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Title: Apo calmodulin binding to the L-type voltage-gated calcium channel Ca{sub v}1.2 IQ peptide

Abstract

The influx of calcium through the L-type voltage-gated calcium channels (LTCCs) is the trigger for the process of calcium-induced calcium release (CICR) from the sarcoplasmic recticulum, an essential step for cardiac contraction. There are two feedback mechanisms that regulate LTCC activity: calcium-dependent inactivation (CDI) and calcium-dependent facilitation (CDF), both of which are mediated by calmodulin (CaM) binding. The IQ domain (aa 1645-1668) housed within the cytoplasmic domain of the LTCC Ca{sub v}1.2 subunit has been shown to bind both calcium-loaded (Ca{sup 2+}CaM ) and calcium-free CaM (apoCaM). Here, we provide new data for the structural basis for the interaction of apoCaM with the IQ peptide using NMR, revealing that the apoCaM C-lobe residues are most significantly perturbed upon complex formation. In addition, we have employed transmission electron microscopy of purified LTCC complexes which shows that both apoCaM and Ca{sup 2+}CaM can bind to the intact channel.

Authors:
 [1];  [2];  [2]
  1. School of Biological Sciences, University of Liverpool, P.O. Box 147, Liverpool L69 7ZB (United Kingdom)
  2. School of Medicine, Cardiovascular and Endocrine Sciences, University of Manchester, Manchester M13 9NT (United Kingdom)
Publication Date:
OSTI Identifier:
20979793
Resource Type:
Journal Article
Journal Name:
Biochemical and Biophysical Research Communications
Additional Journal Information:
Journal Volume: 353; Journal Issue: 3; Other Information: DOI: 10.1016/j.bbrc.2006.12.070; PII: S0006-291X(06)02700-8; Copyright (c) 2006 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; CALCIUM; CALCIUM IONS; CALMODULIN; ELECTRIC POTENTIAL; NUCLEAR MAGNETIC RESONANCE; PEPTIDES; TRANSMISSION ELECTRON MICROSCOPY

Citation Formats

Luyun, Lian, Myatt, Daniel, and Kitmitto, Ashraf. Apo calmodulin binding to the L-type voltage-gated calcium channel Ca{sub v}1.2 IQ peptide. United States: N. p., 2007. Web. doi:10.1016/j.bbrc.2006.12.070.
Luyun, Lian, Myatt, Daniel, & Kitmitto, Ashraf. Apo calmodulin binding to the L-type voltage-gated calcium channel Ca{sub v}1.2 IQ peptide. United States. doi:10.1016/j.bbrc.2006.12.070.
Luyun, Lian, Myatt, Daniel, and Kitmitto, Ashraf. Fri . "Apo calmodulin binding to the L-type voltage-gated calcium channel Ca{sub v}1.2 IQ peptide". United States. doi:10.1016/j.bbrc.2006.12.070.
@article{osti_20979793,
title = {Apo calmodulin binding to the L-type voltage-gated calcium channel Ca{sub v}1.2 IQ peptide},
author = {Luyun, Lian and Myatt, Daniel and Kitmitto, Ashraf},
abstractNote = {The influx of calcium through the L-type voltage-gated calcium channels (LTCCs) is the trigger for the process of calcium-induced calcium release (CICR) from the sarcoplasmic recticulum, an essential step for cardiac contraction. There are two feedback mechanisms that regulate LTCC activity: calcium-dependent inactivation (CDI) and calcium-dependent facilitation (CDF), both of which are mediated by calmodulin (CaM) binding. The IQ domain (aa 1645-1668) housed within the cytoplasmic domain of the LTCC Ca{sub v}1.2 subunit has been shown to bind both calcium-loaded (Ca{sup 2+}CaM ) and calcium-free CaM (apoCaM). Here, we provide new data for the structural basis for the interaction of apoCaM with the IQ peptide using NMR, revealing that the apoCaM C-lobe residues are most significantly perturbed upon complex formation. In addition, we have employed transmission electron microscopy of purified LTCC complexes which shows that both apoCaM and Ca{sup 2+}CaM can bind to the intact channel.},
doi = {10.1016/j.bbrc.2006.12.070},
journal = {Biochemical and Biophysical Research Communications},
issn = {0006-291X},
number = 3,
volume = 353,
place = {United States},
year = {2007},
month = {2}
}