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Papers In Press, published online ahead of print August 24, 2005
Department of Neuroscience and High Throughtput Biology Center, Johns Hopkins University, Baltimore, MD 21205
Corresponding Author: minli{at}jhmi.edu
Diverse functions of 14-3-3 proteins are directly coupled to their ability to interact with targeted peptide substrates. RSX(pS/pT)XP and RX
J. Biol. Chem, 10.1074/jbc.M507559200
Submitted on July 12, 2005
Revised on August 24, 2005
Accepted on August 24, 2005
Carboxyl-terminal recognition by 14-3-3 proteins for surface expression of membrane receptors
X(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 ER localized signal and re-directing membrane proteins to cell surface. Here we report that the carboxyl-terminal SWTY motif, although different from modes I and II consensus, binds tightly to 14-3-3 proteins with a dissociation constant (KD) of 0.17 
M, comparable to 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.
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