ArticleThe Biochemical journal1997
G-protein betagamma subunits antagonize protein kinase C-dependent phosphorylation and inhibition of phospholipase C-beta1.
Article in The Biochemical journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 42 citations in OpenAlex.
- Signaling responses to pulsatile gonadotropin-releasing hormone in LbetaT2 gonadotrope cells.The Journal of biological chemistry · 2010Article
- A comprehensive pathway map of epidermal growth factor receptor signaling.Molecular systems biology · 2005Article
- Reciprocal modulation of phospholipase Cbeta isoforms: adaptation to chronic morphine.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Mechanisms of cross-talk between G-protein-coupled receptors resulting in enhanced release of intracellular Ca2+.The Biochemical journal · 2003Review
- A lobster phospholipase C-beta that associates with G-proteins in response to odorants.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1999Article
- Phosphorylation by protein kinase C decreases catalytic activity of avian phospholipase C-beta.The Biochemical journal · 1999Article
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
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Abstract
Protein kinase C (PKC) isoforms phosphorylated phospholipase C-beta1 (PLC-beta1) in vitro as follows: PKCalpha >> PKCepsilon; not PKCzeta. PLC-beta3 was not phosphorylated by PKCalpha. G-protein betagamma subunits inhibited the PKCalpha phosphorylation of PLC-beta1 in a concentration-dependent manner. Half-maximal inhibition occurred with 500 nM betagamma. G-protein betagamma subunits also antagonized the PKCalpha-mediated inhibition of PLC-beta1 enzymic activity. PKCalpha, in turn, inhibited the stimulation of PLC-beta1 activity by betagamma. There was little effect of PKCalpha on the stimulation of PLC-beta1 by alphaq/11-guanosine 5'[gamma-thio]triphosphate (GTP[S]). These findings demonstrate that G protein betagamma subunits antagonize PKCalpha regulation of PLC-beta1. Thus betagamma subunits might have a role in modulating the negative feedback regulation of this signalling system by PKC.
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