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The GCAP1 and GCAP2 binding site(s) overlaps within the kinase homology and/or dimerization domains of retinal GC1.
This study identifies a new mechanism governing GCAP2 (show GUCA2B Proteins) subcellular distribution in vivo, closely related to disease.
Overexpression of guanylate cyclase activating protein 2 in rod photoreceptors in vivo leads to morphological changes at the synaptic ribbon.
GCAP (show GUCA1A Proteins)-activated native retinal membrane (Ret (show RET Proteins))GC1 and RetGC2 (show GUCY2F Proteins) are less sensitive to inhibition by calcium ions in the presence of GCAP1 (show GUCA1A Proteins) than GCAP2 (show GUCA2B Proteins).
GCAP2 (show GUCA2B Proteins) is a prime candidate for mediating Ca2 (show CA2 Proteins)+-dependent dynamic changes of synaptic ribbons in photoreceptor synapses
GCAP (show GUCA1A Proteins) functions in intact photoreceptors [review]
GCAP2 (show GUCA2B Proteins) regulation of guanylyl cyclase activity quickens the recovery of flash and step responses and adjusts the operating range of rods to higher intensities of ambient illumination
Prolonged illumination up-regulates retinal arrestin (show SAG Proteins) and Guca1a (show GUCA1A Proteins)/b: a novel mechanism for light adaptation.
Mapping Calcium-Sensitive Regions in the Neuronal Calcium Sensor GCAP2 by Site-Specific Fluorescence Labeling.
The C-terminal segment in GCAP2 confers target selectivity, facilitates membrane binding and provides sensitivity of the membrane localization of the protein to phosphorylation by rhodopsin kinase (show GRK1 Proteins).
Based on the distance constraints imposed by the cross-links, the study derived a 3D-structural model of the GCAP2 homodimer.
Data suggest that dimerization domain of GUCY2D (show GUCY2D Proteins) operates as a calcium-sensitive regulatory module; GUCY2D (show GUCY2D Proteins) requires correct conformation of monomer-monomer interface for interaction with guanylate cyclase activating proteins (GCAP1 (show GUCA1A Proteins); GCAP2).
interaction between N-terminally myristoylated GCAP-2 and a peptide derived from the catalytic domain of full-length ROS-GC 1
Ca2 (show CA2 Proteins)+ exerted a stabilizing effect on both myristoylated and non-myristoylated forms of the protein, which was significantly stronger for myristoylated GCAP2.
GCAP2 is a prime candidate for mediating Ca2 (show CA2 Proteins)+-dependent dynamic changes of synaptic ribbons in photoreceptor synapses
Findings show that the sequence motif of the core GCAP2-modulatory site is Tyr965-Asn981 of rod outer segment membrane guanylate cyclase (show GUCY2D Proteins) type 1 (ROS-GC1); this site is absolutely specific for GCAP2 and does not overlap with the GCAP1 (show GUCA1A Proteins)-modulated site.
Our data indicate that the Ca(2 (show CA2 Proteins)+)-sensitivity of GCAP2 is significantly controlled by its third Ca(2 (show CA2 Proteins)+)-binding site, EF-hand 3.
Dimerization domain of RETGC1 (show GUCY2D Proteins) is an essential part of GCAP1 (show GUCA1A Proteins) and GCAP2 binding interface.
The absence of clearly pathogenic mutations in the selected patient group suggests that the GUCA1B gene is a minor cause for retinal degenerations in Europeans or North-Americans.
Mutation in the GCAP 2 gene can cause one form of autosomal dominant retinal dystrophy (show MERTK Proteins), with variable phenotypic expression and incomplete penetrance.
The protein encoded by this gene is a calcium-binding protein that activates photoreceptor guanylate cyclases. This gene may have arisen due to a gene duplication event since there is a highly similar gene clustered with it on chromosome 6. Mutations in this gene can cause a form of retinitis pigmentosa.
guanylate cyclase activator 1B (retina)
, GCAP 2
, GCAP2 (retina)
, guanylyl cyclase-activating protein 2
, retinal guanylyl cyclase activator protein p24
, guanylate cyclase-activating protein, photoreceptor 2
, calcium binding protein
, guanylate cyclase activating protein 2