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anti-Mouse (Murine) GUCA1B Anticorps:
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Cow (Bovine) Polyclonal GUCA1B Primary Antibody pour WB - ABIN6746667
Chen, Chédotal, He, Goodman, Tessier-Lavigne: Neuropilin-2, a novel member of the neuropilin family, is a high affinity receptor for the semaphorins Sema E and Sema IV but not Sema III. dans Neuron 1997
Show all 3 Pubmed References
conclude that, under normal physiological conditions, GCAP1 dominates the regulation of cGMP synthesis in mouse cones, but if its function becomes compromised, GCAP2 contributes to the regulation of phototransduction and light adaptation of cones
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 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-activated native retinal membrane (Ret)GC1 and RetGC2 are less sensitive to inhibition by calcium ions in the presence of GCAP1 than GCAP2.
GCAP2 is a prime candidate for mediating Ca2+-dependent dynamic changes of synaptic ribbons in photoreceptor synapses
GCAP functions in intact photoreceptors [review]
GCAP2 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 and Guca1a/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.
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 operates as a calcium-sensitive regulatory module; GUCY2D requires correct conformation of monomer-monomer interface for interaction with guanylate cyclase activating proteins (GCAP1; GCAP2).
interaction between N-terminally myristoylated GCAP-2 and a peptide derived from the catalytic domain of full-length ROS-GC 1
Ca2+ exerted a stabilizing effect on both myristoylated and non-myristoylated forms of the protein, which was significantly stronger for myristoylated GCAP2.
Findings show that the sequence motif of the core GCAP2-modulatory site is Tyr965-Asn981 of rod outer segment membrane guanylate cyclase type 1 (ROS-GC1); this site is absolutely specific for GCAP2 and does not overlap with the GCAP1-modulated site.
Our data indicate that the Ca(2+)-sensitivity of GCAP2 is significantly controlled by its third Ca(2+)-binding site, EF-hand 3.
GCAP1 and GCAP2 bound to different regions on the target guanylate cyclase type 1 with submicromolar affinity (apparent KD-values of 663 +/- 121 nM and 231 +/- 63 nM for Ca(2+)-free GCAP1 and GCAP2, respectively).
Dimerization domain of RETGC1 is an essential part of GCAP1 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, 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