PKC phosphorylates G alpha (z)

Stable Identifier
R-HSA-751040
Type
Reaction [transition]
Species
Homo sapiens
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G alpha z (Lounsbury et al. 1991) and G alpha 12 (Kozasa & Gilman, 1996) are excellent in vitro substrates for all three subtypes of protein kinase C (PKC). Activation of PKC in intact platelets by agents such as thrombin, thromboxane A2 (TXA2) analogues and phorbol esters leads to rapid and near-stoichiometric phosphorylation of G alpha z (Carlson et al. 1989). The primary phosphorylation site is Ser-27 (Lounsbury et al. 1993). This phosphorylation blocks the interaction of G alpha z with Gbeta:gamma suggesting that it is a regulatory mechanism for attenuating signalling by preventing subunit reassociation.

Literature References
PubMed ID Title Journal Year
7559455 Phosphorylation of Gz alpha by protein kinase C blocks interaction with the beta gamma complex

Fields, TA, Casey, PJ

J. Biol. Chem. 1995
1939224 Phosphorylation of Gz in human platelets. Selectivity and site of modification

Lounsbury, KM, Casey, PJ, Brass, LF, Manning, DR

J Biol Chem 1991
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Catalyst Activity
Title
protein kinase C activity of G-alpha(z):GTP:PKC [plasma membrane]
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