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

Diana Cudia; Effibe O Ahoulou; James B Ames

doi:10.1007/s12104-023-10129-3

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

Biomol NMR Assign. 2023 Jun;17(1):115-119. doi: 10.1007/s12104-023-10129-3. Epub 2023 May 2.

Authors

Diana Cudia¹, Effibe O Ahoulou¹, James B Ames²

Affiliations

¹ Department of Chemistry, University of California, Davis, CA, 95616, USA.
² Department of Chemistry, University of California, Davis, CA, 95616, USA. jbames@ucdavis.edu.

Abstract

Retinal membrane guanylyl cyclases (RetGCs) in vertebrate rod and cone photoreceptors are activated by a family of neuronal Ca²⁺ sensor proteins called guanylyl cyclase activating proteins (GCAP1-7). GCAP5 from zebrafish photoreceptors binds to RetGC and confers Ca²⁺/Fe²⁺-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).

Keywords: EF-hand; GCAP5; Phototransduction; R22A; Retinal guanylyl cyclase.

Publication types

Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't

MeSH terms

Animals
Calcium / metabolism
Dimerization
Guanylate Cyclase* / chemistry
Guanylate Cyclase* / genetics
Guanylate Cyclase* / metabolism
Guanylate Cyclase-Activating Proteins* / chemistry
Mutation
Nuclear Magnetic Resonance, Biomolecular
Zebrafish / metabolism

Substances

Calcium
Guanylate Cyclase
Guanylate Cyclase-Activating Proteins
guca1e protein, zebrafish

Grants and funding

R01 EY012347/EY/NEI NIH HHS/United States