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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 ELISA Kits) is an essential part of GCAP1 and GCAP2 (show GUCA1B ELISA Kits) 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 ELISA Kits) 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 ELISA Kits) activation by GCAP1 involves establishing a tight complex through the binding patch with an additional activation step involving Met-26, Lys (show LYZ ELISA Kits)-85, and Trp (show TBPL1 ELISA Kits)-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 ELISA Kits).
the GUCA1A mutation only contributes to a small portion of CORD in people of Chinese descent.
Stimulation by GCAP (show ALPPL2 ELISA Kits) increases the maximal velocity (Vmax) for retinal guanylyl cyclase activat (show GUCY2D ELISA Kits)ion up to 100-fold in HEK293 cell membranes.
Data suggest that GCAP1 (Mg2 (show MCOLN1 ELISA Kits)+ vs. Ca2 (show CA2 ELISA Kits)+) exhibits conformational changes in Ca2 (show CA2 ELISA Kits)+ switch helix that are important in activation of RetGC1 (show GUCY2D ELISA Kits) (photoreceptor guanylate cyclase); myristoylation of GCAP1 is important as well in attaining activator conformation.
Data suggest that dimerization domain of GUCY2D (show GUCY2D ELISA Kits) operates as a calcium-sensitive regulatory module; GUCY2D (show GUCY2D ELISA Kits) requires correct conformation of monomer-monomer interface for interaction with guanylate cyclase activating proteins (GCAP1; GCAP2 (show GUCA1B ELISA Kits)).
Presence of bound magnesium (Mg2 (show MCOLN1 ELISA Kits)+) in guanylate cyclase activator (show RCVRN ELISA Kits) 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 ELISA Kits)+)-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 ELISA Kits)+).
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 ELISA Kits) and makes RetGC1 (show GUCY2D ELISA Kits) 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 ELISA Kits) 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 ELISA Kits)) activation up to 20-fold in mouse photoreceptor outer segment.
GCAP-activated native retinal membrane (Ret (show RET ELISA Kits))GC1 and RetGC2 (show GUCY2F ELISA Kits) are less sensitive to inhibition by calcium ions in the presence of GCAP1 than GCAP2 (show GUCA2B ELISA Kits).
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.
guanylate cyclase activator 1A (retina)
, GCAP 1
, cone dystrophy 3
, guanylate cyclase-activating protein, photoreceptor 1
, guanylin 1, retina
, guanylyl cyclase-activating protein 1