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Originally published In Press as doi:10.1074/jbc.M011549200 on May 14, 2001

J. Biol. Chem., Vol. 276, Issue 30, 28281-28290, July 27, 2001
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The Chaperone Protein 14-3-3eta Interacts with the Nicotinic Acetylcholine Receptor alpha 4 Subunit
EVIDENCE FOR A DYNAMIC ROLE IN SUBUNIT STABILIZATION*

Elisabeth M. JeanclosDagger , Lin LinDagger , Magdalen W. Treuil§, Jayaraman Rao§, Mark A. DeCosterDagger , and Rene AnandDagger §||

From the Dagger  Neuroscience Center of Excellence and § Department of Neurology, Louisiana State University Health Sciences Center, New Orleans, Louisiana 70112

By using the large cytoplasmic domain of the nicotinic acetylcholine receptor (AChR) alpha 4 subunit as a bait in the yeast two-hybrid system, we isolated the first cytosolic protein, 14-3-3eta , known to interact directly with neuronal AChRs. 14-3-3eta is a member of a family of proteins that function as regulatory or chaperone/ scaffolding/adaptor proteins. 14-3-3eta interacted with the recombinant alpha 4 subunit alone in tsA 201 cells following activation of cAMP-dependent protein kinase by forskolin. The interaction of 14-3-3eta with recombinant alpha 4 subunits was abolished when serine 441 of the alpha 4 subunit was mutated to alanine (alpha 4S441A). The surface levels of recombinant wild-type alpha 4beta 2 AChRs were ~2-fold higher than those of mutant alpha 4S441Abeta 2 AChRs. The interaction significantly increased the steady state levels of the alpha 4 subunit and alpha 4beta 2 AChRs but not that of the mutant alpha 4S441A subunit or mutant alpha 4S441Abeta 2 AChRs. The EC50 values for activation by acetylcholine were not significantly different for alpha 4beta 2 AChRs and alpha 4S441Abeta 2 AChRs coexpressed with 14-3-3eta in oocytes following treatment with forskolin. 14-3-3 coimmunopurified with native alpha 4 AChRs from brain. These results support a role for 14-3-3 in dynamically regulating the expression levels of alpha 4beta 2 AChRs through its interaction with the alpha 4 subunit.

* This work was supported in part by National Institutes of Health Grant NS33625 and generous start-up funds from the Louisiana State University Health Sciences Neuroscience Center.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Supported by funds from the Louisiana State University Health Sciences Parkinson's Center.

|| To whom correspondence should be addressed: Neuroscience Center of Excellence and Dept. of Neurology, 2020 Gravier St., Ste. D, Louisiana State University Health Sciences Center, New Orleans, LA 70112. Tel.: 504-599-0847; Fax: 504-599-0891; E-mail: ranand@lsuhsc.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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