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First published online April 16, 2004
doi: 10.1242/10.1242/jcs.01171

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Unlocking the code of 14-3-3

Laboratory of Protein Dynamics and Signaling, NCI-Frederick, Frederick, MD 21702, USA

View larger version (36K): [in a new window]   Fig. 1. Properties of a 14-3-3 dimer. The diagram shown is derived from the structure of a 14-3-3 dimer bound to the indicated (arrows) phosphoserine peptides (Protein Data Bank accession number 1QJB) (Rittinger et al., 1999).

View larger version (31K): [in a new window]   Fig. 2. Regulation of 14-3-3 target binding by protein phosphatases. PP2A directly interacts with BAD, Raf-1 and KSR1, and mediates the dephosphorylation of pS112 on BAD, pS259 on Raf-1 and pS392 on KSR1. PP1 binds Cdc25C and the Ron receptor tyrosine kinase, and dephosphorylates the pS216 site on Cdc25C [exposing a nuclear localization sequence (NLS)] and the pS1394 site on Ron.

View larger version (63K): [in a new window]   Fig. 3. 14-3-3 is a regulator of protein localization. Indicated are proteins whose subcellular localizations are regulated by 14-3-3 binding. See text for details.