Interaction of nucleoside diphosphate kinase B with heterotrimeric G protein beta gamma dimers: consequences on G protein activation and stability
It is generally accepted that G protein coupled receptors (GPCR) activate heterotrimeric G proteins by inducing a GDP/GTP exchange at the G protein alpha subunit. In addition, the transfer of high energetic phosphate by nucleoside diphosphate kinase (NDPK) and/or the beta subunit of G proteins (G be...
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| Main Author: | |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
3 January 2007
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| In: |
Naunyn-Schmiedeberg's archives of pharmacology
Year: 2007, Volume: 374, Issue: 5/6, Pages: 373-383 |
| ISSN: | 1432-1912 |
| DOI: | 10.1007/s00210-006-0126-6 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1007/s00210-006-0126-6
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| Author Notes: | Thomas Wieland |
MARC
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| 520 | |a It is generally accepted that G protein coupled receptors (GPCR) activate heterotrimeric G proteins by inducing a GDP/GTP exchange at the G protein alpha subunit. In addition, the transfer of high energetic phosphate by nucleoside diphosphate kinase (NDPK) and/or the beta subunit of G proteins (G beta) can induce G protein activation. Recent evidence suggests that the NDPK isoform B (NDPK B) forms a complex with G beta gamma dimers. In this complex, NDPK B acts as a protein histidine kinase phosphorylating G beta at histidine residue 266 (His266). The high energetic phosphoamidate bond on His266 allows for a phosphate transfer specifically onto GDP and thus local formation of GTP, which binds to and thereby activates the respective G protein alpha subunit. Apparently, this process occurs independent of the classical GPCR-induced GDP/GTP exchange at least for members of the G(s) and G(i) subfamilies of heterotrimeric G proteins. By using a mutant of G beta(1) in which His266 was replaced by Leu, it was recently demonstrated that NDPK B/G beta gamma-mediated G(s) activation contributes by about 50% to basal cAMP formation and contractility in rat cardiac myocytes. Besides its apparent role in G protein activation, the complex formation of NDPK B with G beta gamma dimers might be essential for G protein stability. Depletion of either the NDPK B orthologue or G beta(1) isoforms in zebrafish embryos led to a similar phenotype displaying contractile dysfunction in the heart accompanied by a complete loss of heterotrimeric G protein expression. In conclusion, the interaction of NDKP B with G beta gamma dimers might play an important role in signal transduction, and alterations in this novel pathway might be of pathophysiological importance. | ||
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| 650 | 4 | |a binding regulatory proteins | |
| 650 | 4 | |a energy phosphate transfer | |
| 650 | 4 | |a G beta gamma dimers | |
| 650 | 4 | |a heart-failure | |
| 650 | 4 | |a heterotrimeric G proteins | |
| 650 | 4 | |a histidine phosphatase | |
| 650 | 4 | |a human-platelet membranes | |
| 650 | 4 | |a independent activation | |
| 650 | 4 | |a nm23-H2 | |
| 650 | 4 | |a nucleoside diphosphate kinase | |
| 650 | 4 | |a nucleotide exchange | |
| 650 | 4 | |a phosphotransfer reactions | |
| 650 | 4 | |a signal transduction | |
| 650 | 4 | |a signal-transduction | |
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