Chemical shift assignments of retinal guanylyl cyclase activating protein 5 (GCAP5) with a mutation (R22A) that abolishes dimerization and enhances cyclase activation

Retinal membrane guanylyl cyclases (RetGCs) in vertebrate rod and cone photoreceptors are activated by a family of neuronal Ca(2+) sensor proteins called guanylyl cyclase activating proteins (GCAP1-7). GCAP5 from zebrafish photoreceptors binds to RetGC and confers Ca(2+)/Fe(2+)-dependent regulation...

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Autores principales: Cudia, Diana, Ahoulou, Effibe O., Ames, James B.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Netherlands 2023
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10232645/
https://www.ncbi.nlm.nih.gov/pubmed/37129703
http://dx.doi.org/10.1007/s12104-023-10129-3
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author Cudia, Diana
Ahoulou, Effibe O.
Ames, James B.
author_facet Cudia, Diana
Ahoulou, Effibe O.
Ames, James B.
author_sort Cudia, Diana
collection PubMed
description Retinal membrane guanylyl cyclases (RetGCs) in vertebrate rod and cone photoreceptors are activated by a family of neuronal Ca(2+) sensor proteins called guanylyl cyclase activating proteins (GCAP1-7). GCAP5 from zebrafish photoreceptors binds to RetGC and confers Ca(2+)/Fe(2+)-dependent regulation of RetGC enzymatic activity that promotes the recovery phase of visual phototransduction. We report NMR chemical shift assignments of GCAP5 with a R22A mutation (called GCAP5(R22A)) that abolishes protein dimerization and activates RetGC with 3-fold higher activity than that of wild type GCAP5 (BMRB No. 51,783).
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spelling pubmed-102326452023-06-02 Chemical shift assignments of retinal guanylyl cyclase activating protein 5 (GCAP5) with a mutation (R22A) that abolishes dimerization and enhances cyclase activation Cudia, Diana Ahoulou, Effibe O. Ames, James B. Biomol NMR Assign Article Retinal membrane guanylyl cyclases (RetGCs) in vertebrate rod and cone photoreceptors are activated by a family of neuronal Ca(2+) sensor proteins called guanylyl cyclase activating proteins (GCAP1-7). GCAP5 from zebrafish photoreceptors binds to RetGC and confers Ca(2+)/Fe(2+)-dependent regulation of RetGC enzymatic activity that promotes the recovery phase of visual phototransduction. We report NMR chemical shift assignments of GCAP5 with a R22A mutation (called GCAP5(R22A)) that abolishes protein dimerization and activates RetGC with 3-fold higher activity than that of wild type GCAP5 (BMRB No. 51,783). Springer Netherlands 2023-05-02 2023 /pmc/articles/PMC10232645/ /pubmed/37129703 http://dx.doi.org/10.1007/s12104-023-10129-3 Text en © The Author(s) 2023 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
Cudia, Diana
Ahoulou, Effibe O.
Ames, James B.
Chemical shift assignments of retinal guanylyl cyclase activating protein 5 (GCAP5) with a mutation (R22A) that abolishes dimerization and enhances cyclase activation
title Chemical shift assignments of retinal guanylyl cyclase activating protein 5 (GCAP5) with a mutation (R22A) that abolishes dimerization and enhances cyclase activation
title_full Chemical shift assignments of retinal guanylyl cyclase activating protein 5 (GCAP5) with a mutation (R22A) that abolishes dimerization and enhances cyclase activation
title_fullStr Chemical shift assignments of retinal guanylyl cyclase activating protein 5 (GCAP5) with a mutation (R22A) that abolishes dimerization and enhances cyclase activation
title_full_unstemmed Chemical shift assignments of retinal guanylyl cyclase activating protein 5 (GCAP5) with a mutation (R22A) that abolishes dimerization and enhances cyclase activation
title_short Chemical shift assignments of retinal guanylyl cyclase activating protein 5 (GCAP5) with a mutation (R22A) that abolishes dimerization and enhances cyclase activation
title_sort chemical shift assignments of retinal guanylyl cyclase activating protein 5 (gcap5) with a mutation (r22a) that abolishes dimerization and enhances cyclase activation
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10232645/
https://www.ncbi.nlm.nih.gov/pubmed/37129703
http://dx.doi.org/10.1007/s12104-023-10129-3
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AT amesjamesb chemicalshiftassignmentsofretinalguanylylcyclaseactivatingprotein5gcap5withamutationr22athatabolishesdimerizationandenhancescyclaseactivation

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