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A mutation in the β interaction domain of the Ca2+ channel α1C subunit reduces the affinity of the (+)-[3H]isradipine binding site

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Title: A mutation in the β interaction domain of the Ca2+ channel α1C subunit reduces the affinity of the (+)-[3H]isradipine binding site
Authors: Hitzl, Monika, Striessnig, Jörg, Neuhuber, Birgit, Flucher, Bernhard E. bernhard.e.flucher@uibk.ac.at
Source: FEBS Letters. Jul2002, Vol. 524 Issue 1-3, p188. 5p.
Subjects: Calcium channels, Radioligand assay
Abstract: The molecular mechanisms of how α1 and β subunits of voltage-gated Ca2+ channels interact with one another are still controversial. Here we show that despite a mutation in the β interaction domain that has previously been shown to disrupt binding, α1CY467S and β1a-myc still formed immunoprecipitable complexes when coexpressed in tsA201 cells. However, the α1CY467S–β1a-myc complexes had a decreased affinity to (+)-[3H]isradipine. This indicates that the β interaction domain in the I–II loop of the α1 subunit is not merely an anchor required for the functional interaction of the two Ca2+ channel subunits but is itself part of the effector pathway for β-induced channel modulation. [Copyright &y& Elsevier]
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.)
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DbLabel: Engineering Source
An: 7852128
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
PreciseRelevancyScore: 0
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  Data: A mutation in the β interaction domain of the Ca<superscript>2+</superscript> channel α<subscript>1C</subscript> subunit reduces the affinity of the (+)-[<superscript>3</superscript>H]isradipine binding site
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  Data: <searchLink fieldCode="AR" term="%22Hitzl%2C+Monika%22">Hitzl, Monika</searchLink><br /><searchLink fieldCode="AR" term="%22Striessnig%2C+Jörg%22">Striessnig, Jörg</searchLink><br /><searchLink fieldCode="AR" term="%22Neuhuber%2C+Birgit%22">Neuhuber, Birgit</searchLink><br /><searchLink fieldCode="AR" term="%22Flucher%2C+Bernhard+E%2E%22">Flucher, Bernhard E.</searchLink><i> bernhard.e.flucher@uibk.ac.at</i>
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  Data: <searchLink fieldCode="JN" term="%22FEBS+Letters%22">FEBS Letters</searchLink>. Jul2002, Vol. 524 Issue 1-3, p188. 5p.
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  Data: <searchLink fieldCode="DE" term="%22Calcium+channels%22">Calcium channels</searchLink><br /><searchLink fieldCode="DE" term="%22Radioligand+assay%22">Radioligand assay</searchLink>
– Name: Abstract
  Label: Abstract
  Group: Ab
  Data: The molecular mechanisms of how α1 and β subunits of voltage-gated Ca2+ channels interact with one another are still controversial. Here we show that despite a mutation in the β interaction domain that has previously been shown to disrupt binding, α1CY467S and β1a-myc still formed immunoprecipitable complexes when coexpressed in tsA201 cells. However, the α1CY467S–β1a-myc complexes had a decreased affinity to (+)-[3H]isradipine. This indicates that the β interaction domain in the I–II loop of the α1 subunit is not merely an anchor required for the functional interaction of the two Ca2+ channel subunits but is itself part of the effector pathway for β-induced channel modulation. [Copyright &y& Elsevier]
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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/S0014-5793(02)03054-5
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      – Code: eng
        Text: English
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        PageCount: 5
        StartPage: 188
    Subjects:
      – SubjectFull: Calcium channels
        Type: general
      – SubjectFull: Radioligand assay
        Type: general
    Titles:
      – TitleFull: A mutation in the β interaction domain of the Ca2+ channel α1C subunit reduces the affinity of the (+)-[3H]isradipine binding site
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            NameFull: Hitzl, Monika
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            NameFull: Striessnig, Jörg
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            NameFull: Neuhuber, Birgit
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            NameFull: Flucher, Bernhard E.
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              Text: Jul2002
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              Y: 2002
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              Value: 524
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