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Lobe-related concentration- and Ca2+-dependent interactions of calmodulin with C- and N-terminal tails of the CaV1.2 channel
- Source :
- The Journal of Physiological Sciences. 63:345-353
- Publication Year :
- 2013
- Publisher :
- Springer Science and Business Media LLC, 2013.
-
Abstract
- This study examined the bindings of calmodulin (CaM) and its mutants with the C- and N-terminal tails of the voltage-gated Ca(2+) channel CaV1.2 at different CaM and Ca(2+) concentrations ([Ca(2+)]) by using the pull-down assay method to obtain basic information on the binding mode, including its concentration- and Ca(2+)-dependencies. Our data show that more than one CaM molecule could bind to the CaV1.2 C-terminal tail at high [Ca(2+)]. Additionally, the C-lobe of CaM is highly critical in sensing the change of [Ca(2+)] in its binding to the C-terminal tail of CaV1.2, and the binding between CaM and the N-terminal tail of CaV1.2 requires high [Ca(2+)]. Our data provide new details on the interactions between CaM and the CaV1.2 channel.
- Subjects :
- animal structures
Calcium Channels, L-Type
biology
Calmodulin
Voltage-dependent calcium channel
Physiology
Chemistry
Molecular Sequence Data
Mutant
Human physiology
Plasma protein binding
Cav1.2
Biochemistry
Mutation
biology.protein
Biophysics
Humans
Molecule
Calcium
Amino Acid Sequence
Peptide sequence
Protein Binding
Subjects
Details
- ISSN :
- 18806562 and 18806546
- Volume :
- 63
- Database :
- OpenAIRE
- Journal :
- The Journal of Physiological Sciences
- Accession number :
- edsair.doi.dedup.....daaabe22b3b394426e82b0fdd72647bf