ArticleProceedings of the National Academy of Sciences of the United States of America1988
An unusual protein kinase phosphorylates the chemotactic receptor of Dictyostelium discoideum.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1988. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 28 citations in OpenAlex.
- Developmental decisions in Dictyostelium discoideum.Microbiological reviews · 1994Review
- Regulatory role of GDP in the phosphoenzyme formation of guanine nucleotide: specific forms of succinyl coenzyme A synthetase.Journal of protein chemistry · 1994Article
- Evidence for allosteric regulation of succinyl-CoA synthetase.The Biochemical journal · 1993Article
- Cloning and expression of GRK5: a member of the G protein-coupled receptor kinase family.Proceedings of the National Academy of Sciences of the United States of America · 1993Article
- Pulsatile signaling in intercellular communication. Periodic stimuli are more efficient than random or chaotic signals in a model based on receptor desensitization.Biophysical journal · 1992Article
- The receptor kinase family: primary structure of rhodopsin kinase reveals similarities to the beta-adrenergic receptor kinase.Proceedings of the National Academy of Sciences of the United States of America · 1991Article
- Dual role of GDP in the regulation of the levels of p36 phosphorylation in Dictyostelium discoideum.Journal of protein chemistry · 1991Article
- Identification of a protein kinase multigene family of Dictyostelium discoideum: molecular cloning and expression of a cDNA encoding a developmentally regulated protein kinase.Proceedings of the National Academy of Sciences of the United States of America · 1991Article
- Properties of CAR-kinase: the enzyme that phosphorylates the cAMP chemotactic receptor of D. discoideum.Journal of protein chemistry · 1990Article
- Regulation of the two forms of glycogen phosphorylase by cAMP and its analogs in Dictyostelium discoideum.Molecular and cellular biochemistry · 1990Article
- Characterization of a GDP-sensitive phosphorylation in plasma membranes of D. discoideum.Journal of protein chemistry · 1990Article
- A rapid posttranslational myristylation of a 68-kD protein in D. discoideum.The Journal of cell biology · 1990Article
- GDP stimulates the phosphorylation of a 36-kDa membrane protein in Dictyostelium discoideum.Proceedings of the National Academy of Sciences of the United States of America · 1989Article
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2 authors at 1 institution in 1 country.
Funding
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Abstract
We report the cAMP-dependent phosphorylation of the chemotactic receptor of Dictyostelium discoideum in partially purified plasma membranes. The protein kinase responsible for receptor phosphorylation is associated with this fraction and preferentially phosphorylates the ligand-occupied form of the receptor. 8-Azido[32P]cAMP labeling of the cell surface has shown that the cAMP receptor exists in two forms. A 45-kDa protein is predominant on unstimulated cells. cAMP stimulation results in an increased receptor phosphorylation such that the receptor migrates on NaDodSO4/PAGE as a 47-kDa protein. Phosphorylation of the chemotactic receptor is not detected in membrane preparations unless cAMP is added to the incubation mixture. Only under those conditions is the phosphorylated 47-kDa form observed. The requirement for cAMP reflects the fact that the kinase involved preferentially uses the ligand-occupied receptor as a substrate. In vitro phosphorylation of the receptor does not involve tyrosine residues. The enzyme does not appear to be a cAMP- or cGMP-dependent protein kinase nor is it sensitive to guanine nucleotides, Ca2+/calmodulin, Ca2+/phospholipid, or EGTA. Similarities with the beta-adrenergic receptor protein kinase are discussed.
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