Activation of heterotrimeric G proteins by a high energy phosphate transfer via nucleoside diphosphate kinase (NDPK) B and Gβ subunits: specific activation of Gsα by an NDPK B·Gβγ complex in H10 cells

Formation of GTP by nucleoside diphosphate kinase (NDPK) can contribute to G protein activation in vitro. To study the effect of NDPK on G protein activity in living cells, the NDPK isoforms A and B were stably expressed in H10 cells, a cell line derived from neonatal rat cardiomyocytes. Overexpress...

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Hauptverfasser: Hippe, Hans-Jörg (VerfasserIn) , Lutz, Susanne (VerfasserIn) , Cuello, Friederike (VerfasserIn) , Knorr, Katrin (VerfasserIn) , Vogt, Achim (VerfasserIn) , Jakobs, Karl-Heinz (VerfasserIn) , Wieland, Thomas (VerfasserIn) , Niroomand, Feraydoon (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 2003
In: The journal of biological chemistry
Year: 2003, Jahrgang: 278, Heft: 9, Pages: 7227-7233
ISSN:1083-351X
DOI:10.1074/jbc.M210305200
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1074/jbc.M210305200
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Verfasserangaben:Hans-Joerg Hippe, Susanne Lutz, Friederike Cuello, Katrin Knorr, Achim Vogt, Karl H. Jakobs, Thomas Wieland, and Feraydoon Niroomand

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245 1 0 |a Activation of heterotrimeric G proteins by a high energy phosphate transfer via nucleoside diphosphate kinase (NDPK) B and Gβ subunits  |b specific activation of Gsα by an NDPK B·Gβγ complex in H10 cells  |c Hans-Joerg Hippe, Susanne Lutz, Friederike Cuello, Katrin Knorr, Achim Vogt, Karl H. Jakobs, Thomas Wieland, and Feraydoon Niroomand 
246 3 3 |a Activation of heterotrimeric G proteins by a high energy phosphate transfer via nucleoside diphosphate kinase (NDPK) B and G beta subunits$dspecific activation of G s alpha by an NDPK B·G beta gamma complex in H10 cells 
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336 |a Text  |b txt  |2 rdacontent 
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500 |a Im Titel ist das "s" bei Gsα tiefgestellt 
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520 |a Formation of GTP by nucleoside diphosphate kinase (NDPK) can contribute to G protein activation in vitro. To study the effect of NDPK on G protein activity in living cells, the NDPK isoforms A and B were stably expressed in H10 cells, a cell line derived from neonatal rat cardiomyocytes. Overexpression of either NDPK isoform had no effect on cellular GTP and ATP levels, basal cAMP levels, basal adenylyl cyclase activity, and the expression of G(s)alpha and G(i)alpha proteins. However, co-expression of G(s)alpha led to an increase in cAMP synthesis that was largely enhanced by the expression of NDPK B, but not NDPK A, and that was confirmed by direct measurement of adenylyl cyclase activity. Cells expressing an inactive NDPK B mutant (H118N) exhibited a decreased cAMP formation in response to G(s)alpha. Co-immunoprecipitation studies demonstrated a complex formation of the NDPK with Gbetagamma dimers. The overexpression of NDPK B, but not its inactive mutant or NDPK A, increased the phosphorylation of Gbeta subunits. In summary, our data demonstrate a specific NDPK B-mediated activation of a G protein in intact cells, which is apparently caused by formation of NDPK B.Gbetagamma complexes and which appears to contribute to the receptor-independent activation of heterotrimeric G proteins. 
650 4 |a Adenosine Triphosphate 
650 4 |a Adenoviridae 
650 4 |a Animals 
650 4 |a Animals, Newborn 
650 4 |a Blotting, Western 
650 4 |a Catalysis 
650 4 |a Cell Membrane 
650 4 |a Cloning, Molecular 
650 4 |a Cyclic AMP 
650 4 |a Dimerization 
650 4 |a DNA, Complementary 
650 4 |a Dose-Response Relationship, Drug 
650 4 |a GTP-Binding Proteins 
650 4 |a Guanosine Triphosphate 
650 4 |a Humans 
650 4 |a Models, Biological 
650 4 |a Mutation 
650 4 |a Myocardium 
650 4 |a Nucleoside-Diphosphate Kinase 
650 4 |a Phosphates 
650 4 |a Phosphorylation 
650 4 |a Precipitin Tests 
650 4 |a Protein Binding 
650 4 |a Protein Isoforms 
650 4 |a Protein Structure, Tertiary 
650 4 |a Rats 
650 4 |a Temperature 
650 4 |a Time Factors 
650 4 |a Transfection 
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