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Vol. 57, Issue 5, 847-856, May 2000
-Aminobutyric Acid
(GABA)A and GABAC Receptors by Protein Kinase C
Department of Neurobiology, University of Alabama School of
Medicine, Birmingham, Alabama
Activation of protein kinase C (PKC) by phorbol 12-myristate 13-acetate
induced a continuous decrease in the 
-aminobutyric acid
(GABA)-activated current amplitude from recombinant GABA receptors
(formed by 
1 or 
subunits) expressed in
Xenopus oocytes. This decline was due to internalization
of receptors from the plasma membrane as confirmed by a decrease in
surface fluorescence with green fluorescence protein-tagged receptors as well as a concomitant decrease in surface [3H]GABA
binding. PMA specifically caused internalization of GABA receptors, but
not neuronal acetylcholine receptors (7 or
42), indicating the internalization was
not a general, nonspecific phenomenon. Mutation of 1 PKC
phosphorylation sites, identified by in vitro phosphorylation, did not
prevent GABA receptor internalization, nor did coexpression of the 1
M3-M4 intracellular loop along with 1 GABA receptors. It is likely
that PKC-mediated phosphorylation of other proteins, rather than 1
itself, was required for the internalization. Both 1 and
receptors did not degrade after phorbol 12-myristate 13-acetate-induced
internalization, but returned to the membrane surface within 24 h.
These data suggest internalized receptors can exist in an intracellular
compartment that can be delivered back to the plasma membrane. Thus, by
regulating GABA receptor surface expression, PKC may play a key role in
the regulation of GABA-mediated inhibition.
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