specialized sites between two neurons or between a neuron and a non-neuronal cell like a muscle, glandular or sensory cell.
Because chemical synapses depend on the release of neurotransmitter molecules from synaptic vesicles to pass on their signal, there is an approximately one millisecond delay between when the axon potential reaches the presynaptic terminal and when the neurotransmitter leads to opening of postsynaptic ion channels. Additionally, this signaling is...
Because chemical synapses depend on the release of neurotransmitter molecules from synaptic vesicles to pass on their signal, there is an approximately one millisecond delay between when the axon potential reaches the presynaptic terminal and when the neurotransmitter leads to opening of postsynaptic ion channels. Additionally, this signaling is...

