TY - JOUR
T1 - Protein kinase C phosphorylates the inhibitory guanine‐nucleotide‐binding regulatory component and apparently suppresses its function in hormonal inhibition of adenylate cyclase
AU - Katada, T.
AU - Gilman, A. G.
AU - Watanabe, Y.
AU - Bauer, S.
AU - Jakobs, K. H.
N1 - Copyright:
Copyright 2016 Elsevier B.V., All rights reserved.
PY - 1985/9
Y1 - 1985/9
N2 - Human platlet membrane proteins were phosphorylated by exogenous, partially purified Ca2+‐activated phospholipid‐dependent protein kinase (protein kinase C. the phosphorylation of one of the major substrates fro protein kinase C (Mr= 41000) wa specifically suppressed by the β subunit of the inhibitory guaninenucleotide‐binding regulatory component (G1, Ni) of adenylate cyclase. The free α subunit of Gi (Mr= 41000) also served as an excellent substrate for the kinase (<0.5 mol phosphate incorporated per mol of subunit), but the Gi oligomer (α·β·γ) did not. Treatment of cyc‐ S49 lymphoma cells, which are dificient in Gs/Ns(the stimulatory component) but contain functional Gi/Ns, with the phorbol ester, 12‐O‐tetradecanoylophorbol 13‐acetate, a potent activator of protein kinase C, did not alter stimulation of adenylate cyclase catalystic activity by forskolin, whereas the Gi/Ni‐mediated inhibition of the cyclase by the hormone, somatostatin, was impaired in these membranes. The results suggest that the α subunit of the inhibitory guanine‐nucleotide‐binding regulatory component of adenylate cyclase may be a physiological substrate for protein kinase C and that the function of the component in transducing inhibitory hormonal signals to adenylate cyclase is altered by its phosphorylation.
AB - Human platlet membrane proteins were phosphorylated by exogenous, partially purified Ca2+‐activated phospholipid‐dependent protein kinase (protein kinase C. the phosphorylation of one of the major substrates fro protein kinase C (Mr= 41000) wa specifically suppressed by the β subunit of the inhibitory guaninenucleotide‐binding regulatory component (G1, Ni) of adenylate cyclase. The free α subunit of Gi (Mr= 41000) also served as an excellent substrate for the kinase (<0.5 mol phosphate incorporated per mol of subunit), but the Gi oligomer (α·β·γ) did not. Treatment of cyc‐ S49 lymphoma cells, which are dificient in Gs/Ns(the stimulatory component) but contain functional Gi/Ns, with the phorbol ester, 12‐O‐tetradecanoylophorbol 13‐acetate, a potent activator of protein kinase C, did not alter stimulation of adenylate cyclase catalystic activity by forskolin, whereas the Gi/Ni‐mediated inhibition of the cyclase by the hormone, somatostatin, was impaired in these membranes. The results suggest that the α subunit of the inhibitory guanine‐nucleotide‐binding regulatory component of adenylate cyclase may be a physiological substrate for protein kinase C and that the function of the component in transducing inhibitory hormonal signals to adenylate cyclase is altered by its phosphorylation.
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U2 - 10.1111/j.1432-1033.1985.tb09120.x
DO - 10.1111/j.1432-1033.1985.tb09120.x
M3 - Article
C2 - 3161729
AN - SCOPUS:0022357080
SN - 0014-2956
VL - 151
SP - 431
EP - 437
JO - European Journal of Biochemistry
JF - European Journal of Biochemistry
IS - 2
ER -