Identification of domains that control the heteromeric assembly of Kir5.1/Kir4.0 potassium channels.

Heteromultimerization between different inwardly rectifying (Kir) potassium channel subunits is an important mechanism for the generation of functional diversity. However, little is known about the mechanisms that control this process and that prevent promiscuous interactions in cells that express m...

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Main Authors: Konstas, A, Korbmacher, C, Tucker, S
Format: Journal article
Language:English
Published: 2003
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author Konstas, A
Korbmacher, C
Tucker, S
author_facet Konstas, A
Korbmacher, C
Tucker, S
author_sort Konstas, A
collection OXFORD
description Heteromultimerization between different inwardly rectifying (Kir) potassium channel subunits is an important mechanism for the generation of functional diversity. However, little is known about the mechanisms that control this process and that prevent promiscuous interactions in cells that express many different Kir subunits. In this study, we have examined the heteromeric assembly of Kir5.1 with other Kir subunits and have shown that this subunit exhibits a highly selective interaction with members of the Kir4.0 subfamily and does not physically associate with other Kir subunits such as Kir1.1, Kir2.1, and Kir6.2. Furthermore, we have identified regions within the Kir4.1 subunit that appear to govern the specificity of this interaction. These results help us to understand the mechanisms that control Kir subunit recognition and assembly and how cells can express many different Kir channels while maintaining distinct subpopulations of homo- and heteromeric channels within the cell.
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spelling oxford-uuid:45a6c93c-9139-4333-aca8-bf255cd81f4e2022-03-26T15:09:06ZIdentification of domains that control the heteromeric assembly of Kir5.1/Kir4.0 potassium channels.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:45a6c93c-9139-4333-aca8-bf255cd81f4eEnglishSymplectic Elements at Oxford2003Konstas, AKorbmacher, CTucker, SHeteromultimerization between different inwardly rectifying (Kir) potassium channel subunits is an important mechanism for the generation of functional diversity. However, little is known about the mechanisms that control this process and that prevent promiscuous interactions in cells that express many different Kir subunits. In this study, we have examined the heteromeric assembly of Kir5.1 with other Kir subunits and have shown that this subunit exhibits a highly selective interaction with members of the Kir4.0 subfamily and does not physically associate with other Kir subunits such as Kir1.1, Kir2.1, and Kir6.2. Furthermore, we have identified regions within the Kir4.1 subunit that appear to govern the specificity of this interaction. These results help us to understand the mechanisms that control Kir subunit recognition and assembly and how cells can express many different Kir channels while maintaining distinct subpopulations of homo- and heteromeric channels within the cell.
spellingShingle Konstas, A
Korbmacher, C
Tucker, S
Identification of domains that control the heteromeric assembly of Kir5.1/Kir4.0 potassium channels.
title Identification of domains that control the heteromeric assembly of Kir5.1/Kir4.0 potassium channels.
title_full Identification of domains that control the heteromeric assembly of Kir5.1/Kir4.0 potassium channels.
title_fullStr Identification of domains that control the heteromeric assembly of Kir5.1/Kir4.0 potassium channels.
title_full_unstemmed Identification of domains that control the heteromeric assembly of Kir5.1/Kir4.0 potassium channels.
title_short Identification of domains that control the heteromeric assembly of Kir5.1/Kir4.0 potassium channels.
title_sort identification of domains that control the heteromeric assembly of kir5 1 kir4 0 potassium channels
work_keys_str_mv AT konstasa identificationofdomainsthatcontroltheheteromericassemblyofkir51kir40potassiumchannels
AT korbmacherc identificationofdomainsthatcontroltheheteromericassemblyofkir51kir40potassiumchannels
AT tuckers identificationofdomainsthatcontroltheheteromericassemblyofkir51kir40potassiumchannels