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J. Biol. Chem., Vol. 276, Issue 30, 28281-28290, July 27, 2001
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From the By using the large cytoplasmic domain of
the nicotinic acetylcholine receptor (AChR)
The Chaperone Protein 14-3-3
Interacts with the
Nicotinic Acetylcholine Receptor 
4 Subunit
EVIDENCE FOR A DYNAMIC ROLE IN SUBUNIT STABILIZATION*
,,, and§
Neuroscience Center of Excellence and
§ Department of Neurology, Louisiana State University Health
Sciences Center, New Orleans, Louisiana 70112
4 subunit as a bait in
the yeast two-hybrid system, we isolated the first cytosolic protein,
14-3-3
, known to interact directly with neuronal AChRs. 14-3-3 is
a member of a family of proteins that function as regulatory or
chaperone/ scaffolding/adaptor proteins. 14-3-3 interacted with
the recombinant 4 subunit alone in tsA 201 cells following
activation of cAMP-dependent protein kinase by forskolin.
The interaction of 14-3-3 with recombinant 4 subunits was
abolished when serine 441 of the 4 subunit was mutated to alanine
(4S441A). The surface levels of recombinant
wild-type 4
2 AChRs were ~2-fold higher than those of mutant
4S441A2 AChRs. The interaction significantly
increased the steady state levels of the 4 subunit and 42
AChRs but not that of the mutant 4S441A subunit or
mutant 4S441A2 AChRs. The EC50 values for
activation by acetylcholine were not significantly different for
42 AChRs and 4S441A2 AChRs coexpressed with
14-3-3 in oocytes following treatment with forskolin. 14-3-3 coimmunopurified with native 4 AChRs from brain. These results
support a role for 14-3-3 in dynamically regulating the expression
levels of 42 AChRs through its interaction with the 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.
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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