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Expression of Rem2, an RGK Family Small GTPase, Reduces N-Type Calcium Current without Affecting Channel Surface Density
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| Zeitschriftentitel: | The Journal of Neuroscience |
|---|---|
| Personen und Körperschaften: | , , , , |
| In: | The Journal of Neuroscience, 25, 2005, 42, S. 9762-9772 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Society for Neuroscience
|
| Schlagwörter: |
| author_facet |
Chen, Huanmian Puhl, Henry L. Niu, Shui-Lin Mitchell, Drake C. Ikeda, Stephen R. Chen, Huanmian Puhl, Henry L. Niu, Shui-Lin Mitchell, Drake C. Ikeda, Stephen R. |
|---|---|
| author |
Chen, Huanmian Puhl, Henry L. Niu, Shui-Lin Mitchell, Drake C. Ikeda, Stephen R. |
| spellingShingle |
Chen, Huanmian Puhl, Henry L. Niu, Shui-Lin Mitchell, Drake C. Ikeda, Stephen R. The Journal of Neuroscience Expression of Rem2, an RGK Family Small GTPase, Reduces N-Type Calcium Current without Affecting Channel Surface Density General Neuroscience |
| author_sort |
chen, huanmian |
| spelling |
Chen, Huanmian Puhl, Henry L. Niu, Shui-Lin Mitchell, Drake C. Ikeda, Stephen R. 0270-6474 1529-2401 Society for Neuroscience General Neuroscience http://dx.doi.org/10.1523/jneurosci.3111-05.2005 <jats:p>Rad, Gem/Kir, Rem, and Rem2 are members of the Ras-related RGK (Rad, Gem, and Kir) family of small GTP-binding proteins. Heterologous expression of RGK proteins interferes with<jats:italic>de novo</jats:italic>calcium channel assembly/trafficking and dramatically decreases the amplitude of currents arising from preexisting high-voltage-activated calcium channels. These effects probably result from the direct interaction of RGK proteins with calcium channel β subunits. Among the RGK family, Rem2 is the only member abundantly expressed in neuronal tissues. Here, we examined the ability of Rem2 to modulate endogenous voltage-activated calcium channels in rat sympathetic and dorsal root ganglion neurons. Heterologous expression of Rem2 nearly abolished calcium currents arising from preexisting high-voltage-activated calcium channels without affecting low-voltage-activated calcium channels. Rem2 inhibition of N-type calcium channels required both the Ras homology (core) domain and the polybasic C terminus. Mutation of a putative GTP/Mg<jats:sup>2+</jats:sup>binding motif in Rem2 did not affect suppression of calcium currents. Loading neurons with GDP-β-S via the patch pipette did not reverse Rem2-mediated calcium channel inhibition. Finally, [<jats:sup>125</jats:sup>I]Tyr<jats:sup>22</jats:sup>-ω-conotoxin GVIA cell surface binding in tsA201 cells stably expressing N-type calcium channels was not altered by Rem2 expression at a time when calcium current was totally abolished. Together, our results support a model in which Rem2 localizes to the plasma membrane via a C-terminal polybasic motif and interacts with calcium channel β subunits in the preassembled N-type channel, thereby forming a nonconducting species.</jats:p> Expression of Rem2, an RGK Family Small GTPase, Reduces N-Type Calcium Current without Affecting Channel Surface Density The Journal of Neuroscience |
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10.1523/jneurosci.3111-05.2005 |
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ElectronicArticle |
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Society for Neuroscience, 2005 |
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Society for Neuroscience, 2005 |
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0270-6474 1529-2401 |
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0270-6474 1529-2401 |
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2005 |
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The Journal of Neuroscience |
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49 |
| title |
Expression of Rem2, an RGK Family Small GTPase, Reduces N-Type Calcium Current without Affecting Channel Surface Density |
| title_unstemmed |
Expression of Rem2, an RGK Family Small GTPase, Reduces N-Type Calcium Current without Affecting Channel Surface Density |
| title_full |
Expression of Rem2, an RGK Family Small GTPase, Reduces N-Type Calcium Current without Affecting Channel Surface Density |
| title_fullStr |
Expression of Rem2, an RGK Family Small GTPase, Reduces N-Type Calcium Current without Affecting Channel Surface Density |
| title_full_unstemmed |
Expression of Rem2, an RGK Family Small GTPase, Reduces N-Type Calcium Current without Affecting Channel Surface Density |
| title_short |
Expression of Rem2, an RGK Family Small GTPase, Reduces N-Type Calcium Current without Affecting Channel Surface Density |
| title_sort |
expression of rem2, an rgk family small gtpase, reduces n-type calcium current without affecting channel surface density |
| topic |
General Neuroscience |
| url |
http://dx.doi.org/10.1523/jneurosci.3111-05.2005 |
| publishDate |
2005 |
| physical |
9762-9772 |
| description |
<jats:p>Rad, Gem/Kir, Rem, and Rem2 are members of the Ras-related RGK (Rad, Gem, and Kir) family of small GTP-binding proteins. Heterologous expression of RGK proteins interferes with<jats:italic>de novo</jats:italic>calcium channel assembly/trafficking and dramatically decreases the amplitude of currents arising from preexisting high-voltage-activated calcium channels. These effects probably result from the direct interaction of RGK proteins with calcium channel β subunits. Among the RGK family, Rem2 is the only member abundantly expressed in neuronal tissues. Here, we examined the ability of Rem2 to modulate endogenous voltage-activated calcium channels in rat sympathetic and dorsal root ganglion neurons. Heterologous expression of Rem2 nearly abolished calcium currents arising from preexisting high-voltage-activated calcium channels without affecting low-voltage-activated calcium channels. Rem2 inhibition of N-type calcium channels required both the Ras homology (core) domain and the polybasic C terminus. Mutation of a putative GTP/Mg<jats:sup>2+</jats:sup>binding motif in Rem2 did not affect suppression of calcium currents. Loading neurons with GDP-β-S via the patch pipette did not reverse Rem2-mediated calcium channel inhibition. Finally, [<jats:sup>125</jats:sup>I]Tyr<jats:sup>22</jats:sup>-ω-conotoxin GVIA cell surface binding in tsA201 cells stably expressing N-type calcium channels was not altered by Rem2 expression at a time when calcium current was totally abolished. Together, our results support a model in which Rem2 localizes to the plasma membrane via a C-terminal polybasic motif and interacts with calcium channel β subunits in the preassembled N-type channel, thereby forming a nonconducting species.</jats:p> |
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| author | Chen, Huanmian, Puhl, Henry L., Niu, Shui-Lin, Mitchell, Drake C., Ikeda, Stephen R. |
| author_facet | Chen, Huanmian, Puhl, Henry L., Niu, Shui-Lin, Mitchell, Drake C., Ikeda, Stephen R., Chen, Huanmian, Puhl, Henry L., Niu, Shui-Lin, Mitchell, Drake C., Ikeda, Stephen R. |
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| description | <jats:p>Rad, Gem/Kir, Rem, and Rem2 are members of the Ras-related RGK (Rad, Gem, and Kir) family of small GTP-binding proteins. Heterologous expression of RGK proteins interferes with<jats:italic>de novo</jats:italic>calcium channel assembly/trafficking and dramatically decreases the amplitude of currents arising from preexisting high-voltage-activated calcium channels. These effects probably result from the direct interaction of RGK proteins with calcium channel β subunits. Among the RGK family, Rem2 is the only member abundantly expressed in neuronal tissues. Here, we examined the ability of Rem2 to modulate endogenous voltage-activated calcium channels in rat sympathetic and dorsal root ganglion neurons. Heterologous expression of Rem2 nearly abolished calcium currents arising from preexisting high-voltage-activated calcium channels without affecting low-voltage-activated calcium channels. Rem2 inhibition of N-type calcium channels required both the Ras homology (core) domain and the polybasic C terminus. Mutation of a putative GTP/Mg<jats:sup>2+</jats:sup>binding motif in Rem2 did not affect suppression of calcium currents. Loading neurons with GDP-β-S via the patch pipette did not reverse Rem2-mediated calcium channel inhibition. Finally, [<jats:sup>125</jats:sup>I]Tyr<jats:sup>22</jats:sup>-ω-conotoxin GVIA cell surface binding in tsA201 cells stably expressing N-type calcium channels was not altered by Rem2 expression at a time when calcium current was totally abolished. Together, our results support a model in which Rem2 localizes to the plasma membrane via a C-terminal polybasic motif and interacts with calcium channel β subunits in the preassembled N-type channel, thereby forming a nonconducting species.</jats:p> |
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| imprint | Society for Neuroscience, 2005 |
| imprint_str_mv | Society for Neuroscience, 2005 |
| institution | DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229 |
| issn | 0270-6474, 1529-2401 |
| issn_str_mv | 0270-6474, 1529-2401 |
| language | English |
| last_indexed | 2024-03-01T18:06:23.442Z |
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| physical | 9762-9772 |
| publishDate | 2005 |
| publishDateSort | 2005 |
| publisher | Society for Neuroscience |
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| recordtype | ai |
| series | The Journal of Neuroscience |
| source_id | 49 |
| spelling | Chen, Huanmian Puhl, Henry L. Niu, Shui-Lin Mitchell, Drake C. Ikeda, Stephen R. 0270-6474 1529-2401 Society for Neuroscience General Neuroscience http://dx.doi.org/10.1523/jneurosci.3111-05.2005 <jats:p>Rad, Gem/Kir, Rem, and Rem2 are members of the Ras-related RGK (Rad, Gem, and Kir) family of small GTP-binding proteins. Heterologous expression of RGK proteins interferes with<jats:italic>de novo</jats:italic>calcium channel assembly/trafficking and dramatically decreases the amplitude of currents arising from preexisting high-voltage-activated calcium channels. These effects probably result from the direct interaction of RGK proteins with calcium channel β subunits. Among the RGK family, Rem2 is the only member abundantly expressed in neuronal tissues. Here, we examined the ability of Rem2 to modulate endogenous voltage-activated calcium channels in rat sympathetic and dorsal root ganglion neurons. Heterologous expression of Rem2 nearly abolished calcium currents arising from preexisting high-voltage-activated calcium channels without affecting low-voltage-activated calcium channels. Rem2 inhibition of N-type calcium channels required both the Ras homology (core) domain and the polybasic C terminus. Mutation of a putative GTP/Mg<jats:sup>2+</jats:sup>binding motif in Rem2 did not affect suppression of calcium currents. Loading neurons with GDP-β-S via the patch pipette did not reverse Rem2-mediated calcium channel inhibition. Finally, [<jats:sup>125</jats:sup>I]Tyr<jats:sup>22</jats:sup>-ω-conotoxin GVIA cell surface binding in tsA201 cells stably expressing N-type calcium channels was not altered by Rem2 expression at a time when calcium current was totally abolished. Together, our results support a model in which Rem2 localizes to the plasma membrane via a C-terminal polybasic motif and interacts with calcium channel β subunits in the preassembled N-type channel, thereby forming a nonconducting species.</jats:p> Expression of Rem2, an RGK Family Small GTPase, Reduces N-Type Calcium Current without Affecting Channel Surface Density The Journal of Neuroscience |
| spellingShingle | Chen, Huanmian, Puhl, Henry L., Niu, Shui-Lin, Mitchell, Drake C., Ikeda, Stephen R., The Journal of Neuroscience, Expression of Rem2, an RGK Family Small GTPase, Reduces N-Type Calcium Current without Affecting Channel Surface Density, General Neuroscience |
| title | Expression of Rem2, an RGK Family Small GTPase, Reduces N-Type Calcium Current without Affecting Channel Surface Density |
| title_full | Expression of Rem2, an RGK Family Small GTPase, Reduces N-Type Calcium Current without Affecting Channel Surface Density |
| title_fullStr | Expression of Rem2, an RGK Family Small GTPase, Reduces N-Type Calcium Current without Affecting Channel Surface Density |
| title_full_unstemmed | Expression of Rem2, an RGK Family Small GTPase, Reduces N-Type Calcium Current without Affecting Channel Surface Density |
| title_short | Expression of Rem2, an RGK Family Small GTPase, Reduces N-Type Calcium Current without Affecting Channel Surface Density |
| title_sort | expression of rem2, an rgk family small gtpase, reduces n-type calcium current without affecting channel surface density |
| title_unstemmed | Expression of Rem2, an RGK Family Small GTPase, Reduces N-Type Calcium Current without Affecting Channel Surface Density |
| topic | General Neuroscience |
| url | http://dx.doi.org/10.1523/jneurosci.3111-05.2005 |