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Human SYT1 Protein expressed in Wheat germ - ABIN1322010
Liu, Akle, Zheng, Dave, Tortella, Hayes, Wang: Comparing calpain- and caspase-3-mediated degradation patterns in traumatic brain injury by differential proteome analysis. in The Biochemical journal 2006
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 (zeige CA2 Proteine)+)-independent spontaneous fusion and Ca(2 (zeige CA2 Proteine)+)-dependent synchronous release.
effect of APP (zeige APP Proteine) 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 (zeige CA2 Proteine)+) 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 (zeige CA2 Proteine)+) 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 (zeige CA2 Proteine)+) sensor for evoked release and functions to trigger synchronous fusion in response to Ca(2 (zeige CA2 Proteine)+), while suppressing asynchronous release.
The function of synaptotagmin-1 (syt-1):soluble NSF attachment protein (zeige NAPG Proteine) receptor (SNARE (zeige VTI1B Proteine)) interactions during neurotransmission remains unclear.
we identify Syt2 (zeige SYT2 Proteine) as a functionally important Ca(2 (zeige CA2 Proteine)+) sensor at fast-releasing inhibitory synapses, and show that Syt1 and Syt2 (zeige SYT2 Proteine) can redundantly control transmitter release at specific brain synapses
results suggest that postsynaptic Syt1 and Syt7 (zeige SYT7 Proteine) act as redundant Ca(2 (zeige CA2 Proteine)+)-sensors for Ca(2 (zeige CA2 Proteine)+)-dependent exocytosis of AMPA (zeige GRIA3 Proteine) receptors during long-term potentiation, and thereby delineate a simple mechanism for the recruitment of AMPA (zeige GRIA3 Proteine) receptors that mediates LTP (zeige SCP2 Proteine)
demonstrates a developmental Syt1-Syt2 (zeige SYT2 Proteine) 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 (zeige SS18 Proteine) genes has no effect on mouse viability or fertility.
GRASP65 (zeige GORASP1 Proteine) phosphorylation may have a critical role in inducing cell death.
We conclude that synaptotagmin-1 phosphorylation is an essential step in PKC-dependent potentiation of synaptic transmission, acting downstream of the two other essential DAG/PKC substrates, Munc13-1 and Munc18-1 (zeige STXBP1 Proteine).
data show that hepatic Syt1 expression is influenced by diet and hormonal milieu
different structural states of syt (zeige SS18 Proteine) underlie the control of distinct forms of synaptic transmission.
The interaction of Dvl1 (zeige DVL1 Proteine) with Syt-1, which is regulated by Wnts, modulates neurotransmitter release.
findings show extended Synaptotagmi1 (E-Syt1), along with related E-Syt3 (zeige ESYT3 Proteine), 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 (zeige SS18 Proteine) proteins impacted formation of virus-induced syncytia; findings hint at the modulation of the viral fusion machinery by the E-Syt (zeige SS18 Proteine) 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 (zeige CSF2 Proteine) levels of synaptotagmin-1 were consistently elevated in patients with dementia due to Alzheimer's disease.
SYT (zeige SS18 Proteine)-SSX (zeige SSX2 Proteine) 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 (zeige CA2 Proteine)+)-regulated tethers to the Pplasma membrane.
Data indicate that small protein sequence changes in the Ca(2 (zeige CA2 Proteine)+)-binding loops of the C2 domains may give rise to the difference in binding kinetics between Syt-1 and Syt-7 (zeige SYT7 Proteine) isoforms.
These findings identify Syt1 as a novel Ca(2 (zeige CA2 Proteine)+)-sensitive PS1 (zeige PSEN1 Proteine) modulator that could regulate synaptic ABETA (zeige APP Proteine), opening avenues for novel and selective synapse targeting therapeutic strategies.
One-Step reverse transcriptase real time PCR for the detection SYT (zeige SS18 Proteine)-SSX (zeige SSX2 Proteine) 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 (zeige CA2 Proteine)+).
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