Phosphorylation of gamma-aminobutyrate (GABA)/benzodiazepine receptors by cyclic AMP-dependent protein kinase.
Preparations of gamma-aminobutyrate (GABA)/benzodiazepine receptor from pig cerebral cortex are composed of three major bands of polypeptides (51, 55 and 57 kDa) which are purified in a ratio of approx. 2:1:1 respectively. Treatment of purified receptor preparations with cyclic AMP-dependent protein kinase resulted in major incorporation of 32P into the 55 kDa band only. The maximum incorporation achieved was 0.6 mol of 32P/mol of 55 kDa polypeptide. The phosphorylated receptor subunit (beta-subunit) displays the same apparent Mr as a band labelled irreversibly with the GABA receptor agonist [3H]muscimol. The two nonphosphorylated subunit polypeptides (51 and 57 kDa) are each labelled irreversibly with [3H]flunitrazepam and are recognized by anti-peptide antibodies specific for alpha-subunits.
Kirkness
E F
EF
Department of Biochemistry, University of Leeds, U.K.
Bovenkerk
C F
CF
Ueda
T
T
Turner
A J
AJ
D000818:Animals; D002540:Cerebral Cortex / Q000378:metabolism; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D011963:Receptors, GABA-A / Q000378:metabolism*; D013552:Swine
D011963:Receptors, GABA-A; D011494:Protein Kinases