Presynaptic membrane protein phosphorylation modulates the release of GABA from preloaded synaptosomes.
Incubation of rat cortical synaptosomes in the presence of 1 mM ATP markedly reduced Ca2+-dependent K+-induced release of preloaded 3H-GABA. This effect is probably dependent on phosphorylation of presynaptic membrane proteins. By contrast, the uptake of 3H-GABA by the nerve endings was not significantly affected by phosphorylation. These data suggest that membrane protein phosphorylation and dephosphorylation may form a mechanism for the presynaptic control of transmitter release.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002540:Cerebral Cortex / Q000378:metabolism*; D007700:Kinetics; D008297:Male; D008565:Membrane Proteins / Q000378:metabolism; D010766:Phosphorylation; D011188:Potassium / Q000494:pharmacology; D051381:Rats; D013574:Synaptosomes / Q000187:drug effects / Q000378:metabolism*; D005680:gamma-Aminobutyric Acid / Q000378:metabolism*
D008565:Membrane Proteins; D005680:gamma-Aminobutyric Acid; D000255:Adenosine Triphosphate; D011188:Potassium; D002118:Calcium