Regulating synaptic membrane exocytosis protein 1 is a protein that in humans is encoded by the RIMS1 gene. (wikipedia.org)
Proteins11
The RIM family of active zone proteins likely function as protein scaffolds that help regulate vesicle exocytosis during short-term plasticity. (wikipedia.org)
Syntaxins are membrane integrated Q-SNARE proteins known to participate in exocytosis. (ommegaonline.org)
Key interacting proteins of the plasma membrane, the cytosol and the vesicle membrane which function in the membrane fusion pathway, have been identified in a variety of cell types and characterized at the molecular level [10-14] . (ommegaonline.org)
Stefan Boehm The core complex, formed by the SNARE proteins synaptobrevin 2, syntaxin 1 and SNAP-25, is an important component of the synaptic fusion machinery and shows remarkable in vitro stability, as exemplified by its SDS-resistance. (biologists.com)
N. Morel ABSTRACT Synaptic vesicle docking and exocytosis require the specific interaction of synaptic vesicle proteins (such as VAMP/ synaptobrevin ) with presynaptic plasma membrane proteins (such as syntaxin and SNAP 25). (biologists.com)
Proteins that regulate vesicle exocytosis cluster at AZs, composing the cytomatrix at the active zone (CAZ). (eneuro.org)
These proteins aggregate at presynaptic active zones (AZs) to form the cytomatrix at the active zone (CAZ), which controls the recruitment, docking, and priming of synaptic vesicles and enhances calcium channel accumulation ( Gundelfinger and Fejtova, 2012 ). (eneuro.org)
Two important pathways were examined in the current study: (1) a basic pathway of exocytosis that brings new proteins to the cell surface and permits the cell to grow, and (2) synaptic transmission, a specialized form of exocytosis, regulated by Ca 2+ entry, in which vesicles already present at synapses fuse with the membrane and recycle locally (Murthy, 2003). (sdbonline.org)
Presynaptic active zone proteins have a crucial role in regulating vesicle exocytosis, which is essential for synaptic plasticity. (jneurosci.org)
Studies investigating pain pathology have demonstrated that ubiquitination contributes to chronic pain by regulating the turnover of synaptic proteins. (jneurosci.org)
Regulate1
Here, after research involving Sprague Dawley rats, we reported that spinal nerve ligation (SNL), in addition to causing allodynia, enhances the Rab3-interactive molecule-1α (RIM1α), a major active zone protein presumed to regulate neural plasticity, specifically in the synaptic plasma membranes (SPMs) of the ipsilateral dorsal horn. (jneurosci.org)
Regulates2
RAB3A (MIM 179490), a member of the Ras superfamily of genes, is a synaptic vesicle protein that regulates synaptic vesicle exocytosis. (wikipedia.org)
Considerable attention has been paid to understanding how Rab3A regulates secretion from neurons and neuroendocrine cells. (pancreapedia.org)
Neurons3
Here, we systematically studied fusion of DCV with single vesicle resolution upon different stimulation patterns in mammalian CNS neurons. (bvsalud.org)
We monitored DCV exocytosis at single vesicle resolution in tomosyn-deficient primary neurons using a validated pHluorin-based assay. (bvsalud.org)
Although these mice died shortly after birth from respiratory failure (61), their cultured hippocampal neurons showed normal synaptic structure, but reduced transmitter release. (pancreapedia.org)
Protein4
Tomosyn is a large, non-canonical SNARE protein proposed to act as an inhibitor of SNARE complex formation in the exocytosis of secretory vesicles. (bvsalud.org)
The second Rab3 GEF, known as GRAB, interacts with inositol hexakisphosphate kinase and Rab3A and its protein expression is primarily in brain (41). (pancreapedia.org)
Such membrane fusion is mediated by the SNARE complex, which is composed of the vesicle-associated protein synaptobrevin (VAMP2), and the plasma. (biologists.com)
Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release. (affbiotech.cn)
A molecular understanding of membrane traffic has broad implications for our understanding of growth control in cancer, receptor trafficking errors in heart disease, regulation of insulin secretion in diabetes and synaptic vesicle biogenesis and transport in neurological disorders. (stanford.edu)
Rab3D2
The crystal structure of Rab3A in the active configuration or bound to Rabphillin has been determined (19, 50) and Rab3D has been fit to the same model with 6 β-strands and 5 α-helices (45). (pancreapedia.org)
Rab3A and 3D mouse genes possess 5 exons and Rab3D has been localized to chromosome 13 (1,5). (pancreapedia.org)
Vitro1
In order to study the fusion of DCVs in vitro, techniques like perfusion with buffer containing high concentration of potassium or electric field stimulation are needed to trigger the exocytosis of DCVs. (bvsalud.org)
Involves3
Sabine Hilfiker Neurosecretion involves fusion of vesicles with the plasma membrane. (biologists.com)
J. Oliver Dolly Ca 2+ -triggered catecholamine exocytosis from chromaffin cells involves SNAP-25, synaptobrevin and syntaxin (known as SNAREs). (biologists.com)
Synaptic signaling involves the release of neurotransmitter from presynaptic active zones (AZs). (eneuro.org)
Syntaxin1
Our immunoblot data reveals that syntaxin 2 of bovine cauda sperm is released after lysophosphatidylcholine (LPC)-induced acrosomal exocytosis. (ommegaonline.org)
Pathway1
In contrast to the sperm acrosome reaction, the secretory pathway of somatic cells has received detailed characterization in recent years and a great deal has been learned of the processes regulating vesicle docking and fusion with the plasma membrane. (ommegaonline.org)
Calcium2
They are packed into dense core vesicles (DCVs) that undergo calcium and action potential fusion with the plasma membrane. (bvsalud.org)
Rab3A activity is also specifically regulated by calcium-calmodulin complex (15). (pancreapedia.org)
Plasma2
The acrosome reaction is analogous to regulated exocytosis in somatic cells in that both are initiated by ligand acting at the plasma membrane, both require activation of signaling pathways and ion channels, both are Ca 2+ -dependent and both result in the fusion of the plasma membrane with the membrane of a docked secretory granule (acrosome) [2,9,10] . (ommegaonline.org)
In some cases, the exocytotic vesicles derive from the Golgi apparatus and consist of newly synthesized materials, while in others the vesicles derive from the plasma membrane and cycle locally. (sdbonline.org)
Function1
Taken together, our findings argue against an inhibitory role of tomosyns in neuronal DCV exocytosis and suggests an evolutionary conserved function of tomosyns in the packaging of secretory cargo at the Golgi. (bvsalud.org)
Role2
In the brain, tomosyn inhibits the fusion of synaptic vesicles (SVs), whereas its role in the fusion of neuropeptide-containing dense core vesicles (DCVs) is unknown. (bvsalud.org)
A single form of Rab3 exists in C. elegans and is believed to play a role in neurotransmitter release (47), while in sea urchin eggs a Rab3 is believed to play a role in cortical granule exocytosis (13). (pancreapedia.org)
Single1
This defect could be rescued by a single allele of Rab3A. (pancreapedia.org)
Fusion3
Exocytosis of DCVs requires high frequency or patterned stimulation, but the determinants to reach maximal fusion capacity and for efficient replenishment of released DCVs are unknown. (bvsalud.org)
These data indicate that trains of 50Hz AP stimulation patterns triggered DCV exocytosis most efficiently and more intense stimulation promotes longer DCV fusion pore openings.Significance StatementNeuropeptides and neurotrophins modulate multiple regulatory functions of human body like reproduction, food intake or mood. (bvsalud.org)
We used six different stimulation patterns and showed that trains of 50Hz action potential bursts triggered DCV exocytosis most efficiently and more intense stimulation promotes longer DCV fusion pore openings. (bvsalud.org)
Transport1
However, the synaptic phenotype in the rab3-GEF mutant cannot be fully explained by defective transport and loss of GEF activity. (eneuro.org)