High energy phosphate transfer by NDPK B/G β γ complexes - an alternative signaling pathway involved in the regulation of basal cAMP production
The activation of heterotrimeric G proteins induced by G protein coupled receptors (GPCR) is generally believed to occur by a GDP/GTP exchange at the G protein alpha -subunit. Nevertheless, nucleoside diphosphate kinase (NDPK) and the beta-subunit of G proteins (Gbeta) participate in G protein activ...
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| Main Authors: | , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
7 September 2006
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| In: |
Journal of bioenergetics and biomembranes
Year: 2006, Volume: 38, Issue: 3-4, Pages: 197-203 |
| ISSN: | 1573-6881 |
| DOI: | 10.1007/s10863-006-9035-0 |
| Online Access: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1007/s10863-006-9035-0
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| Author Notes: | Hans-Joerg Hippe, Thomas Wieland |
| Summary: | The activation of heterotrimeric G proteins induced by G protein coupled receptors (GPCR) is generally believed to occur by a GDP/GTP exchange at the G protein alpha -subunit. Nevertheless, nucleoside diphosphate kinase (NDPK) and the beta-subunit of G proteins (Gbeta) participate in G protein activation by phosphate transfer reactions leading to the formation of GTP from GDP. Recent work elucidated the role of these reactions. Apparently, the NDPK isoform B (NDPK B) forms a complex with Gbetagamma dimers in which NDPK B acts as a histidine kinase phosphorylating Gbeta at His266. Out of this high energetic phosphoamidate bond the phosphate can be transferred specifically onto GDP. The formed GTP binds to the G protein alpha-subunit and thus activates the respective G protein. Evidence is presented, that this process occurs independent of the classical GPCR-induced GTP/GTP exchange und thus contributes, e.g. to the regulation of basal cAMP synthesis in cells. |
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| Item Description: | Gesehen am 31.03.2022 |
| Physical Description: | Online Resource |
| ISSN: | 1573-6881 |
| DOI: | 10.1007/s10863-006-9035-0 |