Reactome | PKC binds active G alpha (z)

PKC binds active G alpha (z)

Stable Identifier

R-HSA-8982703

Type

Reaction [binding]

Species

Homo sapiens

Compartment

plasma membrane

ReviewStatus

5/5

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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). PKC can bind to G alpha z and facilitate its phosphorylation at 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, Manning, DR, Casey, PJ, Brass, LF	J Biol Chem	1991
7559455	Phosphorylation of Gz alpha by protein kinase C blocks interaction with the beta gamma complex Casey, PJ, Fields, TA	J. Biol. Chem.	1995