The protein phosphatase inhibitor okadaic acid was used to investigate the role of protein phosphatases in regulating the release of amino acids from synaptosomes. Okadaic acid increased the basal release of the amino acids glutamate, aspartate and GABA. The effect was specific in that taurine was not released by either KCl or okadaic acid and there was no synaptosomal lysis or change in ATP/ADP ratios in the presence of okadaic acid. The okadaic acid-stimulated release of amino acids was, however, only a small proportion of that produced by KCl depolarisation. Since okadaic acid raised synaptosomal protein phosphorylation levels to those equivalent to that produced by KCl depolarisation, it is unlikely therefore that there is a direct causal relationship between protein phosphorylation and the release of amino acids. Nevertheless, that release of amino acids from synaptosomes can be elevated under basal conditions by okadaic acid treatment does suggest that okadaic acid-sensitive protein phosphatases have a modulatory role in this process.