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Status: Bibliographieeintrag

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Verfasst von:Hippe, Hans-Jörg [VerfasserIn]   i
 Lutz, Susanne [VerfasserIn]   i
 Cuello, Friederike [VerfasserIn]   i
 Knorr, Katrin [VerfasserIn]   i
 Vogt, Achim [VerfasserIn]   i
 Jakobs, Karl-Heinz [VerfasserIn]   i
 Wieland, Thomas [VerfasserIn]   i
 Niroomand, Feraydoon [VerfasserIn]   i
Titel:Activation of heterotrimeric G proteins by a high energy phosphate transfer via nucleoside diphosphate kinase (NDPK) B and Gβ subunits
Titelzusatz:specific activation of Gsα by an NDPK B·Gβγ complex in H10 cells
Verf.angabe:Hans-Joerg Hippe, Susanne Lutz, Friederike Cuello, Katrin Knorr, Achim Vogt, Karl H. Jakobs, Thomas Wieland, and Feraydoon Niroomand
Jahr:2003
Umfang:7 S.
Fussnoten:Im Titel ist das "s" bei Gsα tiefgestellt ; Available online 16 December 2002, Version of Record 4 January 2021 ; Gesehen am 07.04.2022
Titel Quelle:Enthalten in: The journal of biological chemistry
Ort Quelle:Bethesda, Md. : ASBMB Publications, 1905
Jahr Quelle:2003
Band/Heft Quelle:278(2003), 9, Seite 7227-7233
ISSN Quelle:1083-351X
Abstract: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.
DOI:doi:10.1074/jbc.M210305200
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Volltext: https://doi.org/10.1074/jbc.M210305200
 DOI: https://doi.org/10.1074/jbc.M210305200
Datenträger:Online-Ressource
Sprache:eng
Sach-SW:Adenosine Triphosphate
 Adenoviridae
 Animals
 Animals, Newborn
 Blotting, Western
 Catalysis
 Cell Membrane
 Cloning, Molecular
 Cyclic AMP
 Dimerization
 DNA, Complementary
 Dose-Response Relationship, Drug
 GTP-Binding Proteins
 Guanosine Triphosphate
 Humans
 Models, Biological
 Mutation
 Myocardium
 Nucleoside-Diphosphate Kinase
 Phosphates
 Phosphorylation
 Precipitin Tests
 Protein Binding
 Protein Isoforms
 Protein Structure, Tertiary
 Rats
 Temperature
 Time Factors
 Transfection
K10plus-PPN:1798098687
Verknüpfungen:→ Zeitschrift

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