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Chemical shift assignments of the C-terminal domain of CaBP1 bound to the IQ-motif of voltage-gated Ca(2+) channel (Ca(V)1.2)

The neuronal L-type voltage-gated Ca(2+) channel (Ca(V)1.2) interacts with Ca(2+) binding protein 1 (CaBP1), that promotes Ca(2+)-induced channel activity. The binding of CaBP1 to the IQ-motif in Ca(V)1.2 (residues 1644–1665) blocks the binding of calmodulin and prevents Ca(2+)-dependent inactivatio...

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Detalles Bibliográficos
Autores principales: Salveson, Ian, Ames, James B.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9510106/
https://www.ncbi.nlm.nih.gov/pubmed/36064846
http://dx.doi.org/10.1007/s12104-022-10108-0
Descripción
Sumario:The neuronal L-type voltage-gated Ca(2+) channel (Ca(V)1.2) interacts with Ca(2+) binding protein 1 (CaBP1), that promotes Ca(2+)-induced channel activity. The binding of CaBP1 to the IQ-motif in Ca(V)1.2 (residues 1644–1665) blocks the binding of calmodulin and prevents Ca(2+)-dependent inactivation of Ca(V)1.2. This Ca(2+)-induced binding of CaBP1 to Ca(V)1.2 is important for modulating neuronal synaptic plasticity, which may serve a role in learning and memory. Here we report NMR assignments of the C-terminal domain of CaBP1 (residues 99–167, called CaBP1C) that contains two Ca(2+) bound at the third and fourth EF-hands (EF3 and EF4) and is bound to the Ca(V)1.2 IQ-motif from Ca(V)1.2 (BMRB accession no. 51518).