1. Protein kinase C regulates the interaction between a GABA transporter and syntaxin 1A.
- Author
-
Beckman ML, Bernstein EM, and Quick MW
- Subjects
- Animals, Botulinum Toxins pharmacology, Carrier Proteins genetics, Carrier Proteins metabolism, GABA Plasma Membrane Transport Proteins, Membrane Proteins genetics, Membrane Proteins metabolism, Mutation physiology, PC12 Cells drug effects, PC12 Cells metabolism, Rats, Sodium Channels physiology, Syntaxin 1, Antigens, Surface physiology, Carrier Proteins physiology, Membrane Proteins physiology, Membrane Transport Proteins, Nerve Tissue Proteins physiology, Organic Anion Transporters, Protein Kinase C physiology
- Abstract
Syntaxin 1A inhibits GABA uptake of an endogenous GABA transporter in neuronal cultures from rat hippocampus and in reconstitution systems expressing the cloned rat brain GABA transporter GAT1. Evidence of interactions between syntaxin 1A and GAT1 comes from three experimental approaches: botulinum toxin cleavage of syntaxin 1A, syntaxin 1A antisense treatments, and coimmunoprecipitation of a complex containing GAT1 and syntaxin 1A. Protein kinase C (PKC), shown previously to modulate GABA transporter function, exerts its modulatory effects by regulating the availability of syntaxin 1A to interact with the transporter, and a transporter mutant that fails to interact with syntaxin 1A is not regulated by PKC. These results suggest a new target for regulation by syntaxin 1A and a novel mechanism for controlling the machinery involved in both neurotransmitter release and reuptake.
- Published
- 1998