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tethering of Syt1 to synaptic vesicles in vivo is a prerequisite for its role in facilitating fast synchronous synaptic vesicle release and suppressing asynchronous and spontaneous fusion
synaptic transmission can be regulated by Syt1 multimerization and that both C2 domains of Syt1 are uniquely required for modulating Ca(2 (show CA2 ELISA Kits)+)-independent spontaneous fusion and Ca(2 (show CA2 ELISA Kits)+)-dependent synchronous release.
effect of APP (show APP ELISA Kits) gene on synaptotagmin 1 mRNA level
The major function of Ca2+ binding to synaptotagmin's C2A domain is to neutralize the negative charge of the pocket, thereby unleashing the fusion-stimulating activity of synaptotagmin.
this study provided direct support for the hypothesis that plasma membrane penetration, specifically by the C(2)B domain of synaptotagmin, is the critical effector interaction for coupling Ca(2 (show CA2 ELISA Kits)+) binding with vesicle fusion
Results suggest that the tandem C2 domains of Syt 1 play independent roles in neurotransmission.
The C(2)B Ca(2+)-binding motif of synaptotagmin is required for synaptic transmission in vivo
Synaptotagmins I and IV promote transmitter release independently of Ca(2 (show CA2 ELISA Kits)+) binding in the C(2)A domain
Data show that synaptotagmin I is required for a post-docking step during vesicle fusion but does not function to stabilize the docked vesicle state.
These results indicate that synaptotagmin is the major Ca(2 (show CA2 ELISA Kits)+) sensor for evoked release and functions to trigger synchronous fusion in response to Ca(2 (show CA2 ELISA Kits)+), while suppressing asynchronous release.
Authors propose that the strong reduction of Syt2 (show SYT2 ELISA Kits) and SV2B (show SV2B ELISA Kits) are key factors of the functional synaptic alteration and that the physiological downregulation of Syt1 plays a determinant role in muscle vulnerability in SMA (show SMN1 ELISA Kits).
The function of synaptotagmin-1 (syt-1):soluble NSF attachment protein (show NAPG ELISA Kits) receptor (SNARE (show VTI1B ELISA Kits)) interactions during neurotransmission remains unclear.
we identify Syt2 (show SYT2 ELISA Kits) as a functionally important Ca(2 (show CA2 ELISA Kits)+) sensor at fast-releasing inhibitory synapses, and show that Syt1 and Syt2 (show SYT2 ELISA Kits) can redundantly control transmitter release at specific brain synapses
results suggest that postsynaptic Syt1 and Syt7 (show SYT7 ELISA Kits) act as redundant Ca(2 (show CA2 ELISA Kits)+)-sensors for Ca(2 (show CA2 ELISA Kits)+)-dependent exocytosis of AMPA (show GRIA3 ELISA Kits) receptors during long-term potentiation, and thereby delineate a simple mechanism for the recruitment of AMPA (show GRIA3 ELISA Kits) receptors that mediates LTP (show SCP2 ELISA Kits)
demonstrates a developmental Syt1-Syt2 (show SYT2 ELISA Kits) isoform switch at an identified synapse, a mechanism that could fine-tune the speed, reliability, and plasticity of transmitter release at fast releasing CNS synapses.
the combined inactivation of all 3 E-Syt (show SS18 ELISA Kits) genes has no effect on mouse viability or fertility.
GRASP65 (show GORASP1 ELISA Kits) phosphorylation may have a critical role in inducing cell death.
We conclude that synaptotagmin-1 phosphorylation is an essential step in PKC (show PKC ELISA Kits)-dependent potentiation of synaptic transmission, acting downstream of the two other essential DAG/PKC (show PKC ELISA Kits) substrates, Munc13-1 (show UNC13A ELISA Kits) and Munc18-1 (show STXBP1 ELISA Kits).
data show that hepatic Syt1 expression is influenced by diet and hormonal milieu
different structural states of syt (show SS18 ELISA Kits) underlie the control of distinct forms of synaptic transmission.
findings show extended Synaptotagmi1 (E-Syt1), along with related E-Syt3, negatively modulates viral release into the extracellular milieu, cell-to-cell viral spread and viral entry, processes that implicate membrane fusion events; , these E-Syt (show SS18 ELISA Kits) proteins impacted formation of virus-induced syncytia; findings hint at the modulation of the viral fusion machinery by the E-Syt (show SS18 ELISA Kits) family of proteins
Using electron microscopy combined with targeted mutations, the authors show that under physiologically relevant conditions, both the Syt1 ring assembly and its rapid disruption by Ca(2+) involve the well-established functional surfaces on the C2B domain that are important for synaptic transmission.
This study found that the CSF (show CSF2 ELISA Kits) levels of synaptotagmin-1 were consistently elevated in patients with dementia due to Alzheimer's disease.
SYT-SSX fusion is associated with synovial sarcoma.
the extended synaptotagmins (E-Syts), endoplasmic reticulum (ER) proteins that function as PtdIns(4,5)P2- and Ca(2 (show CA2 ELISA Kits)+)-regulated tethers to the Pplasma membrane.
Data indicate that small protein sequence changes in the Ca(2 (show CA2 ELISA Kits)+)-binding loops of the C2 domains may give rise to the difference in binding kinetics between Syt-1 and Syt-7 (show SYT7 ELISA Kits) isoforms.
These findings identify Syt1 as a novel Ca(2 (show CA2 ELISA Kits)+)-sensitive PS1 (show PSEN1 ELISA Kits) modulator that could regulate synaptic ABETA (show APP ELISA Kits), opening avenues for novel and selective synapse targeting therapeutic strategies.
One-Step reverse transcriptase real time PCR for the detection SYT-SSX transcript is feasible as an aid in confirming the diagnosis of synovial sarcoma.
membrane tethering by E-Syt1 (ER to PM) and by synaptotagmin (secretory vesicles to PM) undergo a similar regulation by plasma membrane lipids and cytosolic Ca(2 (show CA2 ELISA Kits)+).
A dominant negative de novo SYT1 missense variant(I368T)altered the kinetics of synaptic vesicle endocytosis and caused an early onset dyskinetic movement disorder, severe motor delay, and profound cognitive impairment.
The synaptotagmins are integral membrane proteins of synaptic vesicles thought to serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Calcium binding to synaptotagmin-1 participates in triggering neurotransmitter release at the synapse (Fernandez-Chacon et al., 2001
, synaptoptagmin 1
, synaptotagmin 1
, synaptotagmin I
, DKFZP459P193 protein
, Synaptotagmin I
, Golgi reassembly-stacking protein 1
, golgi peripheral membrane protein p65
, golgi reassembly-stacking protein of 65 kDa
, synaptotagmin p65
, synaptotagmin 8
, synaptotagmin I VQ/C2B-beta