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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Main Authors: Hadhimulya Asmara, Etsuko Minobe, Zahangir A. Saud, Masaki Kameyama
Format: Article
Language:English
Published: Elsevier 2010-01-01
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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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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