PKC phosphorylates G alpha (z)

Stable Identifier
R-HSA-751040
Type
Reaction [transition]
Species
Homo sapiens
Compartment
plasma membrane, cytosol
ReviewStatus
5/5
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PKC phosphorylates G alpha (z)
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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
1939224 Phosphorylation of Gz in human platelets. Selectivity and site of modification

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

J Biol Chem 1991
7559455 Phosphorylation of Gz alpha by protein kinase C blocks interaction with the beta gamma complex

Fields, TA, Casey, PJ

J. Biol. Chem. 1995
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Catalyst Activity

diacylglycerol-dependent serine/threonine kinase activity of G-alpha(z):GTP:PKC [plasma membrane]

Physical Entity
G-alpha(z):GTP:PKC [plasma membrane] (Homo sapiens)
Activity
diacylglycerol-dependent serine/threonine kinase activity (GO:0004697)
Inferred From
PKC (cow) phosphorylates G alpha z (rat) (Bos taurus)
Authored
Jupe, S  (2010-05-18)
Reviewed
D'Eustachio, P  (2010-05-22)
Created
Jupe, S  (2010-05-19)
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