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GUCA1A mutations could cause significant variability in maculopathies, including central areolar choroidal dystrophy, which represents a severe pattern of maculopathy.
GCAP1 mutation is associated with macular dystrophy.
Retinal dystrophy-associated missense mutations (L84F, I107T) in GUCA1A with distinct molecular properties result in a similar aberrant regulation of the retinal guanylate cyclase.
Dimerization domain of RETGC1 (show GUCY2D Antibodies) is an essential part of GCAP1 and GCAP2 (show GUCA1B Antibodies) binding interface.
The GCAP1 and GCAP2 binding site(s) overlaps within the kinase homology and/or dimerization domains of retinal GC1.
GUCA1A and GUCY2D (show GUCY2D Antibodies) mutations are both accompanied by similar pattern of generalized cone dysfunction with a tendency to less involvement of the rod photoreceptors and a less severe phenotype in patients with GUCA1A.
RetGC1 (show GUCY2D Antibodies) activation by GCAP1 involves establishing a tight complex through the binding patch with an additional activation step involving Met-26, Lys (show LYZ Antibodies)-85, and Trp (show TBPL1 Antibodies)-94.
All four mutant GCAP1 family members showed sensitivity or acuity losses relative to normal observers.
we predicted that either haploinsufficiency or dominant-negative effect accompanied by creation of a novel function for the mutant protein is a possible mechanism of the retinal degeneration due to c.250C>T and c.320T>C of the GUCA1A
Patients with autosomal dominant cone-rod dystrophy caused by a D100G mutation in GUCA1A exhibit progressive vision loss early within the first decade of life identifiable by distinct ERG (show ERG Antibodies).
Data suggest that GCAP1 (Mg2 (show MCOLN1 Antibodies)+ vs. Ca2 (show CA2 Antibodies)+) exhibits conformational changes in Ca2 (show CA2 Antibodies)+ switch helix that are important in activation of RetGC1 (show GUCY2D Antibodies) (photoreceptor guanylate cyclase); myristoylation of GCAP1 is important as well in attaining activator conformation.
Data suggest that dimerization domain of GUCY2D (show GUCY2D Antibodies) operates as a calcium-sensitive regulatory module; GUCY2D (show GUCY2D Antibodies) requires correct conformation of monomer-monomer interface for interaction with guanylate cyclase activating proteins (GCAP1; GCAP2 (show GUCA1B Antibodies)).
Presence of bound magnesium (Mg2 (show MCOLN1 Antibodies)+) in guanylate cyclase activator (show RCVRN Antibodies) protein GCAP-1 is essential for its ability to stimulate retinal guanylyl cyclase.
Direct association between RD3 and GCAP1 is important for GC1 targeting.
The wild type and mutants of GCAP1 displayed large differences in Ca(2 (show CA2 Antibodies)+)-binding and regulation and preserved an intact secondary and tertiary structure with a significant rearrangement of the aromatic residues upon binding of Ca(2 (show CA2 Antibodies)+).
GCAP1 is the 'first-response' sensor protein that stimulates retinal membrane guanylyl cyclase early in the rod photoresponse.
results argue that there must be a cellular mechanism that limits GCAP1 access to RetGC2 (show GUCY2F Antibodies) and makes RetGC1 (show GUCY2D Antibodies) isozyme a preferential target for the disease-causing GCAP1 mutants.
Recombinant Gcap14 protein cosedimented with pure microtubules, indicating a direct binding between the two
Calcium-myristoyl Tug (show ASPSCR1 Antibodies) is a new mechanism for intramolecular tuning of calcium sensitivity and target enzyme interaction for guanylyl cyclase-activating protein 1
Stimulation by GCAP increases the maximal velocity (Vmax) for retinal guanylyl cyclase (RetGC1 (show GUCY2D Antibodies)) activation up to 20-fold in mouse photoreceptor outer segment.
GCAP-activated native retinal membrane (Ret (show RET Antibodies))GC1 and RetGC2 (show GUCY2F Antibodies) are less sensitive to inhibition by calcium ions in the presence of GCAP1 than GCAP2 (show GUCA2B Antibodies).
Mutant GCAP1, when under normal expression control, causes both rod and cone photoreceptors to lose function and degenerate, with cone cells being more severely affected, in keeping with the human disease phenotype.
This gene plays a role in the recovery of retinal photoreceptors from photobleaching. In the recovery phase, the phototransduction messeneger cGMP is replenished by retinal guanylyl cyclase-1 (GC1). GC1 is activated by decreasing Ca(2+) concentrations following photobleaching. The protein encoded by this gene, guanylyl cyclase activating protein 1 (GCAP1), mediates the sensitivity of GC1 to Ca(2+) concentrations. GCAP1 promotes activity of GC1 at low Ca(2+) concentrations and inhibits GC1 activity at high Ca(2+) concentrations. Mutations in this gene cause autosomal dominant cone dystrophy (COD3)\; a disease characterized by reduced visual acuity associated with progressive loss of color vision. Mutations in this gene prohibit the inactivation of RetGC1 at high Ca(2+) concentrations\; causing the constitutive activation of RetGC1 and, presumably, increased cell death. This gene is expressed in retina and spermatagonia.
, cone dystrophy 3
, guanylate cyclase-activating protein, photoreceptor 1
, guanylin 1, retina
, guanylyl cyclase-activating protein 1
, guanylate cyclase activator 1A (retina)