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Presynaptic Membrane Protein Phosphorylation Modulates the Release of GABA from Preloaded Synaptosomes
Author(s) -
Brennan M. J. W.,
Cantrill R. C.
Publication year - 1980
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1980.tb06295.x
Subject(s) - phosphorylation , dephosphorylation , synaptosome , protein phosphorylation , free nerve ending , chemistry , biophysics , membrane , incubation , microbiology and biotechnology , biochemistry , biology , endocrinology , phosphatase , protein kinase a
Incubation of rat cortical synaptosomes in the presence of 1 mM ATP markedly reduced Ca 2+ ‐dependent K + ‐induced release of preloaded 3 H‐GABA. This effect is probably dependent on phosphorylation of presynaptic membrane proteins. By contrast, the uptake of 3 H‐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.