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Compound heterozygous mutations (NM000087, p.Y82X and p.L89fs) in exon 6 of CNGA1are pathogenic mutations in this Chinese family affected with autosomal recessive retinitis pigmentosa. Of which, p.Y82X is firstly reported in patient with autosomal recessive retinitis pigmentosa.
The mut CNGA1 p.(G513R) protein was largely retained inside the cell rather than being targeted to the plasma membrane, suggesting the absence of cGMP-gated cation channels in the plasma membrane
CNGA1 mutations are one of the most frequent autosomal recessive retinitis pigmentosa-causing mutations in the Japanese patients.
Insulin receptor (IR), an integral membrane protein, directly phosphorylates the CNGA1 subunit of CNG channels that in turn affects the function of these channels negatively. CNGA1 is a direct substrate of IR.
Novel homozygous mutation R28X truncates CNGA1 very prematurely in patients with autosomal recessive retinitis pigmentosa.
isolated an endogenous transcript (anti-CNG1) that is antisense to CNG1 mRNA; data suggest the suppression of CNG(alpha)1 expression by anti-CNG1 may play an important role in neuronal functions, especially in synaptic plasticity and cortical development
The heteromeric cyclic nucleotide-gated channel adopts a 3A:1B stoichiometry
The autosomal recessive retinitis pigmentosa in this family is caused by a mutation in CNGA1 gene.
Expressed in a stage- and cell-specific manner in the rat testis.
These results suggest that restraining the A' helix to the plasma membrane potentiates CNGA1 channel opening.
Conformation changes of CNGA1 associated with its gating function are reported.
Data show that when Pro365 is replaced with a threonine in cyclic nucleotide gated channel alpha 1 (CNGA1), cesium Cs+ permeation is nearly abolished.
Stabilizing the C-helix of intact CNGA1 channels by metal binding to a pair of histidines promoted channel opening.
A ring of threonines in the inner vestibule of the pore of CNGA1 channels constitutes a binding site for permeating ions
Three CNGA1 subunits and a single CNGB1 subunit form the rod cyclic nucleotide-gated ion channels.
Existence of a strong coupling between the upper portion of the S6 helix provides a simple molecular mechanism for CNGA1 gating.
Data suggest that the native rod cyclic nucleotide-gated (CNG) channel is a tetramer composed of three A1 and one B1 subunit.
Data show that the cyclic nucleotide-gated (CNG) channel contains three CNGA1 subunits and only one CNGB1 subunit.
Structural models of the tetrameric cyclic nucleotide gated channel alpha 1 from bovine rod is presented.
In CNGA1 channels, pore gating is involved in the rate-limiting reactions determining the activation time course in the sequence of events between cGMP binding and pore opening.
These observations suggest that these effects are mediated by the formation of a disulfide bond (S-S) between F380C and the endogenous Cys-314 in the S5 segment.
analyze in detail the molecular mechanisms underlying Cd2+ inhibition and longer cross-linkers in mutant CNGA1 channels
detailed analysis of conformational changes of the S6 domain and C-linker during gating of CNGA1 channels
Numb protein interacts with Cnga1 in rod photoreceptor cilia to promote delivery of Cnga1.
that effective knockdown of GUCY2E and CNGA1 expression to counteract loss of PDE6 function may develop into a valuable approach for treating some patients with RP.
Interaction with auxiliary subunit tetratricopeptide repeat-containing Rab8b-interacting protein (TRIP8b) is a major mechanism underlying proper expression of hyperpolarization-activated cyclic nucleotide-gated (HCN) channels and Ih in vivo.
Grb14 is a normal physiological modulator of CNG channel function in vivo.
We demonstrate the association of photoreceptor CNG channels with membrane domains enriched in raft lipids and indicates, for the first time, that raft lipids modulate the plasma membrane localization and functional activity of photoreceptor CNG channels.
The protein encoded by this gene is involved in phototransduction. Along with another protein, the encoded protein forms a cGMP-gated cation channel in the plasma membrane, allowing depolarization of rod photoreceptors. This represents the last step in the phototransduction pathway. Defects in this gene are a cause of retinitis pigmentosa autosomal recessive (ARRP) disease. Two transcript variants encoding different isoforms have been found for this gene.
CNG channel alpha-1
, cGMP-gated cation channel alpha-1
, cyclic nucleotide-gated cation channel 1
, cyclic nucleotide-gated channel alpha-1
, cyclic nucleotide-gated channel, photoreceptor
, interleukin-1 homologue
, rod photoreceptor cGMP-gated channel subunit alpha
, cyclic nucleotide gated chanel (photoreceptor), cGMP gated 1, alpha
, cyclic nucleotide gated channel (photoreceptor), cGMP gated
, rod photoreceptor cGMP-gated channel alpha-subunit
, cyclic nucleotide gated channel alpha 1
, cGMP-gated cation channel alpha-1-like
, cyclic nucleotide gated channel, cGMP gated