Interactions of Calmodulin With the Multiple Binding Sites of Cav1.2 Ca2+ Channels
Although calmodulin binding to various sites of the Cav1.2 Ca2+ channel has been reported, the mechanism of the interaction is not fully understood. In this study we examined calmodulin binding to fragment channel peptides using a semi-quantitative pull-down assay. Calmodulin bound to the peptides w...
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Elsevier
2010-01-01
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Series: | Journal of Pharmacological Sciences |
Online Access: | http://www.sciencedirect.com/science/article/pii/S1347861319309740 |
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author | Hadhimulya Asmara Etsuko Minobe Zahangir A. Saud Masaki Kameyama |
author_facet | Hadhimulya Asmara Etsuko Minobe Zahangir A. Saud Masaki Kameyama |
author_sort | Hadhimulya Asmara |
collection | DOAJ |
description | Although calmodulin binding to various sites of the Cav1.2 Ca2+ channel has been reported, the mechanism of the interaction is not fully understood. In this study we examined calmodulin binding to fragment channel peptides using a semi-quantitative pull-down assay. Calmodulin bound to the peptides with decreasing affinity order: IQ > preIQ > I-II loop > N-terminal peptide. A peptide containing both preIQ and IQ regions (Leu1599 – Leu1668) bound with approximately 2 mol of calmodulin per peptide. These results support the hypothesis that two molecules of calmodulin can simultaneously bind to the C-terminus of the Cav1.2 channel and modulate its facilitatory and inhibitory activities. Keywords:: calcium channel, calmodulin, ion channel regulation, IQ motif, cardiac myocyte |
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institution | Directory Open Access Journal |
issn | 1347-8613 |
language | English |
last_indexed | 2024-12-22T00:40:42Z |
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spelling | doaj.art-4d21783f778f430b9811f0ce841ad9592022-12-21T18:44:42ZengElsevierJournal of Pharmacological Sciences1347-86132010-01-011124397404Interactions of Calmodulin With the Multiple Binding Sites of Cav1.2 Ca2+ ChannelsHadhimulya Asmara0Etsuko Minobe1Zahangir A. Saud2Masaki Kameyama3Department of Physiology, Graduate School of Medical and Dental Sciences, Kagoshima University, Kagoshima 890-8544, JapanDepartment of Physiology, Graduate School of Medical and Dental Sciences, Kagoshima University, Kagoshima 890-8544, JapanDepartment of Physiology, Graduate School of Medical and Dental Sciences, Kagoshima University, Kagoshima 890-8544, JapanDepartment of Physiology, Graduate School of Medical and Dental Sciences, Kagoshima University, Kagoshima 890-8544, Japan; Corresponding author. kame@m.kufm.kagoshima-u.ac.jpAlthough calmodulin binding to various sites of the Cav1.2 Ca2+ channel has been reported, the mechanism of the interaction is not fully understood. In this study we examined calmodulin binding to fragment channel peptides using a semi-quantitative pull-down assay. Calmodulin bound to the peptides with decreasing affinity order: IQ > preIQ > I-II loop > N-terminal peptide. A peptide containing both preIQ and IQ regions (Leu1599 – Leu1668) bound with approximately 2 mol of calmodulin per peptide. These results support the hypothesis that two molecules of calmodulin can simultaneously bind to the C-terminus of the Cav1.2 channel and modulate its facilitatory and inhibitory activities. Keywords:: calcium channel, calmodulin, ion channel regulation, IQ motif, cardiac myocytehttp://www.sciencedirect.com/science/article/pii/S1347861319309740 |
spellingShingle | Hadhimulya Asmara Etsuko Minobe Zahangir A. Saud Masaki Kameyama Interactions of Calmodulin With the Multiple Binding Sites of Cav1.2 Ca2+ Channels Journal of Pharmacological Sciences |
title | Interactions of Calmodulin With the Multiple Binding Sites of Cav1.2 Ca2+ Channels |
title_full | Interactions of Calmodulin With the Multiple Binding Sites of Cav1.2 Ca2+ Channels |
title_fullStr | Interactions of Calmodulin With the Multiple Binding Sites of Cav1.2 Ca2+ Channels |
title_full_unstemmed | Interactions of Calmodulin With the Multiple Binding Sites of Cav1.2 Ca2+ Channels |
title_short | Interactions of Calmodulin With the Multiple Binding Sites of Cav1.2 Ca2+ Channels |
title_sort | interactions of calmodulin with the multiple binding sites of cav1 2 ca2 channels |
url | http://www.sciencedirect.com/science/article/pii/S1347861319309740 |
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