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Gz(rat):PKC(cow) dissociates to give phosphorylated G alpha (z)
Stable Identifier
R-NUL-8982712
Type
Reaction [dissociation]
Species
Bos taurus
Compartment
plasma membrane
ReviewStatus
5/5
General
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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 phosphorylation at Ser-27 (Lounsbury et al. 1993). Subsequently, phosphorylated G alpha z dissociates from the complex. 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
Participants
Input
p(S27)-G-alpha(z):GTP:PKC [plasma membrane]
(Rattus norvegicus)
Output
p(S27)-G protein alpha (z):GTP [plasma membrane]
(Rattus norvegicus)
Protein kinase C conventional and novel isoforms [plasma membrane]
(Bos taurus)
Orthologous Events
G-alpha(z):PKC dissociates to give phosphorylated G alpha (z) (Homo sapiens)
Authored
Jupe, S (2010-05-18)
Reviewed
D'Eustachio, P (2010-05-26)
Created
Varusai, TM (2017-03-22)
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