ArticleThe Journal of biological chemistry2010
A functional kinase homology domain is essential for the activity of photoreceptor guanylate cyclase 1.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 23 citations in OpenAlex.
- Phosphorylation-Dependent Regulation of Guanylyl Cyclase (GC)-A and Other Membrane GC Receptors.Endocrine reviews · 2024Review
- Guanylyl cyclase-A phosphorylation decreases cardiac hypertrophy and improves systolic function in male, but not female, mice.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022Article
- Multilimbed membrane guanylate cyclase signaling system, evolutionary ladder.Frontiers in molecular neuroscience · 2022Review
- Vicinal glutamates are better phosphomimetics: Phosphorylation is required for allosteric activation of guanylyl cyclase-A.Frontiers in molecular neuroscience · 2022Article
- The pseudokinase domain in receptor guanylyl cyclases.Methods in enzymology · 2022Review
- Evolution of the calcium feedback steps of vertebrate phototransduction.Open biology · 2018Article
- Photoreceptor Guanylate Cyclase (Frontiers in molecular neuroscience · 2018Article
- Integrative Signaling Networks of Membrane Guanylate Cyclases: Biochemistry and Physiology.Frontiers in molecular neuroscience · 2016Review
- Retinal phototransduction.Neurosciences (Riyadh, Saudi Arabia) · 2014Review
- High density and ligand affinity confer ultrasensitive signal detection by a guanylyl cyclase chemoreceptor.The Journal of cell biology · 2014Article
- Guanylyl cyclase structure, function and regulation.Cellular signalling · 2011Review
- Targeting of mouse guanylate cyclase 1 (Gucy2e) to Xenopus laevis rod outer segments.Vision research · 2011Article
- Posttranslational modifications of the photoreceptor-specific ABC transporter ABCA4.Biochemistry · 2011Article
- Regulation and therapeutic targeting of peptide-activated receptor guanylyl cyclases.Pharmacology & therapeutics · 2011Review
- Mass spectrometric identification of phosphorylation sites in guanylyl cyclase A and B.Biochemistry · 2010Article
- Electrostatic compensation restores trafficking of the autosomal recessive retinitis pigmentosa E150K opsin mutant to the plasma membrane.The Journal of biological chemistry · 2010Article
- Functional and behavioral restoration of vision by gene therapy in the guanylate cyclase-1 (GC1) knockout mouse.PloS one · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Phototransduction is carried out by a signaling pathway that links photoactivation of visual pigments in retinal photoreceptor cells to a change in their membrane potential. Upon photoactivation, the second messenger of phototransduction, cyclic GMP, is rapidly degraded and must be replenished during the recovery phase of phototransduction by photoreceptor guanylate cyclases (GCs) GC1 (or GC-E) and GC2 (or GC-F) to maintain vision. Here, we present data that address the role of the GC kinase homology (KH) domain in cyclic GMP production by GC1, the major cyclase in photoreceptors. First, experiments were done to test which GC1 residues undergo phosphorylation and whether such phosphorylation affects cyclase activity. Using mass spectrometry, we showed that GC1 residues Ser-530, Ser-532, Ser-533, and Ser-538, located within the KH domain, undergo light- and signal transduction-independent phosphorylation in vivo. Mutations in the putative Mg(2+) binding site of the KH domain abolished phosphorylation, indicating that GC1 undergoes autophosphorylation. The dramatically reduced GC activity of these mutants suggests that a functional KH domain is essential for cyclic GMP production. However, evidence is presented that autophosphorylation does not regulate GC1 activity, in contrast to phosphorylation of other members of this cyclase family.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.