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    Alomone Labs anti cav2 3
    KCTDs directly bind <t>Cav2.3</t> in vitro and KCTD8 enhances currents through <t>Cav2.3</t> A Co-immunoprecipitation from total cell lysates of HEK293 cells transfected with Flag-tagged KCTDs and Cav2.3. Immunoprecipitation of Cav2.3 co-precipitated KCTD8 and KCTD12b, but not KCTD12. Input lanes (bottom) indicate expression of the tagged proteins in the cell lysates. B Whole-cell recordings from HEK293 cells stably expressing Cav2.3. Ba 2+ current densities measured in response to a single depolarizing voltage step from −80 to 10 mV were significantly increased in KCTD8 co-transfected cells. * P
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    KCTDs directly bind Cav2.3 in vitro and KCTD8 enhances currents through Cav2.3 A Co-immunoprecipitation from total cell lysates of HEK293 cells transfected with Flag-tagged KCTDs and Cav2.3. Immunoprecipitation of Cav2.3 co-precipitated KCTD8 and KCTD12b, but not KCTD12. Input lanes (bottom) indicate expression of the tagged proteins in the cell lysates. B Whole-cell recordings from HEK293 cells stably expressing Cav2.3. Ba 2+ current densities measured in response to a single depolarizing voltage step from −80 to 10 mV were significantly increased in KCTD8 co-transfected cells. * P

    Journal: bioRxiv

    Article Title: GABAB receptor auxiliary subunits modulate Cav2.3-mediated release from medial habenula terminals

    doi: 10.1101/2020.04.16.045112

    Figure Lengend Snippet: KCTDs directly bind Cav2.3 in vitro and KCTD8 enhances currents through Cav2.3 A Co-immunoprecipitation from total cell lysates of HEK293 cells transfected with Flag-tagged KCTDs and Cav2.3. Immunoprecipitation of Cav2.3 co-precipitated KCTD8 and KCTD12b, but not KCTD12. Input lanes (bottom) indicate expression of the tagged proteins in the cell lysates. B Whole-cell recordings from HEK293 cells stably expressing Cav2.3. Ba 2+ current densities measured in response to a single depolarizing voltage step from −80 to 10 mV were significantly increased in KCTD8 co-transfected cells. * P

    Article Snippet: Thereafter, lysates were incubated by rotating for 16 h at 4 °C in the presence of 2.5 μl of 0.3 μg/μl anti-Cav2.3 (CACNA1E) antibody (ACC-006, Alomone Labs, Jerusalem, Israel).

    Techniques: In Vitro, Immunoprecipitation, Transfection, Expressing, Stable Transfection

    Co-localization of Cav2.3 with GBR and KCTDs in the active zone of medial habenula terminals A Active zones double-labeled for Cav2.3 and either GABA B1 (left), KCTD8 (middle) or KCTD12b (right) in IPN replicas. Top row images are from presynaptic terminals in the rostral IPN, bottom row images are from presynaptic terminals in the lateral IPN. Scale bar: 100 nm. B Quantification of active zone immunolabeling in the rostral and lateral IPN. With the exception of the absence of KCTD12b in lateral IPN terminals, absolute particle numbers per active zone (left graph) and particle densities (middle graph) are comparable between MHb terminals in the rostral and lateral IPN. Right graph: Over 97% of active zones positive for Cav2.3 labeling also show labeling for one of the other molecules (GABA B1 , KCTD8 or KCTD12b), suggesting co-localization of all presynaptic molecules inside the same active zone. Numbers inside the bars indicate the number of replicas used for each quantification. C Nearest neighbor distance (NND) for all presynaptic molecules in MHb terminals inside the rostral and lateral IPN based on the real (black line) and simulated random distribution (blue line). Smaller NND values in real distributions compared to simulation suggest clustering of all presynaptic molecules. P values calculated via Kolmogorov-Smirnov test.

    Journal: bioRxiv

    Article Title: GABAB receptor auxiliary subunits modulate Cav2.3-mediated release from medial habenula terminals

    doi: 10.1101/2020.04.16.045112

    Figure Lengend Snippet: Co-localization of Cav2.3 with GBR and KCTDs in the active zone of medial habenula terminals A Active zones double-labeled for Cav2.3 and either GABA B1 (left), KCTD8 (middle) or KCTD12b (right) in IPN replicas. Top row images are from presynaptic terminals in the rostral IPN, bottom row images are from presynaptic terminals in the lateral IPN. Scale bar: 100 nm. B Quantification of active zone immunolabeling in the rostral and lateral IPN. With the exception of the absence of KCTD12b in lateral IPN terminals, absolute particle numbers per active zone (left graph) and particle densities (middle graph) are comparable between MHb terminals in the rostral and lateral IPN. Right graph: Over 97% of active zones positive for Cav2.3 labeling also show labeling for one of the other molecules (GABA B1 , KCTD8 or KCTD12b), suggesting co-localization of all presynaptic molecules inside the same active zone. Numbers inside the bars indicate the number of replicas used for each quantification. C Nearest neighbor distance (NND) for all presynaptic molecules in MHb terminals inside the rostral and lateral IPN based on the real (black line) and simulated random distribution (blue line). Smaller NND values in real distributions compared to simulation suggest clustering of all presynaptic molecules. P values calculated via Kolmogorov-Smirnov test.

    Article Snippet: Thereafter, lysates were incubated by rotating for 16 h at 4 °C in the presence of 2.5 μl of 0.3 μg/μl anti-Cav2.3 (CACNA1E) antibody (ACC-006, Alomone Labs, Jerusalem, Israel).

    Techniques: Labeling, Immunolabeling

    Absence of KCTD12b leads to a compensatory increase of KCTD8 inside the active zone of ventral MHb terminals A Example images of active zones containing Cav2.3 and either GABA B1 (left panels) or KCTD8 (right panels) in replicas of WT (upper row) and KCTD12b KO IPN tissue (lower row). Scale bars: 100 nm B Quantification of relative densities for Cav2.3, KCTD8 and GABA B1 in active zones located in the rostral IPN of WT and KCTD12b KO mice. Densities were normalized to the average density in MHb terminals inside the lateral IPN of the same replica. The number inside the bars indicate the number of replicas used for quantification. ** indicate P

    Journal: bioRxiv

    Article Title: GABAB receptor auxiliary subunits modulate Cav2.3-mediated release from medial habenula terminals

    doi: 10.1101/2020.04.16.045112

    Figure Lengend Snippet: Absence of KCTD12b leads to a compensatory increase of KCTD8 inside the active zone of ventral MHb terminals A Example images of active zones containing Cav2.3 and either GABA B1 (left panels) or KCTD8 (right panels) in replicas of WT (upper row) and KCTD12b KO IPN tissue (lower row). Scale bars: 100 nm B Quantification of relative densities for Cav2.3, KCTD8 and GABA B1 in active zones located in the rostral IPN of WT and KCTD12b KO mice. Densities were normalized to the average density in MHb terminals inside the lateral IPN of the same replica. The number inside the bars indicate the number of replicas used for quantification. ** indicate P

    Article Snippet: Thereafter, lysates were incubated by rotating for 16 h at 4 °C in the presence of 2.5 μl of 0.3 μg/μl anti-Cav2.3 (CACNA1E) antibody (ACC-006, Alomone Labs, Jerusalem, Israel).

    Techniques: Mouse Assay

    Expression and function of Cav2.3 and GABA B receptors at two parallel MHb-IPN pathways A Schematic drawing of the two MHb-IPN pathways. In red: the dorsal part of the MHb projects to the lateral subnuclei of the IPN. In blue: the ventral part of the MHb projects to the rostral/central subnuclei of the IPN. B Confocal image of Cav2.3 immunofluorescence signal indicates Cav2.3 presence in MHb axonal projections of both MHb-IPN pathways. C Pharmacological inhibition of Cav2.3 with SNX-482 in whole-cell recordings of rostral IPN neurons. Left: example traces before and after the application of SNX-482; middle: example time course of EPSC amplitude reduction by SNX-482; right: averaged time course of relative EPSC amplitude reduction by SNX-482. EPSC amplitudes were reduced by 83% on average (n=9 cells/9 mice). D In Tac1-ChR2-EYFP mice, SNX-482 reduced light-evoked glutamatergic EPSC amplitudes on average by 52% (n=8 cells/4 mice). E Confocal image of GABA B1 immunofluorescence signal indicates the presence of GABA B receptors (GBRs) in all IPN subnuclei. F In whole-cell recordings of rostral IPN neurons, activation of GBRs by baclofen (1 µM) produced a potentiation of electrically evoked EPSC amplitudes. Left: example EPSC traces before (black) and during the application of baclofen (red) and after washout of baclofen (blue); middle: example time course of EPSC amplitudes in one cell; right: averaged time course of relative EPSC amplitude change after baclofen (n=13 cells/9 mice). G Baclofen reduced the amplitude of light-evoked glutamatergic EPSCs in lateral IPN neurons (n=10 cells/5 mice). Scale bars in panels ( B ) and ( E ) are 100 µm. Averaged data is presented as mean ± SEM.

    Journal: bioRxiv

    Article Title: GABAB receptor auxiliary subunits modulate Cav2.3-mediated release from medial habenula terminals

    doi: 10.1101/2020.04.16.045112

    Figure Lengend Snippet: Expression and function of Cav2.3 and GABA B receptors at two parallel MHb-IPN pathways A Schematic drawing of the two MHb-IPN pathways. In red: the dorsal part of the MHb projects to the lateral subnuclei of the IPN. In blue: the ventral part of the MHb projects to the rostral/central subnuclei of the IPN. B Confocal image of Cav2.3 immunofluorescence signal indicates Cav2.3 presence in MHb axonal projections of both MHb-IPN pathways. C Pharmacological inhibition of Cav2.3 with SNX-482 in whole-cell recordings of rostral IPN neurons. Left: example traces before and after the application of SNX-482; middle: example time course of EPSC amplitude reduction by SNX-482; right: averaged time course of relative EPSC amplitude reduction by SNX-482. EPSC amplitudes were reduced by 83% on average (n=9 cells/9 mice). D In Tac1-ChR2-EYFP mice, SNX-482 reduced light-evoked glutamatergic EPSC amplitudes on average by 52% (n=8 cells/4 mice). E Confocal image of GABA B1 immunofluorescence signal indicates the presence of GABA B receptors (GBRs) in all IPN subnuclei. F In whole-cell recordings of rostral IPN neurons, activation of GBRs by baclofen (1 µM) produced a potentiation of electrically evoked EPSC amplitudes. Left: example EPSC traces before (black) and during the application of baclofen (red) and after washout of baclofen (blue); middle: example time course of EPSC amplitudes in one cell; right: averaged time course of relative EPSC amplitude change after baclofen (n=13 cells/9 mice). G Baclofen reduced the amplitude of light-evoked glutamatergic EPSCs in lateral IPN neurons (n=10 cells/5 mice). Scale bars in panels ( B ) and ( E ) are 100 µm. Averaged data is presented as mean ± SEM.

    Article Snippet: Thereafter, lysates were incubated by rotating for 16 h at 4 °C in the presence of 2.5 μl of 0.3 μg/μl anti-Cav2.3 (CACNA1E) antibody (ACC-006, Alomone Labs, Jerusalem, Israel).

    Techniques: Expressing, Immunofluorescence, Inhibition, Mouse Assay, Activation Assay, Produced

    SDS-digested freeze-fracture replica labeling confirms Cav2.3 in the active zone of medial habenula terminals in the IPN A Example image of a grid-glued replica containing the whole IPN. White line indicates demarcation of rostral/central and lateral subnuclei. Scale bar: 20 µm B Example image of a presynaptic P face and a postsynaptic E face of a habenular synapse in the rostral IPN that was double labeled with antibodies against AMPA receptors (10 nm gold) and Cav2.3 (5 nm gold). Scale bar: 100 nm. C Example image of a similar synaptic profile double labeled with antibodies against AMPA receptors (10 nm gold) and Cav2.3 (5 nm gold) in the rostral IPN of a Cav2.3 KO mouse. Scale bar: 100 nm. D Left panel: double labeling of a WT carbon-only replica with antibodies against Cav2.3 (5 nm gold) and a mixture of active zone proteins (2 nm gold), including RIM1/2, CAST and neurexin. Right panel: the same image with additional coloring of 2 nm (red) and 5 nm (blue) particles and demarcation of the active zone area based on active zone marker labeling. Scale bars: 100 nm. F Left panel: quantification of Cav2.3 labeling densities in the presynaptic P face in WT and Cav2.3 KO mice. *** indicates P

    Journal: bioRxiv

    Article Title: GABAB receptor auxiliary subunits modulate Cav2.3-mediated release from medial habenula terminals

    doi: 10.1101/2020.04.16.045112

    Figure Lengend Snippet: SDS-digested freeze-fracture replica labeling confirms Cav2.3 in the active zone of medial habenula terminals in the IPN A Example image of a grid-glued replica containing the whole IPN. White line indicates demarcation of rostral/central and lateral subnuclei. Scale bar: 20 µm B Example image of a presynaptic P face and a postsynaptic E face of a habenular synapse in the rostral IPN that was double labeled with antibodies against AMPA receptors (10 nm gold) and Cav2.3 (5 nm gold). Scale bar: 100 nm. C Example image of a similar synaptic profile double labeled with antibodies against AMPA receptors (10 nm gold) and Cav2.3 (5 nm gold) in the rostral IPN of a Cav2.3 KO mouse. Scale bar: 100 nm. D Left panel: double labeling of a WT carbon-only replica with antibodies against Cav2.3 (5 nm gold) and a mixture of active zone proteins (2 nm gold), including RIM1/2, CAST and neurexin. Right panel: the same image with additional coloring of 2 nm (red) and 5 nm (blue) particles and demarcation of the active zone area based on active zone marker labeling. Scale bars: 100 nm. F Left panel: quantification of Cav2.3 labeling densities in the presynaptic P face in WT and Cav2.3 KO mice. *** indicates P

    Article Snippet: Thereafter, lysates were incubated by rotating for 16 h at 4 °C in the presence of 2.5 μl of 0.3 μg/μl anti-Cav2.3 (CACNA1E) antibody (ACC-006, Alomone Labs, Jerusalem, Israel).

    Techniques: Labeling, Marker, Mouse Assay

    Quantification of the sub-synaptic localization of presynaptic Cav2.3, GBRs and KCTDs along both MHb-IPN pathways Transmission electron microscopy images of 70 nm−thick sections following pre-embedding immunolabeled IPN slices for Cav2.3 ( A ), GABA B1 ( B ), KCTD8 ( C ), KCTD12 ( D ) and KCTD12b ( E ) from synapses in the rostral (left images) and lateral (right image) IPN subnuclei. Scale bars: 200 nm. Graph on the right displays quantification of relative and absolute silver-enhanced gold particle densities in the active zone and at distances of 50 − 200 nm from the edge of the active zone (50 nm bins). F Absolute labeling densities are summarized for synapses in the rostral (left panel) and lateral IPN (right panel). Note absence of KCTD12 and KCTD12b particles in presynaptic terminals inside the lateral IPN subnuclei. KCTD12 was not included in panel F because of predominantly postsynaptic localization inside the rostral IPN. Data was pooled from two animals, showing no significant difference in gold particle distribution patterns with Kolmogorov-Smirnov test (see Supplementary Figure S1).

    Journal: bioRxiv

    Article Title: GABAB receptor auxiliary subunits modulate Cav2.3-mediated release from medial habenula terminals

    doi: 10.1101/2020.04.16.045112

    Figure Lengend Snippet: Quantification of the sub-synaptic localization of presynaptic Cav2.3, GBRs and KCTDs along both MHb-IPN pathways Transmission electron microscopy images of 70 nm−thick sections following pre-embedding immunolabeled IPN slices for Cav2.3 ( A ), GABA B1 ( B ), KCTD8 ( C ), KCTD12 ( D ) and KCTD12b ( E ) from synapses in the rostral (left images) and lateral (right image) IPN subnuclei. Scale bars: 200 nm. Graph on the right displays quantification of relative and absolute silver-enhanced gold particle densities in the active zone and at distances of 50 − 200 nm from the edge of the active zone (50 nm bins). F Absolute labeling densities are summarized for synapses in the rostral (left panel) and lateral IPN (right panel). Note absence of KCTD12 and KCTD12b particles in presynaptic terminals inside the lateral IPN subnuclei. KCTD12 was not included in panel F because of predominantly postsynaptic localization inside the rostral IPN. Data was pooled from two animals, showing no significant difference in gold particle distribution patterns with Kolmogorov-Smirnov test (see Supplementary Figure S1).

    Article Snippet: Thereafter, lysates were incubated by rotating for 16 h at 4 °C in the presence of 2.5 μl of 0.3 μg/μl anti-Cav2.3 (CACNA1E) antibody (ACC-006, Alomone Labs, Jerusalem, Israel).

    Techniques: Transmission Assay, Electron Microscopy, Immunolabeling, Labeling