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...

Descripción completa

Detalles Bibliográficos
Autores principales: Salveson, Ian, Ames, James B.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2022
Materias:
Article
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
_version_ 1784797379884482560
author Salveson, Ian
Ames, James B.
author_facet Salveson, Ian
Ames, James B.
author_sort Salveson, Ian
collection PubMed
description 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).
format Online
Article
Text
id pubmed-9510106
institution National Center for Biotechnology Information
language English
publishDate 2022
publisher Springer Netherlands
record_format MEDLINE/PubMed
spelling pubmed-95101062022-09-27 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) Salveson, Ian Ames, James B. Biomol NMR Assign Article 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). Springer Netherlands 2022-09-05 2022 /pmc/articles/PMC9510106/ /pubmed/36064846 http://dx.doi.org/10.1007/s12104-022-10108-0 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Salveson, Ian
Ames, James B.
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)
title 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)
title_full 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)
title_fullStr 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)
title_full_unstemmed 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)
title_short 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)
title_sort 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)
topic Article
url 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
work_keys_str_mv AT salvesonian chemicalshiftassignmentsofthecterminaldomainofcabp1boundtotheiqmotifofvoltagegatedca2channelcav12
AT amesjamesb chemicalshiftassignmentsofthecterminaldomainofcabp1boundtotheiqmotifofvoltagegatedca2channelcav12

Ejemplares similares