GDP stimulates the phosphorylation of a 36-kDa membrane protein in Dictyostelium discoideum.
Increasing effort is directed toward elucidating the mechanisms by which guanine nucleotide-binding proteins regulate specific cellular processes. A common feature of this class of proteins is that GTP induces a transition from an inactive to an active conformation. The latter is limited by the hydrolysis of GTP and the coincident production of GDP. Here we provide evidence that guanine nucleotides may regulate biological processes by inducing the phosphorylation of specific proteins. In particular, we report a GDP-dependent phosphorylation of p36, a 36-kDa protein of Dictyostelium discoideum plasma membranes.
Anschutz
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E. A. Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, MO 63104.
Howlet
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Klein
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D000227:Adenine Nucleotides / Q000494:pharmacology; D015153:Blotting, Western; D002462:Cell Membrane / Q000378:metabolism; D004023:Dictyostelium / Q000378:metabolism*; D005656:Fungal Proteins / Q000378:metabolism*; D019204:GTP-Binding Proteins / Q000378:metabolism; D006150:Guanine Nucleotides / Q000494:pharmacology*; D006153:Guanosine Diphosphate / Q000494:pharmacology*; D008565:Membrane Proteins / Q000378:metabolism*; D008970:Molecular Weight; D010749:Phosphoprotein Phosphatases / Q000378:metabolism; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation
D000227:Adenine Nucleotides; D005656:Fungal Proteins; D006150:Guanine Nucleotides; D008565:Membrane Proteins; D010750:Phosphoproteins; D006153:Guanosine Diphosphate; D010749:Phosphoprotein Phosphatases; D019204:GTP-Binding Proteins