Movement of ‘gating charge’ is coupled to ligand binding in a G-protein-coupled receptor.
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| Title: | Movement of ‘gating charge’ is coupled to ligand binding in a G-protein-coupled receptor. |
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| Authors: | Ben-Chaim, Yair, Chanda, Baron, Dascal, Nathan, Bezanilla, Francisco, Parnas, Itzchak, Parnas, Hanna |
| Source: | Nature. 11/2/2006, Vol. 444 Issue 7115, p106-109. 4p. 3 Graphs. |
| Subjects: | Letters to the editor, G proteins |
| Abstract: | Activation by agonist binding of G-protein-coupled receptors (GPCRs) controls most signal transduction processes. Although these receptors span the cell membrane, they are not considered to be voltage sensitive. Recently it was shown that both the activity of GPCRs and their affinity towards agonists are regulated by membrane potential. However, it remains unclear whether GPCRs intrinsically respond to changes in membrane potential. Here we show that two prototypical GPCRs, the m2 and m1 muscarinic receptors (m2R and m1R), display charge-movement-associated currents analogous to ‘gating currents’ of voltage-gated channels. The gating charge–voltage relationship of m2R correlates well with the voltage dependence of the affinity of the receptor for acetylcholine. The loop that couples m2R and m1R to their G protein has a crucial function in coupling voltage sensing to agonist-binding affinity. Our data strongly indicate that GPCRs serve as sensors for both transmembrane potential and external chemical signals. [ABSTRACT FROM AUTHOR] |
| Copyright of Nature is the property of Springer Nature 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: | Psychology and Behavioral Sciences Collection |
| FullText | Links: – Type: pdflink Text: Availability: 0 |
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| Header | DbId: pbh DbLabel: Psychology and Behavioral Sciences Collection An: 22938032 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Movement of ‘gating charge’ is coupled to ligand binding in a G-protein-coupled receptor. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Ben-Chaim%2C+Yair%22">Ben-Chaim, Yair</searchLink><br /><searchLink fieldCode="AR" term="%22Chanda%2C+Baron%22">Chanda, Baron</searchLink><br /><searchLink fieldCode="AR" term="%22Dascal%2C+Nathan%22">Dascal, Nathan</searchLink><br /><searchLink fieldCode="AR" term="%22Bezanilla%2C+Francisco%22">Bezanilla, Francisco</searchLink><br /><searchLink fieldCode="AR" term="%22Parnas%2C+Itzchak%22">Parnas, Itzchak</searchLink><br /><searchLink fieldCode="AR" term="%22Parnas%2C+Hanna%22">Parnas, Hanna</searchLink> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Nature%22">Nature</searchLink>. 11/2/2006, Vol. 444 Issue 7115, p106-109. 4p. 3 Graphs. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Letters+to+the+editor%22">Letters to the editor</searchLink><br /><searchLink fieldCode="DE" term="%22G+proteins%22">G proteins</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Activation by agonist binding of G-protein-coupled receptors (GPCRs) controls most signal transduction processes. Although these receptors span the cell membrane, they are not considered to be voltage sensitive. Recently it was shown that both the activity of GPCRs and their affinity towards agonists are regulated by membrane potential. However, it remains unclear whether GPCRs intrinsically respond to changes in membrane potential. Here we show that two prototypical GPCRs, the m2 and m1 muscarinic receptors (m2R and m1R), display charge-movement-associated currents analogous to ‘gating currents’ of voltage-gated channels. The gating charge–voltage relationship of m2R correlates well with the voltage dependence of the affinity of the receptor for acetylcholine. The loop that couples m2R and m1R to their G protein has a crucial function in coupling voltage sensing to agonist-binding affinity. Our data strongly indicate that GPCRs serve as sensors for both transmembrane potential and external chemical signals. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Nature is the property of Springer Nature 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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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1038/nature05259 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 4 StartPage: 106 Subjects: – SubjectFull: Letters to the editor Type: general – SubjectFull: G proteins Type: general Titles: – TitleFull: Movement of ‘gating charge’ is coupled to ligand binding in a G-protein-coupled receptor. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Ben-Chaim, Yair – PersonEntity: Name: NameFull: Chanda, Baron – PersonEntity: Name: NameFull: Dascal, Nathan – PersonEntity: Name: NameFull: Bezanilla, Francisco – PersonEntity: Name: NameFull: Parnas, Itzchak – PersonEntity: Name: NameFull: Parnas, Hanna IsPartOfRelationships: – BibEntity: Dates: – D: 02 M: 11 Text: 11/2/2006 Type: published Y: 2006 Identifiers: – Type: issn-print Value: 00280836 Numbering: – Type: volume Value: 444 – Type: issue Value: 7115 Titles: – TitleFull: Nature Type: main |
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