G-protein betagamma subunits antagonize protein kinase C-dependent phosphorylation and inhibition of phospholipase C-beta1.

I. Litosch

Research output: Contribution to journalArticle

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.

Original languageEnglish
JournalThe Biochemical journal
Volume326
StatePublished - Sep 15 1997
Externally publishedYes

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Phospholipase C beta
Phosphorylation
Protein Subunits
GTP-Binding Proteins
Protein Kinase C
Guanosine 5'-O-(3-Thiotriphosphate)
Guanosine
Guanosine Triphosphate
Protein Isoforms
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ASJC Scopus subject areas

  • Biochemistry

Cite this

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title = "G-protein betagamma subunits antagonize protein kinase C-dependent phosphorylation and inhibition of phospholipase C-beta1.",
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.",
author = "I. Litosch",
year = "1997",
month = "9",
day = "15",
language = "English",
volume = "326",
journal = "Biochemical Journal",
issn = "0264-6021",
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T1 - G-protein betagamma subunits antagonize protein kinase C-dependent phosphorylation and inhibition of phospholipase C-beta1.

AU - Litosch, I.

PY - 1997/9/15

Y1 - 1997/9/15

N2 - 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.

AB - 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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