Structured Review

Syntaxin ca2
Frequency dependence of presynaptic <t>Ca2+</t> entry and Ca2+  clearance
Ca2, supplied by Syntaxin, used in various techniques. Bioz Stars score: 92/100, based on 25 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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ca2 - by Bioz Stars, 2020-11
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Images

1) Product Images from "Cysteine-String Protein Increases the Calcium Sensitivity of Neurotransmitter Exocytosis in Drosophila"

Article Title: Cysteine-String Protein Increases the Calcium Sensitivity of Neurotransmitter Exocytosis in Drosophila

Journal: The Journal of Neuroscience

doi: 10.1523/JNEUROSCI.20-16-06039.2000

Frequency dependence of presynaptic Ca2+ entry and Ca2+  clearance
Figure Legend Snippet: Frequency dependence of presynaptic Ca2+ entry and Ca2+  clearance

Techniques Used:

2) Product Images from "Cysteine-String Protein Increases the Calcium Sensitivity of Neurotransmitter Exocytosis in Drosophila"

Article Title: Cysteine-String Protein Increases the Calcium Sensitivity of Neurotransmitter Exocytosis in Drosophila

Journal: The Journal of Neuroscience

doi: 10.1523/JNEUROSCI.20-16-06039.2000

Frequency dependence of presynaptic Ca2+ entry and Ca2+ clearance
Figure Legend Snippet: Frequency dependence of presynaptic Ca2+ entry and Ca2+ clearance

Techniques Used:

3) Product Images from "Cysteine-String Protein Increases the Calcium Sensitivity of Neurotransmitter Exocytosis in Drosophila"

Article Title: Cysteine-String Protein Increases the Calcium Sensitivity of Neurotransmitter Exocytosis in Drosophila

Journal: The Journal of Neuroscience

doi: 10.1523/JNEUROSCI.20-16-06039.2000

Frequency dependence of presynaptic Ca2+ entry and Ca2+ clearance
Figure Legend Snippet: Frequency dependence of presynaptic Ca2+ entry and Ca2+ clearance

Techniques Used:

4) Product Images from "Synaptotagmin I delays the fast inactivation of Kv1.4 channel through interaction with its N-terminus"

Article Title: Synaptotagmin I delays the fast inactivation of Kv1.4 channel through interaction with its N-terminus

Journal: Molecular Brain

doi: 10.1186/1756-6606-7-4

Validation of interaction between synaptotagmin I and Kv1.4 channel. (A) Silver-stained SDS-PAGE of the protein complexes affinity purified from rat hippocampal plasma membrane-enriched fraction either with a Kv1.4-specific antibody (anti-Kv1.4) or a preimmunisation IgG pool (Pre-IgG). Arrowheads denote the bands identified by nano-LC tandem mass spectrometry as Kv1.4 and synaptotagmin I, respectively. (B) Western blot showing reverse purification of Kv1.4 from the same fraction with anti-synaptotagmin I. (C) Immunohistochemical analysis of the colocalization of synaptotagmin I and Kv1.4 in rat hippocampus. (a)-(c) show the localizations of pyramidal cell nuclei, Kv1.4 and synaptotagmin I in the CA2- CA3 regions, respectively. (d)-(f) show the localizations of pyramidal cell nuclei, Kv1.4 and synaptotagmin I in the CA1 region and denote gyrus, respectively. (g)-(i) are the enlarged images of CA3 region showing the localizations of Kv1.4 (g), synaptotagmin I (h) and their colocalization (i) in this region.
Figure Legend Snippet: Validation of interaction between synaptotagmin I and Kv1.4 channel. (A) Silver-stained SDS-PAGE of the protein complexes affinity purified from rat hippocampal plasma membrane-enriched fraction either with a Kv1.4-specific antibody (anti-Kv1.4) or a preimmunisation IgG pool (Pre-IgG). Arrowheads denote the bands identified by nano-LC tandem mass spectrometry as Kv1.4 and synaptotagmin I, respectively. (B) Western blot showing reverse purification of Kv1.4 from the same fraction with anti-synaptotagmin I. (C) Immunohistochemical analysis of the colocalization of synaptotagmin I and Kv1.4 in rat hippocampus. (a)-(c) show the localizations of pyramidal cell nuclei, Kv1.4 and synaptotagmin I in the CA2- CA3 regions, respectively. (d)-(f) show the localizations of pyramidal cell nuclei, Kv1.4 and synaptotagmin I in the CA1 region and denote gyrus, respectively. (g)-(i) are the enlarged images of CA3 region showing the localizations of Kv1.4 (g), synaptotagmin I (h) and their colocalization (i) in this region.

Techniques Used: Staining, SDS Page, Affinity Purification, Mass Spectrometry, Western Blot, Purification, Immunohistochemistry

5) Product Images from "Synaptic proteins as multi-sensor devices of neurotransmission"

Article Title: Synaptic proteins as multi-sensor devices of neurotransmission

Journal: BMC Neuroscience

doi: 10.1186/1471-2202-7-S1-S4

Schematic illustration of the Ca2+ occupancy states for Syt1. The maximal number of Ca2+ ions (symbolized as red ovals) that can bind C2A is 3 (marked as 1,2,3) and 2 (marked as 4, 5) for the C2B. The blue and purple lines represent all potential states ranging from no binding to maximal occupancy by 5 ions. Total of 12 edges representing Syt1 states assuming the actual position of the ions within C2A or C2B is not important. Addition of the positional information increases the number of Ca2+ occupancy states as illustrated by the purple edges. The number of individual states associated with the purple edges summarizes to ten combinations of occupancy of 3 Ca2+ ions. With positional information for Ca2+ ions occupancy the number of individual states reaches 32 (1 state for no occupancy, 5 states for one ion, 10 states for 2 ions, 10 states for 3 ions, 5 states for 4 ions and another state for occupancy of 5 ions).
Figure Legend Snippet: Schematic illustration of the Ca2+ occupancy states for Syt1. The maximal number of Ca2+ ions (symbolized as red ovals) that can bind C2A is 3 (marked as 1,2,3) and 2 (marked as 4, 5) for the C2B. The blue and purple lines represent all potential states ranging from no binding to maximal occupancy by 5 ions. Total of 12 edges representing Syt1 states assuming the actual position of the ions within C2A or C2B is not important. Addition of the positional information increases the number of Ca2+ occupancy states as illustrated by the purple edges. The number of individual states associated with the purple edges summarizes to ten combinations of occupancy of 3 Ca2+ ions. With positional information for Ca2+ ions occupancy the number of individual states reaches 32 (1 state for no occupancy, 5 states for one ion, 10 states for 2 ions, 10 states for 3 ions, 5 states for 4 ions and another state for occupancy of 5 ions).

Techniques Used: Binding Assay

6) Product Images from "Cysteine-String Protein Increases the Calcium Sensitivity of Neurotransmitter Exocytosis in Drosophila"

Article Title: Cysteine-String Protein Increases the Calcium Sensitivity of Neurotransmitter Exocytosis in Drosophila

Journal: The Journal of Neuroscience

doi: 10.1523/JNEUROSCI.20-16-06039.2000

Frequency dependence of presynaptic Ca2+ entry and Ca2+  clearance
Figure Legend Snippet: Frequency dependence of presynaptic Ca2+ entry and Ca2+  clearance

Techniques Used:

Related Articles

Modification:

Article Title: Synaptotagmin I delays the fast inactivation of Kv1.4 channel through interaction with its N-terminus
Article Snippet: .. A series of studies have demonstrated that the activity of Ca2+ channels is modified by syntaxin, synaptotagmin I and SNAP-25 alone, or in various combinations [ - ]. .. During the investigation of possible association of Na+ channels with synaptic proteins, Sampo et al. [ ] found that synaptotagmin I displayed a direct high affinity interaction with neuronal voltage-sensitive Na+ channels, with the binding site on the cytosolic loop between domains I and II of the Na+ channel αIIA subunit.

Isolation:

Article Title:
Article Snippet: .. Using isolated synaptic vesicles, it was reported that vesicular synaptobrevin is not reactive but requires Ca2+ to interact with syntaxin and SNAP-25, suggesting regulation by a Ca2+ -binding protein such as synaptotagmin ( ). ..

Binding Assay:

Article Title:
Article Snippet: .. Using isolated synaptic vesicles, it was reported that vesicular synaptobrevin is not reactive but requires Ca2+ to interact with syntaxin and SNAP-25, suggesting regulation by a Ca2+ -binding protein such as synaptotagmin ( ). ..

Article Title: Synaptic proteins as multi-sensor devices of neurotransmission
Article Snippet: .. A short conserved region of polybasic residues (Fig , KK) in the C2B domain was shown to be critical for the Ca2+-dependent NT release and also for the binding to syntaxin-SNAP25 pair. ..

Activity Assay:

Article Title: Synaptotagmin I delays the fast inactivation of Kv1.4 channel through interaction with its N-terminus
Article Snippet: .. A series of studies have demonstrated that the activity of Ca2+ channels is modified by syntaxin, synaptotagmin I and SNAP-25 alone, or in various combinations [ - ]. .. During the investigation of possible association of Na+ channels with synaptic proteins, Sampo et al. [ ] found that synaptotagmin I displayed a direct high affinity interaction with neuronal voltage-sensitive Na+ channels, with the binding site on the cytosolic loop between domains I and II of the Na+ channel αIIA subunit.

Article Title: Cysteine-String Protein Increases the Calcium Sensitivity of Neurotransmitter Exocytosis in Drosophila
Article Snippet: .. Because CSP is an effective competitor of the syntaxin–synprint site interaction in vitro , it has been suggested that CSP may dissociate syntaxin from Ca2+ channels to promote channel activity ( ; ; ; ). .. However, this possibility is not consistent with our in vivo studies revealing increased stimulus-evoked cytosolic Ca2+ levels in csp mutants.

Article Title: Cysteine-String Protein Increases the Calcium Sensitivity of Neurotransmitter Exocytosis in Drosophila
Article Snippet: .. Because CSP is an effective competitor of the syntaxin–synprint site interaction in vitro , it has been suggested that CSP may dissociate syntaxin from Ca2+ channels to promote channel activity ( ; ; ; ). .. However, this possibility is not consistent with our in vivo studies revealing increased stimulus-evoked cytosolic Ca2+ levels in csp mutants.

In Vitro:

Article Title: Cysteine-String Protein Increases the Calcium Sensitivity of Neurotransmitter Exocytosis in Drosophila
Article Snippet: .. Because CSP is an effective competitor of the syntaxin–synprint site interaction in vitro , it has been suggested that CSP may dissociate syntaxin from Ca2+ channels to promote channel activity ( ; ; ; ). .. However, this possibility is not consistent with our in vivo studies revealing increased stimulus-evoked cytosolic Ca2+ levels in csp mutants.

Article Title: Cysteine-String Protein Increases the Calcium Sensitivity of Neurotransmitter Exocytosis in Drosophila
Article Snippet: .. Because CSP is an effective competitor of the syntaxin–synprint site interaction in vitro , it has been suggested that CSP may dissociate syntaxin from Ca2+ channels to promote channel activity ( ; ; ; ). .. However, this possibility is not consistent with our in vivo studies revealing increased stimulus-evoked cytosolic Ca2+ levels in csp mutants.

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    Syntaxin ca2 dependence
    <t>Ca2+</t> CURRENT TYPES DEFINED BY PHYSIOLOGICAL AND PHARMACOLOGICAL PROPERTIES
    Ca2 Dependence, supplied by Syntaxin, used in various techniques. Bioz Stars score: 89/100, based on 27 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/result/ca2 dependence/product/Syntaxin
    Average 89 stars, based on 27 article reviews
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    89
    Syntaxin brain ca2
    A leftward shift in the EPSC–presynaptic <t>Ca2+</t> charge relation during development
    Brain Ca2, supplied by Syntaxin, used in various techniques. Bioz Stars score: 89/100, based on 3 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    90
    Syntaxin presynaptic ca2
    Probing nanodomains and microdomains with exogenous <t>Ca2+</t> chelators
    Presynaptic Ca2, supplied by Syntaxin, used in various techniques. Bioz Stars score: 90/100, based on 2 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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    Average 90 stars, based on 2 article reviews
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    Image Search Results


    Ca2+ CURRENT TYPES DEFINED BY PHYSIOLOGICAL AND PHARMACOLOGICAL PROPERTIES

    Journal: Cold Spring Harbor Perspectives in Biology

    Article Title: Voltage-Gated Calcium Channels

    doi: 10.1101/cshperspect.a003947

    Figure Lengend Snippet: Ca2+ CURRENT TYPES DEFINED BY PHYSIOLOGICAL AND PHARMACOLOGICAL PROPERTIES

    Article Snippet: Alteration of Ca2+ dependence of neurotransmitter release by disruption of Ca2+ channel/syntaxin interaction .

    Techniques:

    Frequency dependence of presynaptic Ca2+ entry and Ca2+  clearance

    Journal: The Journal of Neuroscience

    Article Title: Cysteine-String Protein Increases the Calcium Sensitivity of Neurotransmitter Exocytosis in Drosophila

    doi: 10.1523/JNEUROSCI.20-16-06039.2000

    Figure Lengend Snippet: Frequency dependence of presynaptic Ca2+ entry and Ca2+  clearance

    Article Snippet: The synprint site mediates interactions of multiple synaptic proteins with Ca2+ channels, including syntaxin, synaptotagmin, and SNAP25 (for review, see ; ).

    Techniques:

    A leftward shift in the EPSC–presynaptic Ca2+ charge relation during development

    Journal: The Journal of Physiology

    Article Title: Developmental regulation of the intracellular Ca2+ sensitivity of vesicle fusion and Ca2+-secretion coupling at the rat calyx of Held

    doi: 10.1113/jphysiol.2009.172387

    Figure Lengend Snippet: A leftward shift in the EPSC–presynaptic Ca2+ charge relation during development

    Article Snippet: Isoform-specific interaction of theα1A subunits of brain Ca2+ channels with the presynaptic proteins syntaxin and SNAP-25.

    Techniques:

    Probing nanodomains and microdomains with exogenous Ca2+ chelators

    Journal: Nature reviews. Neuroscience

    Article Title: Nanodomain coupling between Ca2+ channels and sensors of exocytosis at fast mammalian synapses

    doi: 10.1038/nrn3125

    Figure Lengend Snippet: Probing nanodomains and microdomains with exogenous Ca2+ chelators

    Article Snippet: The first presynaptic proteins shown to be involved in protein-protein interactions with presynaptic Ca2+ channels were the t-SNARE proteins, syntaxin and SNAP25.

    Techniques: