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J Biol Chem, Vol. 274, Issue 30, 21257-21264, July 23, 1999

A Novel Serine Kinase with Specificity for 3-Subunits Is Tightly Associated with GABA_A Receptors

From the Department of Pharmacology, University of Bern, CH-3010 Bern, Switzerland and the ^§ Section of Biochemical Psychiatry, University Clinic for Psychiatry, A-1090 Vienna, Austria

Tuning of -aminobutyric acid type A (GABA_A) receptor function via phosphorylation of the receptor potentially allows neurons to modulate their inhibitory input. Several kinases, both of the serine-threonine kinase and the tyrosine kinase families, have been proposed as candidates for such a modulatory role in vivo. However, no GABA_A receptor-phosphorylating kinase physically associated with the receptor has been identified so far on a molecular level. In this study, we demonstrate a GABA_A receptor-associated protein serine kinase phosphorylating specifically 3-subunits of native GABA_A receptors. The characteristics of this novel kinase clearly distinguish it from enzymatic activities that have been shown so far to phosphorylate the GABA_A receptor. We putatively identify this protein kinase as the previously described GTAP34 (GABA_A receptor-tubulin complex-associated protein of molecular mass 34 kDa). Using expressed recombinant fusion proteins, we identify serine 408 as a major target of the phosphorylation reaction, whereas serine 407 is not phosphorylated. This demonstrates the high specificity of the kinase. Phosphorylation of serine 408 is known to result in a decreased receptor function. The direct association of this kinase with the receptor indicates an important physiological role.

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