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CK2 accumulation at the axon initial segment depends on sodium channel Nav1.

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Title: CK2 accumulation at the axon initial segment depends on sodium channel Nav1.
Authors: Hien, Y.E.1, Montersino, A.1, Castets, F.1, Leterrier, C.1, Filhol, O.2, Vacher, H.1 helene.vacher@univ-amu.fr, Dargent, B.1
Source: FEBS Letters. Sep2014, Vol. 588 Issue 18, p3403-3408. 6p.
Subjects: Bioaccumulation, In vitro studies, Phosphorylation, Protein expression, Protein kinase CK2, Axons
Abstract: 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 FROM AUTHOR]
Copyright of FEBS Letters is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
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Header DbId: egs
DbLabel: Engineering Source
An: 97933176
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
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  Data: CK2 accumulation at the axon initial segment depends on sodium channel Nav1.
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  Data: <searchLink fieldCode="JN" term="%22FEBS+Letters%22">FEBS Letters</searchLink>. Sep2014, Vol. 588 Issue 18, p3403-3408. 6p.
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  Data: <searchLink fieldCode="DE" term="%22Bioaccumulation%22">Bioaccumulation</searchLink><br /><searchLink fieldCode="DE" term="%22In+vitro+studies%22">In vitro studies</searchLink><br /><searchLink fieldCode="DE" term="%22Phosphorylation%22">Phosphorylation</searchLink><br /><searchLink fieldCode="DE" term="%22Protein+expression%22">Protein expression</searchLink><br /><searchLink fieldCode="DE" term="%22Protein+kinase+CK2%22">Protein kinase CK2</searchLink><br /><searchLink fieldCode="DE" term="%22Axons%22">Axons</searchLink>
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  Data: 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 FROM AUTHOR]
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  Data: <i>Copyright of FEBS Letters is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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      – Type: doi
        Value: 10.1016/j.febslet.2014.07.032
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      – Code: eng
        Text: English
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        Type: general
      – SubjectFull: In vitro studies
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      – SubjectFull: Phosphorylation
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      – SubjectFull: Protein expression
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      – SubjectFull: Protein kinase CK2
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      – SubjectFull: Axons
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      – TitleFull: CK2 accumulation at the axon initial segment depends on sodium channel Nav1.
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              Text: Sep2014
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