Abstract
Transmembrane signal transduction was investigated in four Dictyostelium discoideum mutants that belong to the fgd A complementation group. The results show the following. (a) Cell surface cAMP receptors are present in fgd A mutants, but cAMP does not induce any of the intracellular responses, including the activation of adenylate or guanylate cyclase and chemotaxis. (b) cAMP induces down-regulation and the covalent modification (presumably phosphorylation) of the cAMP receptor. (c) The inhibitory effects of GTP gamma S and GDP beta S on cAMP binding are reduced; the stimulatory effect of cAMP on GTP gamma S binding is lost in fgd A mutants. (d) Basal high-affinity GTPase activity is reduced 40% and the stimulatory effect of cAMP is decreased from 40% in wild type to 30% in fgd A. (e) GTP-mediated stimulation and inhibition of adenylate cyclase is normal in mutant membranes. The results suggest a defective interaction between cell surface cAMP receptors and a specific G-protein in fgd A mutants. This interaction appears to be essential for nearly all signal transduction pathways in Dictyostelium discoideum.
MeSH Terms
Adenylyl Cyclases/metabolism
Binding, Competitive
Chemotaxis
Cyclic AMP/metabolism
Dictyostelium/genetics,metabolism
Electrophoresis, Polyacrylamide Gel
GTP Phosphohydrolases/metabolism
GTP-Binding Proteins/genetics,metabolism
Guanosine 5'-O-(3-Thiotriphosphate)
Guanosine Diphosphate/analogs & derivatives,metabolism
Guanosine Triphosphate/analogs & derivatives,metabolism
Immunoassay
Kinetics
Mutation
Receptors, Cyclic AMP/genetics,metabolism
Thionucleotides/metabolism
Chemicals
Receptors, Cyclic AMP
Thionucleotides
Guanosine Diphosphate
Guanosine 5'-O-(3-Thiotriphosphate)
guanosine 5'-O-(2-thiodiphosphate)
Guanosine Triphosphate
Cyclic AMP
GTP Phosphohydrolases
GTP-Binding Proteins
Adenylyl Cyclases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Kesbeke F
Department of Biology, University of Leiden, The Netherlands.
Snaar-Jagalska B E
Van Haastert P J
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