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J. Biol. Chem., Vol. 280, Issue 43, 36263-36272, October 28, 2005

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C-terminal Recognition by 14-3-3 Proteins for Surface Expression of Membrane Receptors^*

Brian Coblitz, Sojin Shikano1, Meng Wu, Sandra B. Gabelli, Lisa M. Cockrell¶, Matt Spieker, Yoshiro Hanyu||, Haian Fu¶, L. Mario Amzel, and Min Li1

From the Department of Neuroscience and the High Throughput Biology Center and the Department of Biophysics and Biophysical Chemistry, School of Medicine, Johns Hopkins University, Baltimore, Maryland 21205, the ^¶Department of Pharmacology, Emory University School of Medicine, Atlanta, Georgia 30322, and the ^||Institute for Biological Resources and Functions, National Institutes of Advanced Industrial Science and Technology, 1-1-1 Higashi, Tsukuba, 305-8566 Japan

Diverse functions of 14-3-3 proteins are directly coupled to their ability to interact with targeted peptide substrates. RSX(pS/pT)XP and RXX(pS/pT)XP are two canonical consensus binding motifs for 14-3-3 proteins representing the two common binding modes, modes I and II, between 14-3-3 and internal peptides. Using a genetic selection, we have screened a random peptide library and identified a group of C-terminal motifs, termed SWTY, capable of overriding an endoplasmic reticulum localization signal and redirecting membrane proteins to cell surface. Here we report that the C-terminal SWTY motif, although different from mode I and II consensus, binds tightly to 14-3-3 proteins with a dissociation constant (K_D) of 0.17 µM, comparable with that of internal canonical binding peptides. We show that all residues but proline in -SWTX-COOH are compatible for the interaction and surface expression. Because SWTY-like sequences have been found in native proteins, these results support a broad significance of 14-3-3 interaction with protein C termini. The C-terminal binding consensus, mode III, represents an expansion of the repertoire of 14-3-3-targeted sequences.

Received for publication, July 12, 2005 , and in revised form, August 24, 2005.

^* This work was supported by National Institutes of Health Grants GM70959 and NS33324 (to M. L.) and GM53165 and GM60033 (to H. F.) and a predoctoral fellowship award from the American Heart Association (to B. C.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Dept. of Neuroscience, Johns Hopkins University School of Medicine, BRB311, 733 North Broadway, Baltimore, MD 21205. Tel.: 410-614-5131; Fax: 410-614-1001; E-mail: minli{at}jhmi.edu.

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