Structured Review

Ipsen Group synaptotagmin
Calcium dependent exocytosis at the presynaptic terminal. In neurons, synaptic vesicles are loaded with neurotransmitters and docked to the plasma membrane via the interaction of VAMP2 and t-SNARE (SNAP25 and syntaxin 1). Further zippering of SNARE by <t>synaptotagmin</t> (often Syt1, although other isoforms are present in certain neurons ), Munc-13 and Munc-18 (not shown) primes the vesicles ready to be fused. Upon the arrival of an action potential, VDCC facilitates an increase of intracellular Ca 2+ concentration. Syt1, as a Ca 2+ sensor, senses this change in calcium and initiates fusion of the vesicle and presynaptic membranes, resulting in the release of neurotransmitter into the synaptic cleft to activate a specific receptor or population of receptors on postsynaptic terminals.
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Images

1) Product Images from "GPCR Regulation of Secretion"

Article Title: GPCR Regulation of Secretion

Journal: Pharmacology & therapeutics

doi: 10.1016/j.pharmthera.2018.07.005

Calcium dependent exocytosis at the presynaptic terminal. In neurons, synaptic vesicles are loaded with neurotransmitters and docked to the plasma membrane via the interaction of VAMP2 and t-SNARE (SNAP25 and syntaxin 1). Further zippering of SNARE by synaptotagmin (often Syt1, although other isoforms are present in certain neurons ), Munc-13 and Munc-18 (not shown) primes the vesicles ready to be fused. Upon the arrival of an action potential, VDCC facilitates an increase of intracellular Ca 2+ concentration. Syt1, as a Ca 2+ sensor, senses this change in calcium and initiates fusion of the vesicle and presynaptic membranes, resulting in the release of neurotransmitter into the synaptic cleft to activate a specific receptor or population of receptors on postsynaptic terminals.
Figure Legend Snippet: Calcium dependent exocytosis at the presynaptic terminal. In neurons, synaptic vesicles are loaded with neurotransmitters and docked to the plasma membrane via the interaction of VAMP2 and t-SNARE (SNAP25 and syntaxin 1). Further zippering of SNARE by synaptotagmin (often Syt1, although other isoforms are present in certain neurons ), Munc-13 and Munc-18 (not shown) primes the vesicles ready to be fused. Upon the arrival of an action potential, VDCC facilitates an increase of intracellular Ca 2+ concentration. Syt1, as a Ca 2+ sensor, senses this change in calcium and initiates fusion of the vesicle and presynaptic membranes, resulting in the release of neurotransmitter into the synaptic cleft to activate a specific receptor or population of receptors on postsynaptic terminals.

Techniques Used: Concentration Assay

Gβγ regulation of the presynaptic vesicle release. Synaptic vesicles are primed by a tethering interaction between VAMP2 on the vesicle and the SNAP25/syntaxin 1 dimer at the plasma me mbrane. At low intracellular concentrations of calcium, activation of Gi/o coupled receptors results in release of Gβγ that will bind to the c-terminal of SNARE proteins and displace synaptotagmin in a competitive manner. In addition to c-terminal of SNARE, we found residues at N-terminal of SNARE complex which may affect the Gβγ-SNARE interaction (orange circle). At high enough intracellular calcium concentrations, such as with repetitive neuronal stimulation, synaptotagmin is able to compete with Gβγ for binding to SNARE, and thereby promote fusion of the vesicles with the plasma membrane.
Figure Legend Snippet: Gβγ regulation of the presynaptic vesicle release. Synaptic vesicles are primed by a tethering interaction between VAMP2 on the vesicle and the SNAP25/syntaxin 1 dimer at the plasma me mbrane. At low intracellular concentrations of calcium, activation of Gi/o coupled receptors results in release of Gβγ that will bind to the c-terminal of SNARE proteins and displace synaptotagmin in a competitive manner. In addition to c-terminal of SNARE, we found residues at N-terminal of SNARE complex which may affect the Gβγ-SNARE interaction (orange circle). At high enough intracellular calcium concentrations, such as with repetitive neuronal stimulation, synaptotagmin is able to compete with Gβγ for binding to SNARE, and thereby promote fusion of the vesicles with the plasma membrane.

Techniques Used: Activation Assay, Binding Assay

2) Product Images from "GPCR Regulation of Secretion"

Article Title: GPCR Regulation of Secretion

Journal: Pharmacology & therapeutics

doi: 10.1016/j.pharmthera.2018.07.005

Calcium dependent exocytosis at the presynaptic terminal. In neurons, synaptic vesicles are loaded with neurotransmitters and docked to the plasma membrane via the interaction of VAMP2 and t-SNARE (SNAP25 and syntaxin 1). Further zippering of SNARE by synaptotagmin (often Syt1, although other isoforms are present in certain neurons ), Munc-13 and Munc-18 (not shown) primes the vesicles ready to be fused. Upon the arrival of an action potential, VDCC facilitates an increase of intracellular Ca 2+ concentration. Syt1, as a Ca 2+ sensor, senses this change in calcium and initiates fusion of the vesicle and presynaptic membranes, resulting in the release of neurotransmitter into the synaptic cleft to activate a specific receptor or population of receptors on postsynaptic terminals.
Figure Legend Snippet: Calcium dependent exocytosis at the presynaptic terminal. In neurons, synaptic vesicles are loaded with neurotransmitters and docked to the plasma membrane via the interaction of VAMP2 and t-SNARE (SNAP25 and syntaxin 1). Further zippering of SNARE by synaptotagmin (often Syt1, although other isoforms are present in certain neurons ), Munc-13 and Munc-18 (not shown) primes the vesicles ready to be fused. Upon the arrival of an action potential, VDCC facilitates an increase of intracellular Ca 2+ concentration. Syt1, as a Ca 2+ sensor, senses this change in calcium and initiates fusion of the vesicle and presynaptic membranes, resulting in the release of neurotransmitter into the synaptic cleft to activate a specific receptor or population of receptors on postsynaptic terminals.

Techniques Used: Concentration Assay

Gβγ regulation of the presynaptic vesicle release. Synaptic vesicles are primed by a tethering interaction between VAMP2 on the vesicle and the SNAP25/syntaxin 1 dimer at the plasma me mbrane. At low intracellular concentrations of calcium, activation of Gi/o coupled receptors results in release of Gβγ that will bind to the c-terminal of SNARE proteins and displace synaptotagmin in a competitive manner. In addition to c-terminal of SNARE, we found residues at N-terminal of SNARE complex which may affect the Gβγ-SNARE interaction (orange circle). At high enough intracellular calcium concentrations, such as with repetitive neuronal stimulation, synaptotagmin is able to compete with Gβγ for binding to SNARE, and thereby promote fusion of the vesicles with the plasma membrane.
Figure Legend Snippet: Gβγ regulation of the presynaptic vesicle release. Synaptic vesicles are primed by a tethering interaction between VAMP2 on the vesicle and the SNAP25/syntaxin 1 dimer at the plasma me mbrane. At low intracellular concentrations of calcium, activation of Gi/o coupled receptors results in release of Gβγ that will bind to the c-terminal of SNARE proteins and displace synaptotagmin in a competitive manner. In addition to c-terminal of SNARE, we found residues at N-terminal of SNARE complex which may affect the Gβγ-SNARE interaction (orange circle). At high enough intracellular calcium concentrations, such as with repetitive neuronal stimulation, synaptotagmin is able to compete with Gβγ for binding to SNARE, and thereby promote fusion of the vesicles with the plasma membrane.

Techniques Used: Activation Assay, Binding Assay

3) Product Images from "GPCR Regulation of Secretion"

Article Title: GPCR Regulation of Secretion

Journal: Pharmacology & therapeutics

doi: 10.1016/j.pharmthera.2018.07.005

Calcium dependent exocytosis at the presynaptic terminal. In neurons, synaptic vesicles are loaded with neurotransmitters and docked to the plasma membrane via the interaction of VAMP2 and t-SNARE (SNAP25 and syntaxin 1). Further zippering of SNARE by synaptotagmin (often Syt1, although other isoforms are present in certain neurons ), Munc-13 and Munc-18 (not shown) primes the vesicles ready to be fused. Upon the arrival of an action potential, VDCC facilitates an increase of intracellular Ca 2+ concentration. Syt1, as a Ca 2+ sensor, senses this change in calcium and initiates fusion of the vesicle and presynaptic membranes, resulting in the release of neurotransmitter into the synaptic cleft to activate a specific receptor or population of receptors on postsynaptic terminals.
Figure Legend Snippet: Calcium dependent exocytosis at the presynaptic terminal. In neurons, synaptic vesicles are loaded with neurotransmitters and docked to the plasma membrane via the interaction of VAMP2 and t-SNARE (SNAP25 and syntaxin 1). Further zippering of SNARE by synaptotagmin (often Syt1, although other isoforms are present in certain neurons ), Munc-13 and Munc-18 (not shown) primes the vesicles ready to be fused. Upon the arrival of an action potential, VDCC facilitates an increase of intracellular Ca 2+ concentration. Syt1, as a Ca 2+ sensor, senses this change in calcium and initiates fusion of the vesicle and presynaptic membranes, resulting in the release of neurotransmitter into the synaptic cleft to activate a specific receptor or population of receptors on postsynaptic terminals.

Techniques Used: Concentration Assay

Gβγ regulation of the presynaptic vesicle release. Synaptic vesicles are primed by a tethering interaction between VAMP2 on the vesicle and the SNAP25/syntaxin 1 dimer at the plasma me mbrane. At low intracellular concentrations of calcium, activation of Gi/o coupled receptors results in release of Gβγ that will bind to the c-terminal of SNARE proteins and displace synaptotagmin in a competitive manner. In addition to c-terminal of SNARE, we found residues at N-terminal of SNARE complex which may affect the Gβγ-SNARE interaction (orange circle). At high enough intracellular calcium concentrations, such as with repetitive neuronal stimulation, synaptotagmin is able to compete with Gβγ for binding to SNARE, and thereby promote fusion of the vesicles with the plasma membrane.
Figure Legend Snippet: Gβγ regulation of the presynaptic vesicle release. Synaptic vesicles are primed by a tethering interaction between VAMP2 on the vesicle and the SNAP25/syntaxin 1 dimer at the plasma me mbrane. At low intracellular concentrations of calcium, activation of Gi/o coupled receptors results in release of Gβγ that will bind to the c-terminal of SNARE proteins and displace synaptotagmin in a competitive manner. In addition to c-terminal of SNARE, we found residues at N-terminal of SNARE complex which may affect the Gβγ-SNARE interaction (orange circle). At high enough intracellular calcium concentrations, such as with repetitive neuronal stimulation, synaptotagmin is able to compete with Gβγ for binding to SNARE, and thereby promote fusion of the vesicles with the plasma membrane.

Techniques Used: Activation Assay, Binding Assay

4) Product Images from "GPCR Regulation of Secretion"

Article Title: GPCR Regulation of Secretion

Journal: Pharmacology & therapeutics

doi: 10.1016/j.pharmthera.2018.07.005

Calcium dependent exocytosis at the presynaptic terminal. In neurons, synaptic vesicles are loaded with neurotransmitters and docked to the plasma membrane via the interaction of VAMP2 and t-SNARE (SNAP25 and syntaxin 1). Further zippering of SNARE by synaptotagmin (often Syt1, although other isoforms are present in certain neurons ), Munc-13 and Munc-18 (not shown) primes the vesicles ready to be fused. Upon the arrival of an action potential, VDCC facilitates an increase of intracellular Ca 2+ concentration. Syt1, as a Ca 2+ sensor, senses this change in calcium and initiates fusion of the vesicle and presynaptic membranes, resulting in the release of neurotransmitter into the synaptic cleft to activate a specific receptor or population of receptors on postsynaptic terminals.
Figure Legend Snippet: Calcium dependent exocytosis at the presynaptic terminal. In neurons, synaptic vesicles are loaded with neurotransmitters and docked to the plasma membrane via the interaction of VAMP2 and t-SNARE (SNAP25 and syntaxin 1). Further zippering of SNARE by synaptotagmin (often Syt1, although other isoforms are present in certain neurons ), Munc-13 and Munc-18 (not shown) primes the vesicles ready to be fused. Upon the arrival of an action potential, VDCC facilitates an increase of intracellular Ca 2+ concentration. Syt1, as a Ca 2+ sensor, senses this change in calcium and initiates fusion of the vesicle and presynaptic membranes, resulting in the release of neurotransmitter into the synaptic cleft to activate a specific receptor or population of receptors on postsynaptic terminals.

Techniques Used: Concentration Assay

Gβγ regulation of the presynaptic vesicle release. Synaptic vesicles are primed by a tethering interaction between VAMP2 on the vesicle and the SNAP25/syntaxin 1 dimer at the plasma me mbrane. At low intracellular concentrations of calcium, activation of Gi/o coupled receptors results in release of Gβγ that will bind to the c-terminal of SNARE proteins and displace synaptotagmin in a competitive manner. In addition to c-terminal of SNARE, we found residues at N-terminal of SNARE complex which may affect the Gβγ-SNARE interaction (orange circle). At high enough intracellular calcium concentrations, such as with repetitive neuronal stimulation, synaptotagmin is able to compete with Gβγ for binding to SNARE, and thereby promote fusion of the vesicles with the plasma membrane.
Figure Legend Snippet: Gβγ regulation of the presynaptic vesicle release. Synaptic vesicles are primed by a tethering interaction between VAMP2 on the vesicle and the SNAP25/syntaxin 1 dimer at the plasma me mbrane. At low intracellular concentrations of calcium, activation of Gi/o coupled receptors results in release of Gβγ that will bind to the c-terminal of SNARE proteins and displace synaptotagmin in a competitive manner. In addition to c-terminal of SNARE, we found residues at N-terminal of SNARE complex which may affect the Gβγ-SNARE interaction (orange circle). At high enough intracellular calcium concentrations, such as with repetitive neuronal stimulation, synaptotagmin is able to compete with Gβγ for binding to SNARE, and thereby promote fusion of the vesicles with the plasma membrane.

Techniques Used: Activation Assay, Binding Assay

5) Product Images from "New Insights Into Interactions of Presynaptic Calcium Channel Subtypes and SNARE Proteins in Neurotransmitter Release"

Article Title: New Insights Into Interactions of Presynaptic Calcium Channel Subtypes and SNARE Proteins in Neurotransmitter Release

Journal: Frontiers in Molecular Neuroscience

doi: 10.3389/fnmol.2018.00213

Molecular model of synaptic vesicle fusion machinery, interactions of active zone proteins, presynaptic Ca 2+ channel and SNAREs. (A) The process of vesicle fusion: 1. synaptic vesicle recruiting to active zone; 2. synaptic vesicle docking at the presynaptic membrane and with SNAREs complex conformation. 3. priming of synaptic vesicle on presynaptic membrane; and 4. fusion pore to open and with neurotransmitter release. (B) Direct interaction of Cav2 α1 subunits with proteins Rab3 interacting molecules (RIM), RIM-binding protein (RIM-BP), Munc-13 and SNAREs (syntaxin, SNAP-25 and synaptobrevin). (C) RIM binding to RIM-BP induced Munc13 from inactive homodimer to active heterodimer, which promoted Sec1/Munc18-1 (SM) protein dissociated with syntaxin-1. Syntaxin-1 changes from closed formation to open formation. Syntaxin-1 and SNAP-25 interacted with synaptobrevin to form SNAREs. Ca 2+ entry through Ca 2+ channel induced interaction with synaptotagmin, which trigger vesicle fusion.
Figure Legend Snippet: Molecular model of synaptic vesicle fusion machinery, interactions of active zone proteins, presynaptic Ca 2+ channel and SNAREs. (A) The process of vesicle fusion: 1. synaptic vesicle recruiting to active zone; 2. synaptic vesicle docking at the presynaptic membrane and with SNAREs complex conformation. 3. priming of synaptic vesicle on presynaptic membrane; and 4. fusion pore to open and with neurotransmitter release. (B) Direct interaction of Cav2 α1 subunits with proteins Rab3 interacting molecules (RIM), RIM-binding protein (RIM-BP), Munc-13 and SNAREs (syntaxin, SNAP-25 and synaptobrevin). (C) RIM binding to RIM-BP induced Munc13 from inactive homodimer to active heterodimer, which promoted Sec1/Munc18-1 (SM) protein dissociated with syntaxin-1. Syntaxin-1 changes from closed formation to open formation. Syntaxin-1 and SNAP-25 interacted with synaptobrevin to form SNAREs. Ca 2+ entry through Ca 2+ channel induced interaction with synaptotagmin, which trigger vesicle fusion.

Techniques Used: Binding Assay

6) Product Images from "Nitric oxide-mediated posttranslational modifications control neurotransmitter release by modulating complexin farnesylation and enhancing its clamping ability"

Article Title: Nitric oxide-mediated posttranslational modifications control neurotransmitter release by modulating complexin farnesylation and enhancing its clamping ability

Journal: PLoS Biology

doi: 10.1371/journal.pbio.2003611

Reduced farnesylation of cpx enhances AZ localization and alters interactions with SNARE proteins. (A) Maximal projection confocal images of w 1118 NMJs in Ctrl, following 60 min of exposure to NO or farnesylation inhibitor (“farnesyl inh”: 10 μM GGTI-298 + 20 μM L-744,832). PLA fluorescence in red and HRP staining in green for: left, syntaxin-cpx; middle: Brp-cpx; right: synaptotagmin-cpx interactions. (B) Analysis of summated PLA signal volumes relative to NMJ volumes. (C) FRAP experiments were performed at NMJs expressing GFP-cpx, shown as representative images of WT GFP-cpx at different time points (bleaching area: 2.5 μm 2 . Data denote mean ± SEM, Student t test, or ANOVA with post hoc Tukey-Kramer as indicated, * p
Figure Legend Snippet: Reduced farnesylation of cpx enhances AZ localization and alters interactions with SNARE proteins. (A) Maximal projection confocal images of w 1118 NMJs in Ctrl, following 60 min of exposure to NO or farnesylation inhibitor (“farnesyl inh”: 10 μM GGTI-298 + 20 μM L-744,832). PLA fluorescence in red and HRP staining in green for: left, syntaxin-cpx; middle: Brp-cpx; right: synaptotagmin-cpx interactions. (B) Analysis of summated PLA signal volumes relative to NMJ volumes. (C) FRAP experiments were performed at NMJs expressing GFP-cpx, shown as representative images of WT GFP-cpx at different time points (bleaching area: 2.5 μm 2 . Data denote mean ± SEM, Student t test, or ANOVA with post hoc Tukey-Kramer as indicated, * p

Techniques Used: Proximity Ligation Assay, Fluorescence, Staining, Expressing

Effects of SNO formation on farnesylation and cpx function. (A) The farnesyl transferase facilitates the addition of a farnesyl group to cpx (green) containing the CAAX motif. Upon S-nitrosylation, this motif is not recognized and the protein will not be farnesylated, resulting in lack of endomembrane targeting. (B) The schematic shows the effects of S-nitrosylation of cpx Cys within CAAX, resulting in fewer proteins being farnesylated and tethered to endomembranes. This allows a greater proportion of cytosolic cpx to be able to bind to the SNARE complex (including syntaxin [yellow]/Munc-18 [red], SNAP-25 [dark purple], synaptobrevin [purple]) to compete with synaptotagmin [blue] binding and prevent fusion because of its clamping function, which results in reduced transmitter release. This process is reversible and depends on the availability of GSH-dependent de-nitrosylation of cpx. GSH is generated by GCL and GSNO is broken down into G-SS-G and NH 2 OH by GSNOR activity. Cys, cysteine; cpx, complexin; G-SS-G, glutathione disulphide; GCL, glutamate-cysteine ligase; GluR, glutamate receptor; GSH, glutathione; GSNO, S-nitrosoglutathione; GSNOR, S-nitrosoglutathione reductase; NH 2 OH, hydroxylamine; SNARE, soluble N -ethyl-maleimide-sensitive fusion protein Attachment Protein Receptor; SNO, S-nitrosothiol.
Figure Legend Snippet: Effects of SNO formation on farnesylation and cpx function. (A) The farnesyl transferase facilitates the addition of a farnesyl group to cpx (green) containing the CAAX motif. Upon S-nitrosylation, this motif is not recognized and the protein will not be farnesylated, resulting in lack of endomembrane targeting. (B) The schematic shows the effects of S-nitrosylation of cpx Cys within CAAX, resulting in fewer proteins being farnesylated and tethered to endomembranes. This allows a greater proportion of cytosolic cpx to be able to bind to the SNARE complex (including syntaxin [yellow]/Munc-18 [red], SNAP-25 [dark purple], synaptobrevin [purple]) to compete with synaptotagmin [blue] binding and prevent fusion because of its clamping function, which results in reduced transmitter release. This process is reversible and depends on the availability of GSH-dependent de-nitrosylation of cpx. GSH is generated by GCL and GSNO is broken down into G-SS-G and NH 2 OH by GSNOR activity. Cys, cysteine; cpx, complexin; G-SS-G, glutathione disulphide; GCL, glutamate-cysteine ligase; GluR, glutamate receptor; GSH, glutathione; GSNO, S-nitrosoglutathione; GSNOR, S-nitrosoglutathione reductase; NH 2 OH, hydroxylamine; SNARE, soluble N -ethyl-maleimide-sensitive fusion protein Attachment Protein Receptor; SNO, S-nitrosothiol.

Techniques Used: Binding Assay, Generated, Activity Assay

7) Product Images from "Nitric oxide-mediated posttranslational modifications control neurotransmitter release by modulating complexin farnesylation and enhancing its clamping ability"

Article Title: Nitric oxide-mediated posttranslational modifications control neurotransmitter release by modulating complexin farnesylation and enhancing its clamping ability

Journal: PLoS Biology

doi: 10.1371/journal.pbio.2003611

Reduced farnesylation of cpx enhances AZ localization and alters interactions with SNARE proteins. (A) Maximal projection confocal images of w 1118 NMJs in Ctrl, following 60 min of exposure to NO or farnesylation inhibitor (“farnesyl inh”: 10 μM GGTI-298 + 20 μM L-744,832). PLA fluorescence in red and HRP staining in green for: left, syntaxin-cpx; middle: Brp-cpx; right: synaptotagmin-cpx interactions. (B) Analysis of summated PLA signal volumes relative to NMJ volumes. (C) FRAP experiments were performed at NMJs expressing GFP-cpx, shown as representative images of WT GFP-cpx at different time points (bleaching area: 2.5 μm 2 , scale bar: 2 μm). Right, mean data showing recovery of WT, CpxΔX, and NO-treated WT cpx, with mean tau values summarized. Note, lack of farnesylation due to the mutation or NO treatment results in faster recovery rates. (D) Representative mEJC recordings following 60 min incubation with GGTI-298 + L-744,832 (“farnesyl inh”) or of a larva expressing FTase-RNAi with mean mEJC frequencies. (E) Trains of 50-Hz stimulation of a larva incubated for 60 min with GGTI-298 + L-744,832 (“farnesyl inh”) or expressing FTase-RNAi with mean eEJC amplitudes and QC. (F) Cumulative QC of 50-Hz trains with mean estimated RRP sizes (right). The raw data can be found in S7 Data . Data denote mean ± SEM, Student t test, or ANOVA with post hoc Tukey-Kramer as indicated, * p
Figure Legend Snippet: Reduced farnesylation of cpx enhances AZ localization and alters interactions with SNARE proteins. (A) Maximal projection confocal images of w 1118 NMJs in Ctrl, following 60 min of exposure to NO or farnesylation inhibitor (“farnesyl inh”: 10 μM GGTI-298 + 20 μM L-744,832). PLA fluorescence in red and HRP staining in green for: left, syntaxin-cpx; middle: Brp-cpx; right: synaptotagmin-cpx interactions. (B) Analysis of summated PLA signal volumes relative to NMJ volumes. (C) FRAP experiments were performed at NMJs expressing GFP-cpx, shown as representative images of WT GFP-cpx at different time points (bleaching area: 2.5 μm 2 , scale bar: 2 μm). Right, mean data showing recovery of WT, CpxΔX, and NO-treated WT cpx, with mean tau values summarized. Note, lack of farnesylation due to the mutation or NO treatment results in faster recovery rates. (D) Representative mEJC recordings following 60 min incubation with GGTI-298 + L-744,832 (“farnesyl inh”) or of a larva expressing FTase-RNAi with mean mEJC frequencies. (E) Trains of 50-Hz stimulation of a larva incubated for 60 min with GGTI-298 + L-744,832 (“farnesyl inh”) or expressing FTase-RNAi with mean eEJC amplitudes and QC. (F) Cumulative QC of 50-Hz trains with mean estimated RRP sizes (right). The raw data can be found in S7 Data . Data denote mean ± SEM, Student t test, or ANOVA with post hoc Tukey-Kramer as indicated, * p

Techniques Used: Proximity Ligation Assay, Fluorescence, Staining, Expressing, Mutagenesis, Incubation

Effects of SNO formation on farnesylation and cpx function. (A) The farnesyl transferase facilitates the addition of a farnesyl group to cpx (green) containing the CAAX motif. Upon S-nitrosylation, this motif is not recognized and the protein will not be farnesylated, resulting in lack of endomembrane targeting. (B) The schematic shows the effects of S-nitrosylation of cpx Cys within CAAX, resulting in fewer proteins being farnesylated and tethered to endomembranes. This allows a greater proportion of cytosolic cpx to be able to bind to the SNARE complex (including syntaxin [yellow]/Munc-18 [red], SNAP-25 [dark purple], synaptobrevin [purple]) to compete with synaptotagmin [blue] binding and prevent fusion because of its clamping function, which results in reduced transmitter release. This process is reversible and depends on the availability of GSH-dependent de-nitrosylation of cpx. GSH is generated by GCL and GSNO is broken down into G-SS-G and NH 2 OH by GSNOR activity. Cys, cysteine; cpx, complexin; G-SS-G, glutathione disulphide; GCL, glutamate-cysteine ligase; GluR, glutamate receptor; GSH, glutathione; GSNO, S-nitrosoglutathione; GSNOR, S-nitrosoglutathione reductase; NH 2 OH, hydroxylamine; SNARE, soluble N -ethyl-maleimide-sensitive fusion protein Attachment Protein Receptor; SNO, S-nitrosothiol.
Figure Legend Snippet: Effects of SNO formation on farnesylation and cpx function. (A) The farnesyl transferase facilitates the addition of a farnesyl group to cpx (green) containing the CAAX motif. Upon S-nitrosylation, this motif is not recognized and the protein will not be farnesylated, resulting in lack of endomembrane targeting. (B) The schematic shows the effects of S-nitrosylation of cpx Cys within CAAX, resulting in fewer proteins being farnesylated and tethered to endomembranes. This allows a greater proportion of cytosolic cpx to be able to bind to the SNARE complex (including syntaxin [yellow]/Munc-18 [red], SNAP-25 [dark purple], synaptobrevin [purple]) to compete with synaptotagmin [blue] binding and prevent fusion because of its clamping function, which results in reduced transmitter release. This process is reversible and depends on the availability of GSH-dependent de-nitrosylation of cpx. GSH is generated by GCL and GSNO is broken down into G-SS-G and NH 2 OH by GSNOR activity. Cys, cysteine; cpx, complexin; G-SS-G, glutathione disulphide; GCL, glutamate-cysteine ligase; GluR, glutamate receptor; GSH, glutathione; GSNO, S-nitrosoglutathione; GSNOR, S-nitrosoglutathione reductase; NH 2 OH, hydroxylamine; SNARE, soluble N -ethyl-maleimide-sensitive fusion protein Attachment Protein Receptor; SNO, S-nitrosothiol.

Techniques Used: Binding Assay, Generated, Activity Assay

8) Product Images from "Nitric oxide-mediated posttranslational modifications control neurotransmitter release by modulating complexin farnesylation and enhancing its clamping ability"

Article Title: Nitric oxide-mediated posttranslational modifications control neurotransmitter release by modulating complexin farnesylation and enhancing its clamping ability

Journal: PLoS Biology

doi: 10.1371/journal.pbio.2003611

Reduced farnesylation of cpx enhances AZ localization and alters interactions with SNARE proteins. (A) Maximal projection confocal images of w 1118 NMJs in Ctrl, following 60 min of exposure to NO or farnesylation inhibitor (“farnesyl inh”: 10 μM GGTI-298 + 20 μM L-744,832). PLA fluorescence in red and HRP staining in green for: left, syntaxin-cpx; middle: Brp-cpx; right: synaptotagmin-cpx interactions. (B) Analysis of summated PLA signal volumes relative to NMJ volumes. (C) FRAP experiments were performed at NMJs expressing GFP-cpx, shown as representative images of WT GFP-cpx at different time points (bleaching area: 2.5 μm 2 , scale bar: 2 μm). Right, mean data showing recovery of WT, CpxΔX, and NO-treated WT cpx, with mean tau values summarized. Note, lack of farnesylation due to the mutation or NO treatment results in faster recovery rates. (D) Representative mEJC recordings following 60 min incubation with GGTI-298 + L-744,832 (“farnesyl inh”) or of a larva expressing FTase-RNAi with mean mEJC frequencies. (E) Trains of 50-Hz stimulation of a larva incubated for 60 min with GGTI-298 + L-744,832 (“farnesyl inh”) or expressing FTase-RNAi with mean eEJC amplitudes and QC. (F) Cumulative QC of 50-Hz trains with mean estimated RRP sizes (right). The raw data can be found in S7 Data . Data denote mean ± SEM, Student t test, or ANOVA with post hoc Tukey-Kramer as indicated, * p
Figure Legend Snippet: Reduced farnesylation of cpx enhances AZ localization and alters interactions with SNARE proteins. (A) Maximal projection confocal images of w 1118 NMJs in Ctrl, following 60 min of exposure to NO or farnesylation inhibitor (“farnesyl inh”: 10 μM GGTI-298 + 20 μM L-744,832). PLA fluorescence in red and HRP staining in green for: left, syntaxin-cpx; middle: Brp-cpx; right: synaptotagmin-cpx interactions. (B) Analysis of summated PLA signal volumes relative to NMJ volumes. (C) FRAP experiments were performed at NMJs expressing GFP-cpx, shown as representative images of WT GFP-cpx at different time points (bleaching area: 2.5 μm 2 , scale bar: 2 μm). Right, mean data showing recovery of WT, CpxΔX, and NO-treated WT cpx, with mean tau values summarized. Note, lack of farnesylation due to the mutation or NO treatment results in faster recovery rates. (D) Representative mEJC recordings following 60 min incubation with GGTI-298 + L-744,832 (“farnesyl inh”) or of a larva expressing FTase-RNAi with mean mEJC frequencies. (E) Trains of 50-Hz stimulation of a larva incubated for 60 min with GGTI-298 + L-744,832 (“farnesyl inh”) or expressing FTase-RNAi with mean eEJC amplitudes and QC. (F) Cumulative QC of 50-Hz trains with mean estimated RRP sizes (right). The raw data can be found in S7 Data . Data denote mean ± SEM, Student t test, or ANOVA with post hoc Tukey-Kramer as indicated, * p

Techniques Used: Proximity Ligation Assay, Fluorescence, Staining, Expressing, Mutagenesis, Incubation

Effects of SNO formation on farnesylation and cpx function. (A) The farnesyl transferase facilitates the addition of a farnesyl group to cpx (green) containing the CAAX motif. Upon S-nitrosylation, this motif is not recognized and the protein will not be farnesylated, resulting in lack of endomembrane targeting. (B) The schematic shows the effects of S-nitrosylation of cpx Cys within CAAX, resulting in fewer proteins being farnesylated and tethered to endomembranes. This allows a greater proportion of cytosolic cpx to be able to bind to the SNARE complex (including syntaxin [yellow]/Munc-18 [red], SNAP-25 [dark purple], synaptobrevin [purple]) to compete with synaptotagmin [blue] binding and prevent fusion because of its clamping function, which results in reduced transmitter release. This process is reversible and depends on the availability of GSH-dependent de-nitrosylation of cpx. GSH is generated by GCL and GSNO is broken down into G-SS-G and NH 2 OH by GSNOR activity. Cys, cysteine; cpx, complexin; G-SS-G, glutathione disulphide; GCL, glutamate-cysteine ligase; GluR, glutamate receptor; GSH, glutathione; GSNO, S-nitrosoglutathione; GSNOR, S-nitrosoglutathione reductase; NH 2 OH, hydroxylamine; SNARE, soluble N -ethyl-maleimide-sensitive fusion protein Attachment Protein Receptor; SNO, S-nitrosothiol.
Figure Legend Snippet: Effects of SNO formation on farnesylation and cpx function. (A) The farnesyl transferase facilitates the addition of a farnesyl group to cpx (green) containing the CAAX motif. Upon S-nitrosylation, this motif is not recognized and the protein will not be farnesylated, resulting in lack of endomembrane targeting. (B) The schematic shows the effects of S-nitrosylation of cpx Cys within CAAX, resulting in fewer proteins being farnesylated and tethered to endomembranes. This allows a greater proportion of cytosolic cpx to be able to bind to the SNARE complex (including syntaxin [yellow]/Munc-18 [red], SNAP-25 [dark purple], synaptobrevin [purple]) to compete with synaptotagmin [blue] binding and prevent fusion because of its clamping function, which results in reduced transmitter release. This process is reversible and depends on the availability of GSH-dependent de-nitrosylation of cpx. GSH is generated by GCL and GSNO is broken down into G-SS-G and NH 2 OH by GSNOR activity. Cys, cysteine; cpx, complexin; G-SS-G, glutathione disulphide; GCL, glutamate-cysteine ligase; GluR, glutamate receptor; GSH, glutathione; GSNO, S-nitrosoglutathione; GSNOR, S-nitrosoglutathione reductase; NH 2 OH, hydroxylamine; SNARE, soluble N -ethyl-maleimide-sensitive fusion protein Attachment Protein Receptor; SNO, S-nitrosothiol.

Techniques Used: Binding Assay, Generated, Activity Assay

9) Product Images from "Nitric oxide-mediated posttranslational modifications control neurotransmitter release by modulating complexin farnesylation and enhancing its clamping ability"

Article Title: Nitric oxide-mediated posttranslational modifications control neurotransmitter release by modulating complexin farnesylation and enhancing its clamping ability

Journal: PLoS Biology

doi: 10.1371/journal.pbio.2003611

Reduced farnesylation of cpx enhances AZ localization and alters interactions with SNARE proteins. (A) Maximal projection confocal images of w 1118 NMJs in Ctrl, following 60 min of exposure to NO or farnesylation inhibitor (“farnesyl inh”: 10 μM GGTI-298 + 20 μM L-744,832). PLA fluorescence in red and HRP staining in green for: left, syntaxin-cpx; middle: Brp-cpx; right: synaptotagmin-cpx interactions. (B) Analysis of summated PLA signal volumes relative to NMJ volumes. (C) FRAP experiments were performed at NMJs expressing GFP-cpx, shown as representative images of WT GFP-cpx at different time points (bleaching area: 2.5 μm 2 . Data denote mean ± SEM, Student t test, or ANOVA with post hoc Tukey-Kramer as indicated, * p
Figure Legend Snippet: Reduced farnesylation of cpx enhances AZ localization and alters interactions with SNARE proteins. (A) Maximal projection confocal images of w 1118 NMJs in Ctrl, following 60 min of exposure to NO or farnesylation inhibitor (“farnesyl inh”: 10 μM GGTI-298 + 20 μM L-744,832). PLA fluorescence in red and HRP staining in green for: left, syntaxin-cpx; middle: Brp-cpx; right: synaptotagmin-cpx interactions. (B) Analysis of summated PLA signal volumes relative to NMJ volumes. (C) FRAP experiments were performed at NMJs expressing GFP-cpx, shown as representative images of WT GFP-cpx at different time points (bleaching area: 2.5 μm 2 . Data denote mean ± SEM, Student t test, or ANOVA with post hoc Tukey-Kramer as indicated, * p

Techniques Used: Proximity Ligation Assay, Fluorescence, Staining, Expressing

Effects of SNO formation on farnesylation and cpx function. (A) The farnesyl transferase facilitates the addition of a farnesyl group to cpx (green) containing the CAAX motif. Upon S-nitrosylation, this motif is not recognized and the protein will not be farnesylated, resulting in lack of endomembrane targeting. (B) The schematic shows the effects of S-nitrosylation of cpx Cys within CAAX, resulting in fewer proteins being farnesylated and tethered to endomembranes. This allows a greater proportion of cytosolic cpx to be able to bind to the SNARE complex (including syntaxin [yellow]/Munc-18 [red], SNAP-25 [dark purple], synaptobrevin [purple]) to compete with synaptotagmin [blue] binding and prevent fusion because of its clamping function, which results in reduced transmitter release. This process is reversible and depends on the availability of GSH-dependent de-nitrosylation of cpx. GSH is generated by GCL and GSNO is broken down into G-SS-G and NH 2 OH by GSNOR activity. Cys, cysteine; cpx, complexin; G-SS-G, glutathione disulphide; GCL, glutamate-cysteine ligase; GluR, glutamate receptor; GSH, glutathione; GSNO, S-nitrosoglutathione; GSNOR, S-nitrosoglutathione reductase; NH 2 OH, hydroxylamine; SNARE, soluble N -ethyl-maleimide-sensitive fusion protein Attachment Protein Receptor; SNO, S-nitrosothiol.
Figure Legend Snippet: Effects of SNO formation on farnesylation and cpx function. (A) The farnesyl transferase facilitates the addition of a farnesyl group to cpx (green) containing the CAAX motif. Upon S-nitrosylation, this motif is not recognized and the protein will not be farnesylated, resulting in lack of endomembrane targeting. (B) The schematic shows the effects of S-nitrosylation of cpx Cys within CAAX, resulting in fewer proteins being farnesylated and tethered to endomembranes. This allows a greater proportion of cytosolic cpx to be able to bind to the SNARE complex (including syntaxin [yellow]/Munc-18 [red], SNAP-25 [dark purple], synaptobrevin [purple]) to compete with synaptotagmin [blue] binding and prevent fusion because of its clamping function, which results in reduced transmitter release. This process is reversible and depends on the availability of GSH-dependent de-nitrosylation of cpx. GSH is generated by GCL and GSNO is broken down into G-SS-G and NH 2 OH by GSNOR activity. Cys, cysteine; cpx, complexin; G-SS-G, glutathione disulphide; GCL, glutamate-cysteine ligase; GluR, glutamate receptor; GSH, glutathione; GSNO, S-nitrosoglutathione; GSNOR, S-nitrosoglutathione reductase; NH 2 OH, hydroxylamine; SNARE, soluble N -ethyl-maleimide-sensitive fusion protein Attachment Protein Receptor; SNO, S-nitrosothiol.

Techniques Used: Binding Assay, Generated, Activity Assay

10) Product Images from "Cortical Synaptic Transmission and Plasticity in Acute Liver Failure Are Decreased by Presynaptic Events"

Article Title: Cortical Synaptic Transmission and Plasticity in Acute Liver Failure Are Decreased by Presynaptic Events

Journal: Molecular Neurobiology

doi: 10.1007/s12035-016-0367-4

Protein content of selected presynaptic proteins. a Purity of S2 and P2 fraction. b Synaptophysin, synaptotagmin-1, and Munc 18–1 protein contents in the cerebral cortex of control and symptomatic AOM-treated mice shown as membrane (P2) to cytosolic (S2) fraction ratio (P2/S2) ( n = 8), followed by representative electrophorograms. c Syntaxin-1 and vti1A protein contents in membrane fraction (P2) in control and symptomatic AOM-injected mice ( n = 8), followed by representative electrophorograms. d Changes in synaptophysin protein content in cytosolic (S2) and membrane fraction (P2) at prodromal and symptomatic stage of ALF ( n = 6), followed by representative electrophorograms. Asterisk indicates p
Figure Legend Snippet: Protein content of selected presynaptic proteins. a Purity of S2 and P2 fraction. b Synaptophysin, synaptotagmin-1, and Munc 18–1 protein contents in the cerebral cortex of control and symptomatic AOM-treated mice shown as membrane (P2) to cytosolic (S2) fraction ratio (P2/S2) ( n = 8), followed by representative electrophorograms. c Syntaxin-1 and vti1A protein contents in membrane fraction (P2) in control and symptomatic AOM-injected mice ( n = 8), followed by representative electrophorograms. d Changes in synaptophysin protein content in cytosolic (S2) and membrane fraction (P2) at prodromal and symptomatic stage of ALF ( n = 6), followed by representative electrophorograms. Asterisk indicates p

Techniques Used: Mouse Assay, Injection

11) Product Images from "Cortical Synaptic Transmission and Plasticity in Acute Liver Failure Are Decreased by Presynaptic Events"

Article Title: Cortical Synaptic Transmission and Plasticity in Acute Liver Failure Are Decreased by Presynaptic Events

Journal: Molecular Neurobiology

doi: 10.1007/s12035-016-0367-4

Protein content of selected presynaptic proteins. a Purity of S2 and P2 fraction. b Synaptophysin, synaptotagmin-1, and Munc 18–1 protein contents in the cerebral cortex of control and symptomatic AOM-treated mice shown as membrane (P2) to cytosolic (S2) fraction ratio (P2/S2) ( n = 8), followed by representative electrophorograms. c Syntaxin-1 and vti1A protein contents in membrane fraction (P2) in control and symptomatic AOM-injected mice ( n = 8), followed by representative electrophorograms. d Changes in synaptophysin protein content in cytosolic (S2) and membrane fraction (P2) at prodromal and symptomatic stage of ALF ( n = 6), followed by representative electrophorograms. Asterisk indicates p
Figure Legend Snippet: Protein content of selected presynaptic proteins. a Purity of S2 and P2 fraction. b Synaptophysin, synaptotagmin-1, and Munc 18–1 protein contents in the cerebral cortex of control and symptomatic AOM-treated mice shown as membrane (P2) to cytosolic (S2) fraction ratio (P2/S2) ( n = 8), followed by representative electrophorograms. c Syntaxin-1 and vti1A protein contents in membrane fraction (P2) in control and symptomatic AOM-injected mice ( n = 8), followed by representative electrophorograms. d Changes in synaptophysin protein content in cytosolic (S2) and membrane fraction (P2) at prodromal and symptomatic stage of ALF ( n = 6), followed by representative electrophorograms. Asterisk indicates p

Techniques Used: Mouse Assay, Injection

12) Product Images from "The Multifaceted Role of SNARE Proteins in Membrane Fusion"

Article Title: The Multifaceted Role of SNARE Proteins in Membrane Fusion

Journal: Frontiers in Physiology

doi: 10.3389/fphys.2017.00005

Structure of the Ca 2+ -bound synaptotagmin 1-SNARE complex (Zhou et al., 2015 ) . SNAP25 shown in green, synaptobrevin in blue, syntaxin-1A in red, one copy of synaptotagmin-1 in violet and one in yellow.
Figure Legend Snippet: Structure of the Ca 2+ -bound synaptotagmin 1-SNARE complex (Zhou et al., 2015 ) . SNAP25 shown in green, synaptobrevin in blue, syntaxin-1A in red, one copy of synaptotagmin-1 in violet and one in yellow.

Techniques Used:

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