<<< < te with G proteins. The N-terminal binding site of CSP, wte with G proteins. The N-terminal binding site of CSP, white with G proteins. The N-terminal binding site of CSPte with G proteins. The N-terminal binding site of CSP, wte with G proteins. The N-terminal binding site of CSP, wte with G proteins. The N-terminal binding site of CSP, white with G proteins. The N-terminal binding site of CSP, whicte with G proteins. The N-terminal binding site of CSP, which includes the J domain, binds G? subunits but not G?? subunits whereas the C termite with G proteins. The N-terminal binding site of CSP, which includes the J domain, binds G? subte with G proteins. The N-terminal binding site of CSP, which includes the J domain, bite with G proteins. The N-terminal binding site of CSP, which includes the J domain, binds G? subunits but not G?? subunits whereas tte with G proteins. The N-terminal binding site of CSP, which includes the J domain, binds G? subunits but not G?? subunits whereas the C terminal binding site of CSP associates with either free G?? subunits or G?? in complex with G?. The interaction of eitheding proteins (G proteins) and N-type calcium channels that results in a tonic G protein inhibition of the channels. In this report we directly demonstrate that two separate regions of CSP associate with G proteins. The N-terminal binding site of CSP, which includes the J domain, binds G? subunits but not G?? subunits whereas the C terminal binding site of CSP associates with either free G?? subunits or G?? in complex with G?. The interaction of either binding site of CSP (CSP1-82 or CSP83-198) with G proteins elicits robust tonic inhibition of N-type calcium channel activity. However, CSP1-82 inhibition and CSP83-198 inhibition of calcium channels occur through distinct mechanisms. Calcium channel inhibition by CSP83-198 (but not CSP1-82) is completely blocked by co-expression of the synaptic protein interaction site (synprint) of the N-type channel, indicating that CSP83-198 inhibition is dependent on a physical interaction with the calcium channel. These results suggest that distinct binding sites of CSP can play a role in modulating G protein function and G protein inhibition of calcium channels." /> ding proteins (G proteins) and N-type calcium channels that rding proteins (G proteins) and N-type calcium channels that ding proteins (G proteins) and N-type calcium channels thatding proteins (G proteins) and N-type calcium channels that results in a tonic G protein inhibition of the channels. In this repoding proteins (G proteins) and N-type calcium channels that results in a tonic G protein inhibition of the channels. In this report we directly demonstrate that two separate regions of CSP associate with G proteins. The N-terminal binding site of CSP, which includes the J domain, binds G? subunits but not G?? subunits whereas the C terminal binding site of CSP associates with either free G?? subunits or G?? in complex with G?. The interaction of either binding site of CSP (CSP1-82 or CSP83-198) with G proteins elicits robust tonic inhibition of N-type calcium channel activity. However, CSP1-82 inhibition and Cits whereas the C terminal binding site of CSP associates with either free G<sub>??</sub> subunits or G<sub>??</sub> in complex with G<sub>?</sub>. The interaction of either binding site of CSP (CSP<sub>1-82</sub> or CSP83-198) with G proteins elicits robust tonic inhibition of N-type calcium channel activity. However, CSP<sub>1-82</sub> inhibition and CSP83-198 inhibition of calcium channels occur through distinct mechanisms. Calcium channel inhibition by CSP83-198 (but not CSP<sub>1-82</sub>) is completely blocked by co-expression of the synaptic protein interaction site (synprint) of the N-type channel, indicating that CSP83-198 inhibition is dependent on a physical interaction with the calcium channel. These results suggest that distinct binding sites of CSP can play a role in modulating G protein function and G protein inhibition of calcium channels.</p>" /> its whereas the C terminal binding site of CSP associates with either freits whereas the C terminal binding site of CSP associates with either free its whereas the C terminal binding site of CSP associates with its whereas the C terminal binding site of CSP associates its whereas the C terminal binding site of CSP assits whereas the C terminal binding site of CSP associates with either free G<sub>??<its whereas the C terminal binding site of CSP associates with either free G<sub>??</sub> subuniits whereas the C terminal binding site of CSP associates with either free G<sub>??</sub>its whereas the C terminal binding site of CSP associates with either free G<sub>??</sub&its whereas the C terminal binding site of CSP assits whereas the C terminal binding site of CSP assits whereas the C terminal binding site of CSP associatesits whereas the C terminal binding site of CSP asits whereas the C terminal binding site of CSPits whereas the C terminal binding site of Cits whereas the C terminal binding site of CSP associa eta name="citation_section" content="Research Artieta name="citation_section" content="Research Arteta name="citation_section" content="Research Article" /> eta name="citation_section" content="Research Article" /> eta name="citation_section" content="Research Article" /> eta name="citation_section" content="Research Article" /> eta name="citation_section" content="Research Article" /> tation_title=Biochem. J.;citation_volume=322;citation_year=1997;citation_pmid=9148760;citation_doi=10.1042/bj3220853" /> nd Mutant alpha -SNAP Overexpression Reveals a Role for Csp in Late Steps of Membrane Fusion in Dense-Core Granule Exocytosis in Adrenal Chromaffin Cells;citation_pages=1281-1289;citation_volume=20;citation_year=2000;citation_issue=4;citation_pmid=10662817" /> ype Calcium Channels Is Facilitated by Physical Interactions between Syntaxin 1A and Gbeta gamma;citation_pages=6388-6394;citation_v_title=Interaction of Cysteine String Proteins with the {alpha}1A Subunit of the P/Q-type Calcium Channel;citation_pages=13488-13492;citation_volume=273;citation_year=1998;citation_issue=22;citation_pmid=9593683;citation_doi=10.1074/jbc.273.22.13488" /> _title=Interaction of Cysteine String Proteins with the {alpha}1A Subunit of the P/Q-type Calcium Channel;citation_pages=13488-13492;citation_volume=273;citation_year=1998;citation_issue=22;citation_pmid=9593683;citation_doi=10.1074/jbc.273.22.13488" /> ame="citation_reference" content="citation_title=The EMBO Journal;citation_journal_abbrev=EMBO Journal;citation_title=Rab-{alpha}GDI activity is regulated by a Hsp90 chaperone complex;citation_pages=6125-6135;citation_volume=21;citation_year=2002;citation_issue=22;citation_pmid=12426384;citation_doi=10.1093/emboj/cdf603" /> >>>> ppppppprprotein modulation of N-type calcium channels | Journal of Cell Science type="text/css" type&&&&&< << << |arj||arj|asf|asx|avi|bin|csv|doc(x|m)?|dot(x|m)?|exe|flv|gif|gz|gzip|hqx|jar|jpe?g|js|mp(2|3|4|e?g)|mov(ie)?|m|arj|asf|a|arj|asf|asx|avi|bin|csv|doc(x|m)?|dot(x|m)?|exe|flv|gif|gz|gzip|hqx|jar|jpe?g|js|mp(2|3|4|e?g)|mov(ie)?|msi|msp|pdf|phps|png|ppt(x|m)?|pot(x|m)?|pps(x|m)?|ppam|sld(x|m)?|thmx|qtm?|ra(m|r)?|sea|sit|tar|tgz|torren|arj|asf|asx|avi|bin|csv|do|arj|asf|asx|avi|bin|arj|asf||arj|asf|asx|av|arj|asf|asx|avi|bin|csv|doc(x|m)?|dot(x|m)?|exe|flv|gif|gz|gzip|hqx|jar|jpe?g|js|mp(2|3|4|e?g)|mov(ie)?|msi|msp||arj|asf|asx|avi|bin|csv|doc(x|m)?|dot(x|m)?|exe|flv|gif|gz|gz|arj|asf|asx|avi|bin|csv|doc(x|m)?|dot(x|m)?|exe|flv|gif|gz|gzip|hqx|jar|jpe?g|js|mp(2|3|4|e?g)|mov(ie)|arj|asf|asx|avi|bin|csv|doc(x|m)?|dot(x|m)?|exe|flv|gif|gz|gzip|hqx|jar|jpe?g|js|mp(2|3|4|e?g)|mov(ie)?|m|arj|asf|asx|avi|bin|csv|doc(x|m)?|dot(x|m)?|exe|flv|gif|gz|gzip|hqx|jar|jpe?g|js||arj|asf|asx|avi|bin|csv|doc(x|m)?|dot(x|m)?|exe|fl|arj|asf|asx|avi|bin|csv|doc(x|m)?|dot(x|m)?|exe|flv|gif|gz|gzip|hqx|jar|jpe?g|js|mp(2|3|4|e?g)|mov(ie)?|msi|msp|pdf|phps|png|ppt(x|m)?|pot(x|m)?|pps(x|m)?|ppam|sld(x|m)?|thmx|qtm?|ra(m||arj|asf|asx|avi|bin|csv|doc(x|m)?|dot(x|m)?|exe|flv|gif|arj|asf|asxcontent clearfix"> content clearfix">
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    sitesitesitesitesitesiteabs" data-entiabs"abs" data-entity-context=abs" databs"? subunits but not G?? subunits whereas the C terminal binding siding protding pding proteins (G proteins)ding proteins (Gding proteins (G proteidingding ding proteins (Gding protedingding ding proteins (Gding protedingding ding proteins (G rel="nofollow">N-type- rel rel= rel="nofollow"> rel="nofollow">N-typ rel rel= rel="nofollow"> rel="no rel rel= rel= rel="nofollow">N-type-calcium channels rel="nofollow"> rel="nofoll rel="nofollow">N-type-calcium channels
  • N-type-calcium channels
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  • Synaptic transmission
  • rel="nofollow">N-t rel="nofollow">N-type-calcium channels
  • Synaptic transmission
  • J domain
  • eviewed by eviewed by eviewed by Zinsmaier and Bronk, 2001) (Chamberlain and eviewed by Zinsmaier and Bronk, 2001) (Chamberlain and Burgoyne, 2000).

    We have recently shown that CSP is capable of binding to both the N-type calcium channel eviewed by Guan and Dixon, 1991) and expressed as GST fusion protinto pGEX-KG (Guan and Dixon, 1991) and expressed as GST fusion proteins in AB1899 cells. His6? 1B calcium channel II-III linker synprint motif fusion protein (amino acids 718-963) was prepared as described previously (Guan and Dixon, 1991) and expressed as GST fusion proteins in AB1899 cells. His6? 1B calcium channel II-III linker synprint motif fusion protein (nceau S. Nitrocellulose membranes were blocked for non-specific binding using 5% milk, 0.1% Tween 20, PBS solution [137 mM NaCl, 2.7 mM KCl, 4.3 mM Nanceau nceau S. nceau nceau S. Nitrocelnceau nceau S.nceau nceau S. Nitrocellulose membranes were blocked for non-specific binding using 5% milk, 0.1% Tween 20, PBS solution [137 mM NaCl, 2.7 mM KCl, 4.3 mM Na2HPO4, 1.4 mM KH2PO4 (pH 7.3)] and incubated overnight at 4C or 2 hours at room temperature with primary antibody. The membranes were washed three to four times in the above milk/Tween/PBS solution and incubated for 30 minutes with goat anti-rabbit or goat anti-mouse IgG-coupled horseradnceau S. Ninceau S. Nitrnceau S. Nitrocellulose membranes were blocknceau S. Nitrocellulose membranes were nceau S. Nitronceau S. Nitrocellulose membranes were blocked for non-specific bindinnceau Snceau S. Nitrocellulose membranes were blocked for non-specific binding using 5% milk, 0.1% Tween 20, PBS solution [137 mM NaCl, 2.7 mM KCl, 4.3 mM Na2nceau S. Nitrocellnceau S. Nitrocellulose membranes were blocked for non-specificnceau S. nceau S. Ninceau S. Nnceau S. Nitronceau S. Ninceau S. Nitrocellulose membranes were blocked for non-specific binding nceau nceau S. Nitrocellulose membranes were blocked for non-specific binding using 5% milk, 0.1% Tween 20, PBS solution [137 mM NaCl, 2.7 mM KCl, 4.3 mM Na2HPO4, 1.4 mM KH2PO4 (pH 7.3)] and incubated overnight at 4C or 2 hours at room temperature with primary antibody. The membranes were washed three to four times in the above milk/Tween/PBS solution and incubated for 30 minutes with goat anti-rabbit or goat anti-mouse IgG-cnceau Snceau S. Nitrocellulose membranes were blocked for non-specific binding using 5%2+sup>2+ channel subunsup>2+2+2+sup>2+sup>2+2+ channel subunsup>2+2+ chansup>2+sup>2+ channsup>2+sup>2+2+2+ channel subunits (?1B +? 2-? + ?1b; accession nsup>2+2+ sup>2+2+ channel subunits (?1B +? 2-? + ?1b; accession numbersup>2+2+ sup>2+ channel subunits (?1B2+ channel subunsup>2+ csup>2+ channel subunits (?1B +? 2-? + ?1b; accession numbers? 1B: M92905, ?2-?: NM000722,2+sup>2+ chansup>2+sup>2+ channel subunits (?1B +? 2-? + ?1b; accession numbers? 1B: M92905, ?2-?: NM000722, ?1b: AB054985) and, as appropriate green fluorescent protein (EGFP; Clontech, CA) CSP, CSP1-82 or CSP83-198. After 12 hours, the cells were washed with fresh DMEM and allowed to recover for 12 hours.

    Patch clamp recordings

    Immediately prior to recording, individuasup>2+sup>2+ channel subunits (?1B +? 2-? + ?1b; accession numbers? 1B: M92905, ?2-?: NM000722, ?1b: AB054985) and, as appropriate green fluorescent protein (EGFP; Clontech, CA) CSP, CSP1-82 or CSP83-198. After 12 hours, the cells were washed with fresh DMEM and allowed to recover for 12 hours.

    Patch clamp recordings

    Immediately prior to recording, individual coverslips were transferred to a 3 cm culture dish containing recording solution comprised of 20 mMsup>2+2+ channel subunits (?1B +? 2-? + ?1b; accession numbers? 1B: M92905, ?2using using Sigmaplot vusing using Sigmaplot v 4.0. Unless stated otherwise, all using Siusing Sigmaplot v 4.0. Unless stated otherwise, all error bars are standard errors, and numbers in parentheses displayed in thusing Sigmaplot v using Siusing using Sigmaplot v 4.0. Unless stated otherwise, all error bars are standard errors, and numbers in parentheses dispusing using Sigmaplot v 4.0. Unless stated otherwise, using using Sigmaplot v 4.0. Unless stated otherwise, all error bars are standard erusing using Sigmaplot v 4.0. Unlesusing using Sigmaplot v 4.0. Unlusing Siusing Sigmaplot v 4.0. Unless stated otherwise, all error bars are standard errors, and numbers in parentheses displayed in the figures reflect numberusing using Sigmaplot v 4.0.ed Ged G??? preparation with the J domain suggests that an additional component present in the homogenate fraction is required for thed G??? ed G?????? preparation wied Ged G??? preparation with theed G??? preparatioed G??? preparation with ed G??? preparatied G??? preparation w  Fig. 1.  H5BAEAAAAA  Fig. 1.  H5BAEAAAAALH5BAEAAH5BAH5BAEAH5BAEAH5BAEAAAAALAAAAAABAAEAAAIBRAA7" data-src=H5BAEAAAAALAAAAAABAAEAAAIBRAA7"H5BAEAAAAALAAAAH5BAH5BAEH5BAEAAAAALAAAAAABAAH5BAEAAAAALAAAAH5BAH5BAEH5BAEAAAAALAAAAAABAAEAAAIBRAA7H5BAEAAAAALAAAAAABAH5BAH5BAEH5BAEH5BAEAH5BAEAAAAALAAAAAABAAEAAAIBRAA7" data-src="http://jcs.biologists.org/H5BAEAAAAALAAAAAABAAEAAAIBRAA7" data-srH5BAEAAAAALAAAAH5BAEAAAAALAAAAAABAAEAH5BAEAAAAALAAAAAABAAEAAH5BAEAAAAALAAAAAABAAEAAAIBRAA7" data-src="http://jcs.H5BAEAH5BAEAAAAALAAAAAABAAEAAAIBRAA7" data-src="http://jcs.biologH5BAEAH5BAEAAAAALAAAAAABAAEAAAIBRAA7" data-src="http://jcs.biologists.org/content/joces/116/14/2967/F1.medium.gif"/>

    trunca truncation mutants 83 trunc trunc trunc truncation mutants 83-198 and 137-198 migrate anomalously on SDS trunc truncation mutants 83-198 and 137-198 migrate anomalously on SDS-PAGE. These results are repr trunc truncation mutants 83-198 and 137-198 migrate anomalously o trunc trunc trunc truncation mutants 83-198 and 137-198 migrate anomalously on SDS-PAGE. These resul trunc truncation mutants 83-198 and trunc truncation mutants 83-198 and 137-198 migrate anomal trunc truncation trunc truncation mutants 83-198 and 137-198 migrate anomalously on SDS-PAGE. These results are representative of four independent experiments.

    The ability of the trunc truncation mutants 83-19 trunca truncation mutants 83-198 and 137-198 migrate anomalously on SDS-PAGE. These results are trunca truncation mutants trunca truncation mutants 83-1 trunc trunca truncation m truncation mutants 83-198 and 137-198 migrate anomalously on SDS-PAGE. These results trunca truncatio trunc truncation mutants 83-198 and 137-198 migrate anomalously on SDS-PAGE. Thes trunc truncation mutants 83-198 and 137-198 migrate anomalously on SDS-PAGE. Theseed on glutathione agarose beads and then incubated with soluble Hised on ed on glutathione agarose beads and then incubated with soluble His6 synprint followed by several washes to remove unbound protein. The proteins were then denatured and fractionated by SDS-PAGE, and bound synprint was detected by western blotting. Full-length CSP, CSP83-198, CSP1-190, CSP1-180, CSed on ed on glutathione agarose beads and then incubated with soluble His6 synprint followed by several washes to remove unbound protein. The proteins were then denatured and fractionated by SDS-PAGE, and bound synpred on glued on glutathione agarose beads and then incubated with soluble His6 synprint followed by several washes to remove unbound protein. The proteins were then denatured and fractionated by SDS-PAGE, and bound synprint was detected by western ed on ed on glutated on ed on glutathione agarose beads and then incubated with soluble His6 synprint followed by several washes to remove unbound protein. The proteins were then denatured and fractionated by SDS-PAGE, and bound synprint was detected by western blotting. Full-led on ed on glutated on ed on glutathioned on glutathed on glutathione agarose beads aed oed on glutathione agarose beads and theed on glutathione agarose beaed on glutathione agarose beads and ed on glutathione agarose beexperiments." class="highwire-fr  Fig. 5.  experiment  Fig. 5.  experimentsexperimexpeexperiexperiexperiments." class="highwire-fragment frexperiments." class="highwire-fexperiments." cexpeexperexperiments." class=experiments." cexpeexperexperiments." class="highwire-experiments." classexpeexperexperexperiexperclass="fig-caption">class="fig-caption"> Fig. 5.

    Identification of the CSP regions that associate with N-typclass="class="fig-caption"class=class="fig-caption"> Fig. 5.

    Identification of the CSP regions that associate with N-type calcium channels. CSP deletion mutants were immobilized on glutathione-agarose beads and incubated with recombinant ?1B synprint Hisclass="fig-captioclass="fig-caption"> class="fig-caption"> Fig. 5. Fig. 5. Fig. 5.

    Identification of the CSP regions that associaclass="fig-captionclass="fig-caption"> Fig. 5. class="class="fig-caption"> Fig. 5.

    Identification of the CSP regions that associate with N-type calcium channels. CSP deletion mutants were immobilized on glutathione-agarose beads and incubated with recombinant ?1B synpclass=class="fig-captioncclass="ficclass="fig-caption"> Fig. 5. of full-length CSP to promote G protein inhibition of N-type calcium channels. As shown in of fulof full-length CSP to promote G protein inhibition of N-type calcium channels. As shown in Fig. 6, this is indeed the case. Whereas N-type channels undergo little prepulse facilitation in the absence of coexpressed CSP, coexpression of the cysteine string (CSP83-198of fulof full-length CSP to promote G protein inhibition of N-type calcium channels. As shown in Fig. 6, thiof full-length CSPof fulof full-lengtof full-length CSP to promote G pof fof full-length CSP to promote G proteinof full-length CSP to promoteof full-length CSP to promote G protof full-length CSP to promottor kinase (βARK) reduces   Fig. 6.  tor kinase  Fig. 6.  " alt=" Fi" alt="" al" alt=" alt=" alt=" Fig. 6. " src="http://jcs.biolo" alt=" Fig. 6. " src="http:/" alt=" Fig. 6" al" alt" alt=" Fig. 6. " " alt=" Fig. 6" al" alt" alt=" Fig. 6. " src="http:" alt=" Fig. 6. "" al" alt" alt" alt=" alt=" Fig. 6. " src="" alt=" Fig. 6. " src="http://jcs.bio" alt=" Fig. 6" alt=" Fig. 6. " sr" alt=" Fig. 6. " src" alt=" Fig. 6. " src="http://jcs.biologists.org/content/joces/116/14/2967/F6.medium.gif"/>

      kinas kinase (?ARK) reduces the CSP-mediated current inhibition as shown by the reduced PP relief. The numbers in parentheses reflect the number of experiments; the asterisks indicate s kinase (?ARK kinase (?ARK) reduces the CSP-mediated current inhibition as shown by the reduced PP relief. The num kinase kinase (?ARK) reduces the CSP-mediated current inhibition as shown by the reduced PP relief. The numbers in parentheses reflect the number of experiments; the asterisks indicate statistical significance relative to control conditions at kinas kinase (?ARK) reduces the CSP-mediated current inhibition as shown by the reduced PP relief. The numbers in parentheses reflect the number of experiments; the asterisks indicate statisticalregion did not interfere with the J-domain-mediated effect (regionregion did not interfere with the J-domain-mediated effect (Fig. 7), indicating that the J-domain-mediated effect occurs independently of the N-type channel domain II-III linker. Hence, separate portions of the CSP molecule can independently promote G protein region did noregion did not interfere with theregiregion did not interfere with the J-domregion did not interfere withregion did not interfere with the J-region did not interfere witcorresponding to the synprint re  Fig. 7.  correspond  Fig. 7.  correspondicorrespcorrcorrescorrescorresponding to the synprint region of tcorresponding to the synprint rcorresponding tcorrcorrecorresponding to thecorresponding tcorrcorrecorresponding to the synprint corresponding to thcorrcorrecorrecorrescorresponding to the synpcorresponding to the synprint region ofcorresponding tcorresponding to the scorresponding to

      Effect of synprint peptides on CSP action. (A) Current records obtained with transiently expressed N-type calcium channels following co-expression of either the cysteine string domain (left traces) or the J domain (right traces) and a cDNA construct corresponding to the synprint region of the rat N-type calcium channel. Note that synprint blocks the effect of the cysteine string region but not that mediated by the J domain. The experimental conditions were as outlin

      Effect of synprint peptides on CSP action. (A) Current records obtained with transiently expressed N-type calcium channels following co-expression of either the cysteine string domain (left traces) or the J domain (right traces) and a cDNA construct corresponding to the synprint region of the rat N-type calcium channel. Note that synprint blocks the

      E

      Effect of synprint peptides on CSP action. (A) Current records obtained with transiently expressed N-type calcium channels following co-expression of either the cysteine string domain (left traces) or the J domain (right traces) and a cDNA cons

      Effect of synprint peptides on CSP action. (A) Cur <

      Effect of synprint peptides on CSP action. (A) Current records obtained with transiently expressed N-t <

      Effect of synprint peptides on CSP action. (A) Current records obtained with transiently expressed N-type calcium channels following co-exprns to be established. We propose that the C-terminus of CSP (CSP83-198), by physically binding to the II-III linker region of the N-type calcium channel subunit and to the Gns to bns to be established. We propose that tns to bns to be established. We propose that the C-terminus of CSP (CSP83-198), by physically binding to the II-III linker ns to be establishns to be established. We propose that the C-terminuns to be establishens to ns to be established. We ns to ns to be established. We ns to be established. We propose that the C-terminus of CSP (CSP83-198), by physically binding to the IIns to be establishns to ns to be esns to be established. We propose that the C-terminuns to be ns to be established. We propose that the C-terminus of CSP (CSP83-198), by physically bindns to ns to be establins to ns to be established. We propose that the C-terminus of CSP (CSP83-198), by physically binding to thenns to nns to nns to nns to bns to be establishns to be establisns to ns to be established. We propose that the C-terminus of CSP (CSP83-198), by physically binding to the II-III linker region of the N-type calcium channel subunit and to the G?? protein dimer, may help target G?? to its site of action on the N-type calcium ns to ns to be established. We propose that the C-terminus of CSP (CSP83-198), by physically binding to thens to bens to be established. We propose that the C-terminumay prevent the assembly of the trimer. In each case, this would result in free Gmay premay prevent the assembly of the trimer. In each case, this would result in free G?? subunits that would then be available to produce a tonic inhibition of the channel. To discriminate between the alternatives, we perfused J domain peptides into tsa-201 cells expressing N-type channels, but did not observe the development of G protein inhibition over a 10 minute time course (data not shown), indicating that the J domain cannot acutely trigger the activation of the G pmay prmay preventmay premay prevent the assembly of the trimer. In each case, this would result in free G?? subunits that would then be available to produce a tonic inhibition of the channmay prmay prevent the assembly ofmay prmay prevent the assembly of the trimer. In each case, this would result in free Gmay preventmay prevent the assembly of the trimer. In each case, this would result in free G?? subunits that would then be available to may prevent the asmay prevent the assembly of the trimer. In each case, this would result in free G?? subunits that would then be available to produce a tonic inhibition of the channel. To discriminate between the alternatives, we perfused J domain peptides into tsa-201 cells expressing N-type channels, but did not observe the development of G protein inhibition over a 10 minute time course (data not shown), indicating that the J domain cannot amay prevent the asmay prevent the assembly of the trimer. In each case, this would result in free G?? subunits that may prmay premay preventmay prevent the assembly of the trimer. In each case, this would result in free G?? subunits that would then be available to produce a tonic inhibition of the channel. To discriminate between the alternatives, we perfused J domaictivity of members of the heat-shock family Hsp70 (ctivity of membersctivitctivity of membersctivitctivity of members of the heatctivitctivity of membersctivity of members of the heat-shock family Hsp70 (Braun et al., 1996; ctivity of members of the ctivitctivity of members of the ctivity of members of the heat-shock family Hsp70 (Braun et al., 1996; Bronk et al., 2001; goyne, 2000).goyne, 2000). In contrast, the synprint sites of P/Q calcium channels (goyne, 2000)goyne,goyne, 2000). goyne,goyne, 2000goyne, 2000). In contrast, the synprigoyne, 2000). Ingoyne, 2000). In congoyne, 2000). In cgoyne, 2000goyne, 2000). In goyne, 2000)goyne, 2000). goyne, 2000). In contrast, the synprint sites of P/Q calcium channels (

      In conclusion, our results reveal that two separate motifs of CSP bind to G proteins and regulate G protein inhibition of N-type calcium channels. The multitude of G-protein-triggered cascades and the distinct mechanisms of action by CSP N- and C-terminal domains may, in part, explain the paradoxical findings regarding CSP's role in exocytosis. Chaperone-assisted protein folding of signalionformation of these possibonformation of these possible target proteins and the nature of the conflicting results regarding the role of CSP in exocytosis.

      In conclusion, our results onformationformonformation of these possible targetonformation of thesonformation onformation of these possible target proteins and the nature of the conflicting results regarding the role of CSP in exocytosis.

      In conclusion, our results reveal that two separate motifs of CSP bind to G proteins and regulate G protein inhibition of N-type calcium channels. The multitude of G-protein-triggered cascades and the distinct mechanisms of action by CSP N- and C-terminal domains may, in part, explain the paradoxical findings regarding CSP's role in exocytosis. Chaperone-assisted protein folding of signaling components has beenonformationformonformation of these possible target proteins onformation oonforonfoonformation of these possible target proteins and the nature ofonformation ooonfoonformation of these posonformation of these possible target proteins and the onformationonforonforonformonformation of these possonformation of these possible target proteins and the nature of the conflicting results regonformation of these possible tcepted cepted April 3cepteceptecepted April 3, 2003.April 3, 2003.

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    • 1998te">1998). Cysteine string protein functions directly in regulated exocte">1998). Cysteine string proteinte">1998te">1998). Cystete">1998te">1998). Cysteine ste">1998199te">19te">1998). Cystete">1998199te">te">1998199te">te">19te">19981te">te">1998). Cysteine string proteite">199tte">19981998). Cysteine string protein functions directly in regulated exocytosis. 1998). Cysteinete">19te">1998). Cysteine string protein functe">19981998). Cysteine strite">1998). Cysteine string protein functions directly in rte">1998). Cysteine string protte">1998te">1998). Cysteite">1998te">1998). Cysteine ste">1998199te">19te">1998). CysteDZ39.88-2004%DZ39.88DZ39DZ39.88-2004%2DZ39.88DZ39DZ39.88-2004DZ39.88DZ39DZ39.88-2004%26url_vDZ39.88DZ39DZ39.8DZ39.88-2004%DZ39.DZ39DZ39.88-2004%26url_ver%253DZ39.88-2004%2DZ39.88DDZ39.88-2004%DZ39.88-2004%26url_ver%253DZ39.88-2004%26url_ctx_fmt%253Dinfo%253Aofi%252Ffmt%253Akev%253Amtx%253ADZ39.88-2004%26url_ver%253DZ39.8DZ39.88-2004%26url_ver%253DZ39.88-2004%26url_ctx_fmt%253Dinfo%253Aofi%252Ffmt%253Akev%DZ39.88-200DZ39.88-2004%26url_ver%253DZ39.DZ39.88-2004%26url_ver%253DZ39.88-2004%26url_ctx_fmt%253Dinfo%253Aofi%252Ffmt%253DZ39.88-2004%26url_ver%253DZ39.88-20DZ39.88-DZ39.88-2004%26url_ver%25DZ39.88-DZ39.88-2004%26url_ver%253DDZ39.88-2004%DZ39.88DZ39.8DZ39.88-2004%26url_ver%DZ39.88-2004%DZ39.88DZ39">CrossR">">Cros">">CrossRefCross">CrossRef"">Cross">CrossRefCrossRefCrossRefCro">CrossRefCrossRef<">CrossRefCrossRef<">">CrossRef">Cross">CrossRef">Cross">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). Phosphorylation of cysteine string protein by protein kinase A. Implications for the modulation of exocytosis. ). Phosphorylation of cysteine string p). Phosp). Phosphorylation of cys). Phosp). Phosphorylation of cystein). Phosphorylat). Phos). Pho). Phosphorylation of c). Phosphoryl). Phos). P). Pho). Phosphorylation of cysteine string protei). Phos). Phosphorylation of cysteine string protein by prot). Phos). Phosphorylation of cysteine string). Phosphorylation of cysteine str). Phosphorylati). Phos). Phos). P). Pho). Phosphoryl). Ph). P). Phosphorylation of cysteine string pr). Phos)). Phosphoryl). Phosphorylation of cysteine string protein by protein kinase A. Implications for the m). Phosphorylation of cyst). Pho). Phosphorylation of cysteine string ). Phosphor). Phosphorylation of cysteine ). Phosphorylation of cysteine string protein by protein kinase A. 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