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Activation of G‐proteins by receptor‐stimulated nucleoside diphosphate kinase in Dictyostelium.
Author(s) -
Bominaar A.A.,
Molijn A.C.,
Pestel M.,
Veron M.,
Van Haastert P.J.
Publication year - 1993
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1993.tb05881.x
Subject(s) - biology , nucleoside diphosphate kinase , dictyostelium , biochemistry , kinase , receptor , nucleoside , microbiology and biotechnology , gene
Recently, interest in the enzyme nucleoside diphosphate kinase (EC2.7.4.6) has increased as a result of its possible involvement in cell proliferation and development. Since NDP kinase is one of the major sources of GTP in cells, it has been suggested that the effects of an altered NDP kinase activity on cellular processes might be the result of altered transmembrane signal transduction via guanine nucleotide‐binding proteins (G‐proteins). In the cellular slime mould Dictyostelium discoideum, extracellular cAMP induces an increase of phospholipase C activity via a surface cAMP receptor and G‐proteins. In this paper it is demonstrated that part of the cellular NDP kinase is associated with the membrane and stimulated by cell surface cAMP receptors. The GTP produced by the action of NDP kinase is capable of activating G‐proteins as monitored by altered G‐protein‐receptor interaction and the activation of the effector enzyme phospholipase C. Furthermore, specific monoclonal antibodies inhibit the effect of NDP kinase on G‐protein activation. These results suggest that receptor‐stimulated NDP kinase contributes to the mediation of hormone action by producing GTP for the activation of GTP‐binding proteins.