CK2 accumulation at the axon initial segment depends on sodium channel Nav1
•Phosphorylation of Nav1 ankyrin-binding motif occurs in vivo.•Nav1 expression is necessary for CK2 localization at the AIS.•CK2-Nav1 molecular complex modulates CK2-clustering at the AIS. Accumulation of voltage-gated sodium channel Nav1 at the axon initial segment (AIS), results from a direct inte...
Gespeichert in:
| Veröffentlicht in: | FEBS letters 2014-09, Vol.588 (18), p.3403-3408 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 3408 |
|---|---|
| container_issue | 18 |
| container_start_page | 3403 |
| container_title | FEBS letters |
| container_volume | 588 |
| creator | Hien, Y.E. Montersino, A. Castets, F. Leterrier, C. Filhol, O. Vacher, H. Dargent, B. |
| description | •Phosphorylation of Nav1 ankyrin-binding motif occurs in vivo.•Nav1 expression is necessary for CK2 localization at the AIS.•CK2-Nav1 molecular complex modulates CK2-clustering at the AIS.
Accumulation of voltage-gated sodium channel Nav1 at the axon initial segment (AIS), results from a direct interaction with ankyrin G. This interaction is regulated in vitro by the protein kinase CK2, which is also highly enriched at the AIS. Here, using phosphospecific antibodies and inhibition/depletion approaches, we showed that Nav1 channels are phosphorylated in vivo in their ankyrin-binding motif. Moreover, we observed that CK2 accumulation at the AIS depends on expression of Nav1 channels, with which CK2 forms tight complexes. Thus, the CK2–Nav1 interaction is likely to initiate an important regulatory mechanism to finely control Nav1 phosphorylation and, consequently, neuronal excitability. |
| doi_str_mv | 10.1016/j.febslet.2014.07.032 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_hal_p</sourceid><recordid>TN_cdi_hal_primary_oai_HAL_hal_01701430v1</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S001457931400581X</els_id><sourcerecordid>1694975892</sourcerecordid><originalsourceid>FETCH-LOGICAL-c614X-235098f35c6f190f08abcd1be97e84c2bc343bf8f9302d0d139430dc740c3b143</originalsourceid><addsrcrecordid>eNqNkU1v1DAQhi0EokvhJ4ByhEPCTOzE8QmVVcuiruAASL1Zjj1hvcrHEicL_fc42qXXcvLHPPN6rIex1wgZApbv91lDdWhpynJAkYHMgOdP2AoryVMuyuopW0GspIVU_IK9CGEP8Vyhes4u8gJBSVmu2O36Nk-MtXM3t2byQ5-YKZl2lJg_ce97P3nTJoF-dtRPiaMD9S4ksRQG5-cusTvT99QmX8wRX7JnjWkDvTqvl-zHzfX39Sbdfv30eX21TW2J4i7NeQGqanhhywYVNFCZ2jqsSUmqhM1rywWvm6pRHHIHDrkSHJyVAiyvUfBL9u6UuzOtPoy-M-O9HozXm6utXu4AZfw5hyNG9u2JPYzDr5nCpDsfLLWt6WmYg8ZSCSWLSuWPo0WJqpSoeESLE2rHIYSRmocxEPSiR-_1WY9e9GiQOuqJfW_OT8x1R-6h65-PCGxOwG_f0v3_peqb64_5t8X1ohoFQFHhXYz6cIqiqOLoadTBeuotOT-SnbQb_CPT_gUt-bZM</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1561967193</pqid></control><display><type>article</type><title>CK2 accumulation at the axon initial segment depends on sodium channel Nav1</title><source>MEDLINE</source><source>Wiley Online Library Journals Frontfile Complete</source><source>Wiley Free Content</source><source>ScienceDirect Journals (5 years ago - present)</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>Hien, Y.E. ; Montersino, A. ; Castets, F. ; Leterrier, C. ; Filhol, O. ; Vacher, H. ; Dargent, B.</creator><creatorcontrib>Hien, Y.E. ; Montersino, A. ; Castets, F. ; Leterrier, C. ; Filhol, O. ; Vacher, H. ; Dargent, B.</creatorcontrib><description>•Phosphorylation of Nav1 ankyrin-binding motif occurs in vivo.•Nav1 expression is necessary for CK2 localization at the AIS.•CK2-Nav1 molecular complex modulates CK2-clustering at the AIS.
Accumulation of voltage-gated sodium channel Nav1 at the axon initial segment (AIS), results from a direct interaction with ankyrin G. This interaction is regulated in vitro by the protein kinase CK2, which is also highly enriched at the AIS. Here, using phosphospecific antibodies and inhibition/depletion approaches, we showed that Nav1 channels are phosphorylated in vivo in their ankyrin-binding motif. Moreover, we observed that CK2 accumulation at the AIS depends on expression of Nav1 channels, with which CK2 forms tight complexes. Thus, the CK2–Nav1 interaction is likely to initiate an important regulatory mechanism to finely control Nav1 phosphorylation and, consequently, neuronal excitability.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/j.febslet.2014.07.032</identifier><identifier>PMID: 25109776</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Amino Acid Motifs ; Animals ; Axon initial segment ; Axons - enzymology ; Casein Kinase II - metabolism ; Cells, Cultured ; Dominant negative ; Gene Expression ; Hippocampus - cytology ; Life Sciences ; Nav1 ; NAV1.2 Voltage-Gated Sodium Channel - genetics ; NAV1.2 Voltage-Gated Sodium Channel - metabolism ; Neurobiology ; Neurons and Cognition ; Phosphorylation ; Phosphospecific antibody ; Protein kinase CK2 ; Protein Processing, Post-Translational ; Protein Transport ; Rats ; Rats, Wistar</subject><ispartof>FEBS letters, 2014-09, Vol.588 (18), p.3403-3408</ispartof><rights>2014 Federation of European Biochemical Societies</rights><rights>FEBS Letters 588 (2014) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><rights>Copyright © 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c614X-235098f35c6f190f08abcd1be97e84c2bc343bf8f9302d0d139430dc740c3b143</citedby><cites>FETCH-LOGICAL-c614X-235098f35c6f190f08abcd1be97e84c2bc343bf8f9302d0d139430dc740c3b143</cites><orcidid>0000-0002-2957-2032 ; 0000-0003-1964-7958 ; 0000-0001-7853-7156</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2Fj.febslet.2014.07.032$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.febslet.2014.07.032$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,780,784,885,1417,1433,3549,27923,27924,45573,45574,45994,46408,46832</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25109776$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-01701430$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Hien, Y.E.</creatorcontrib><creatorcontrib>Montersino, A.</creatorcontrib><creatorcontrib>Castets, F.</creatorcontrib><creatorcontrib>Leterrier, C.</creatorcontrib><creatorcontrib>Filhol, O.</creatorcontrib><creatorcontrib>Vacher, H.</creatorcontrib><creatorcontrib>Dargent, B.</creatorcontrib><title>CK2 accumulation at the axon initial segment depends on sodium channel Nav1</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>•Phosphorylation of Nav1 ankyrin-binding motif occurs in vivo.•Nav1 expression is necessary for CK2 localization at the AIS.•CK2-Nav1 molecular complex modulates CK2-clustering at the AIS.
Accumulation of voltage-gated sodium channel Nav1 at the axon initial segment (AIS), results from a direct interaction with ankyrin G. This interaction is regulated in vitro by the protein kinase CK2, which is also highly enriched at the AIS. Here, using phosphospecific antibodies and inhibition/depletion approaches, we showed that Nav1 channels are phosphorylated in vivo in their ankyrin-binding motif. Moreover, we observed that CK2 accumulation at the AIS depends on expression of Nav1 channels, with which CK2 forms tight complexes. Thus, the CK2–Nav1 interaction is likely to initiate an important regulatory mechanism to finely control Nav1 phosphorylation and, consequently, neuronal excitability.</description><subject>Amino Acid Motifs</subject><subject>Animals</subject><subject>Axon initial segment</subject><subject>Axons - enzymology</subject><subject>Casein Kinase II - metabolism</subject><subject>Cells, Cultured</subject><subject>Dominant negative</subject><subject>Gene Expression</subject><subject>Hippocampus - cytology</subject><subject>Life Sciences</subject><subject>Nav1</subject><subject>NAV1.2 Voltage-Gated Sodium Channel - genetics</subject><subject>NAV1.2 Voltage-Gated Sodium Channel - metabolism</subject><subject>Neurobiology</subject><subject>Neurons and Cognition</subject><subject>Phosphorylation</subject><subject>Phosphospecific antibody</subject><subject>Protein kinase CK2</subject><subject>Protein Processing, Post-Translational</subject><subject>Protein Transport</subject><subject>Rats</subject><subject>Rats, Wistar</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU1v1DAQhi0EokvhJ4ByhEPCTOzE8QmVVcuiruAASL1Zjj1hvcrHEicL_fc42qXXcvLHPPN6rIex1wgZApbv91lDdWhpynJAkYHMgOdP2AoryVMuyuopW0GspIVU_IK9CGEP8Vyhes4u8gJBSVmu2O36Nk-MtXM3t2byQ5-YKZl2lJg_ce97P3nTJoF-dtRPiaMD9S4ksRQG5-cusTvT99QmX8wRX7JnjWkDvTqvl-zHzfX39Sbdfv30eX21TW2J4i7NeQGqanhhywYVNFCZ2jqsSUmqhM1rywWvm6pRHHIHDrkSHJyVAiyvUfBL9u6UuzOtPoy-M-O9HozXm6utXu4AZfw5hyNG9u2JPYzDr5nCpDsfLLWt6WmYg8ZSCSWLSuWPo0WJqpSoeESLE2rHIYSRmocxEPSiR-_1WY9e9GiQOuqJfW_OT8x1R-6h65-PCGxOwG_f0v3_peqb64_5t8X1ohoFQFHhXYz6cIqiqOLoadTBeuotOT-SnbQb_CPT_gUt-bZM</recordid><startdate>20140917</startdate><enddate>20140917</enddate><creator>Hien, Y.E.</creator><creator>Montersino, A.</creator><creator>Castets, F.</creator><creator>Leterrier, C.</creator><creator>Filhol, O.</creator><creator>Vacher, H.</creator><creator>Dargent, B.</creator><general>Elsevier B.V</general><general>Wiley</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7TK</scope><scope>1XC</scope><scope>VOOES</scope><orcidid>https://orcid.org/0000-0002-2957-2032</orcidid><orcidid>https://orcid.org/0000-0003-1964-7958</orcidid><orcidid>https://orcid.org/0000-0001-7853-7156</orcidid></search><sort><creationdate>20140917</creationdate><title>CK2 accumulation at the axon initial segment depends on sodium channel Nav1</title><author>Hien, Y.E. ; Montersino, A. ; Castets, F. ; Leterrier, C. ; Filhol, O. ; Vacher, H. ; Dargent, B.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c614X-235098f35c6f190f08abcd1be97e84c2bc343bf8f9302d0d139430dc740c3b143</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Amino Acid Motifs</topic><topic>Animals</topic><topic>Axon initial segment</topic><topic>Axons - enzymology</topic><topic>Casein Kinase II - metabolism</topic><topic>Cells, Cultured</topic><topic>Dominant negative</topic><topic>Gene Expression</topic><topic>Hippocampus - cytology</topic><topic>Life Sciences</topic><topic>Nav1</topic><topic>NAV1.2 Voltage-Gated Sodium Channel - genetics</topic><topic>NAV1.2 Voltage-Gated Sodium Channel - metabolism</topic><topic>Neurobiology</topic><topic>Neurons and Cognition</topic><topic>Phosphorylation</topic><topic>Phosphospecific antibody</topic><topic>Protein kinase CK2</topic><topic>Protein Processing, Post-Translational</topic><topic>Protein Transport</topic><topic>Rats</topic><topic>Rats, Wistar</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hien, Y.E.</creatorcontrib><creatorcontrib>Montersino, A.</creatorcontrib><creatorcontrib>Castets, F.</creatorcontrib><creatorcontrib>Leterrier, C.</creatorcontrib><creatorcontrib>Filhol, O.</creatorcontrib><creatorcontrib>Vacher, H.</creatorcontrib><creatorcontrib>Dargent, B.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Neurosciences Abstracts</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>Hyper Article en Ligne (HAL) (Open Access)</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hien, Y.E.</au><au>Montersino, A.</au><au>Castets, F.</au><au>Leterrier, C.</au><au>Filhol, O.</au><au>Vacher, H.</au><au>Dargent, B.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>CK2 accumulation at the axon initial segment depends on sodium channel Nav1</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2014-09-17</date><risdate>2014</risdate><volume>588</volume><issue>18</issue><spage>3403</spage><epage>3408</epage><pages>3403-3408</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>•Phosphorylation of Nav1 ankyrin-binding motif occurs in vivo.•Nav1 expression is necessary for CK2 localization at the AIS.•CK2-Nav1 molecular complex modulates CK2-clustering at the AIS.
Accumulation of voltage-gated sodium channel Nav1 at the axon initial segment (AIS), results from a direct interaction with ankyrin G. This interaction is regulated in vitro by the protein kinase CK2, which is also highly enriched at the AIS. Here, using phosphospecific antibodies and inhibition/depletion approaches, we showed that Nav1 channels are phosphorylated in vivo in their ankyrin-binding motif. Moreover, we observed that CK2 accumulation at the AIS depends on expression of Nav1 channels, with which CK2 forms tight complexes. Thus, the CK2–Nav1 interaction is likely to initiate an important regulatory mechanism to finely control Nav1 phosphorylation and, consequently, neuronal excitability.</abstract><cop>England</cop><pub>Elsevier B.V</pub><pmid>25109776</pmid><doi>10.1016/j.febslet.2014.07.032</doi><tpages>6</tpages><orcidid>https://orcid.org/0000-0002-2957-2032</orcidid><orcidid>https://orcid.org/0000-0003-1964-7958</orcidid><orcidid>https://orcid.org/0000-0001-7853-7156</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0014-5793 |
| ispartof | FEBS letters, 2014-09, Vol.588 (18), p.3403-3408 |
| issn | 0014-5793 1873-3468 |
| language | eng |
| recordid | cdi_hal_primary_oai_HAL_hal_01701430v1 |
| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Wiley Free Content; ScienceDirect Journals (5 years ago - present); EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Amino Acid Motifs Animals Axon initial segment Axons - enzymology Casein Kinase II - metabolism Cells, Cultured Dominant negative Gene Expression Hippocampus - cytology Life Sciences Nav1 NAV1.2 Voltage-Gated Sodium Channel - genetics NAV1.2 Voltage-Gated Sodium Channel - metabolism Neurobiology Neurons and Cognition Phosphorylation Phosphospecific antibody Protein kinase CK2 Protein Processing, Post-Translational Protein Transport Rats Rats, Wistar |
| title | CK2 accumulation at the axon initial segment depends on sodium channel Nav1 |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-09T02%3A48%3A56IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_hal_p&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=CK2%20accumulation%20at%20the%20axon%20initial%20segment%20depends%20on%20sodium%20channel%20Nav1&rft.jtitle=FEBS%20letters&rft.au=Hien,%20Y.E.&rft.date=2014-09-17&rft.volume=588&rft.issue=18&rft.spage=3403&rft.epage=3408&rft.pages=3403-3408&rft.issn=0014-5793&rft.eissn=1873-3468&rft_id=info:doi/10.1016/j.febslet.2014.07.032&rft_dat=%3Cproquest_hal_p%3E1694975892%3C/proquest_hal_p%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1561967193&rft_id=info:pmid/25109776&rft_els_id=S001457931400581X&rfr_iscdi=true |