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Mutant mice lacking the phosphorylation of SNAP-25 serine-187 exhibited reduced neurotransmitter release and enhanced presynaptic short-term plasticity.
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Single-molecule optical tweezers were used to measure the assembly energy and kinetics of SNARE complexes containing single mutations I67T/N in SNAP-25B, which disrupt neurotransmitter release and have been implicated in neurological disorders. Both mutations lead to unfolding of the C-terminal region in the t-SNARE complex.
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Study identified Gbeta1 and Gbeta2 as the interacting partners of both SNAP-25 isoforms in mouse hippocampus, but Gbeta2 was less efficiently captured by SNAP-25a. These results implicate that the two SNAP-25 isoforms could differently mediate protein interactions outside the ternary SNARE core complex and thereby contribute to modulate neurotransmission.
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SNAP25 is necessary for accurate regulation of Ca2+-dynamics and insulin secretion in pancreatic beta cells.
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We describe a high degree of structural similarity between the CpxII CTD and the SNAP25-SN1 domain (C-terminal half) and show that the CTD peptide lowers the rate of SDS-resistant SNARE complex formation in vitro. Moreover, corresponding CpxII:SNAP25 chimeras do restore complexin's function and even 'superclamp' tonic secretion.
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Our findings provide in vivo functional evidence showing a critical role of SNAP-25 dysfunction on synaptic transmission, which contributes to the developmental of schizophrenia.
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Snap-25-null mutant neurons degenerate after 4 days in vitro and contain fewer dense-core vesicles.
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a mouse mutant engineered to express normal levels of SNAP-25 but only SNAP-25a shows metabolic disease.
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The function of synaptotagmin-1 (syt-1):soluble NSF attachment protein receptor (SNARE) interactions during neurotransmission remains unclear.
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proteins, such as syntaxin-1, Munc18-1, or SNAP-25, modulate alpha-synuclein neuropathy and/or are dysregulated in Alzheimer's disease, understanding this type of neurodegeneration may provide new links between synaptic defects and neurodegeneration in humans
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Study showed that SNAP25 is synthesized in the motor nerve endings and that the level of SNAP25 mRNA affects the activity of exocytosis of the neurotransmitter
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Data demonstrate a role for SNAP-25 in controlling PSD-95 clustering and open the possibility that genetic reductions of the protein levels may contribute to the pathology through an effect on postsynaptic function and plasticity.
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Data suggest that porosome-associated proteins SNAP25, TREK-1, syntaxin-1A, and Gai3 exhibit stability and functionality such that isolated proteins can be reconstituted as insulin-secreting porosomes in cell membrane of live cells.
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Study conducted long-term continuous video-EEG recordings of Snap25S187A/S187A mice and found that all mutant mice followed essentially the same process of epileptogenesis despite some individual differences
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we demonstrate that Syb2 and SNAP25 mediate the vesicular release of BDNF in axons and dendrites of cortical neurons
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The extreme C terminus of SNAP25 is a critical region for the GBetaGamma-SNARE interaction.
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Reduction of SNAP-25 levels in adolescent mice was associated with hyperactivity, cognitive and social impairment and an abnormal EEG, characterized by the occurrence of frequent spikes.
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Data show a significant increase of vesicle-associated membrane protein 2 (VAMP-2) mRNA expression, however, the expressions of synaptosome-associated protein of 25 kDa (SNAP-25) and syntaxin 1A did not exhibit the changes in hippocampus.
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SNAP-25 phosphorylation is regulated in a stress-dependent manner through both central and peripheral mechanisms.
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Results indicate that reduction of SNAP-25 expression is associated to generation of epileptiform discharges and cognitive dysfunctions, which can be effectively treated by antiepileptic drugs
