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

具有消除二聚化并增强环化酶活化的突变 (R22A) 的视网膜鸟苷酸环化酶活化蛋白 5 (GCAP5) 的化学位移分配。

• 影响指数: 0.731
• 发表时间: 2023 06 2
• 来源期刊: Biomol NMR Assign
• DOI: 10.1007/s12104-023-10129-3
• PMID: 37129703
• 文章类型: Journal Article
• 作者列表: Cudia D,Ahoulou EO,Ames JB

关键词: EF-hand; GCAP5; Phototransduction; R22A; Retinal guanylyl cyclase

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

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 GCAP5R22A) that abolishes protein dimerization and activates RetGC with 3-fold higher activity than that of wild type GCAP5 (BMRB No. 51,783).

摘要

脊椎动物视杆和视锥光感受器中的视网膜膜鸟苷酸环化酶（RetGC）被称为鸟苷酸环化酶激活蛋白（GCAP1-7）的神经元Ca2传感器蛋白家族激活。来自斑马鱼光感受器的GCAP5与RetGC结合，并赋予Ca2/Fe2依赖性调节RetGC酶活性，从而促进视觉光转导的恢复阶段。我们报告了具有R22A突变（称为GCAP5R22A）的GCAP5的NMR化学位移分配，该突变消除了蛋白质二聚化并激活了RetGC，其活性比野生型GCAP5高3倍（BMRB编号51,783）。