14-3-3 proteins activate Pseudomonas exotoxins-S and -T by chaperoning a hydrophobic surface

The 14-3-3 proteins

So what’s so interesting about them? In 1996 14-3-3 was found to bind to a variety of oncoproteins including Raf-1, polyoma middle T, and Bcr-Abl. Since then the 14-3-3 proteins have been shown to bind to a wide variety of proteins involved in signal transduction, cell cycle and apoptosis. These proteins include Cdc25, NFAT, Bad, Cbl, A20, PI 3-kinase, IRS-1, MEKK, p130Cas, glucocorticoid recep...

14-3-3 proteins are required for the inhibition of Ras by exoenzyme S.

14-3-3 proteins play a regulatory role and participate in both signal transduction and checkpoint control pathways. 14-3-3 proteins bind phosphoserine ligands, such as Raf-1 kinase and Bad, by recognizing the phosphorylated consensus motif, Arg-Ser-Xaa-pSer-Xaa-Pro (where 'Xaa' represents 'any residue', and 'pSer' is 'phosphoserine'). However, 14-3-3 proteins must bind unphosphorylated ligands,...

C-terminal recognition by 14-3-3 proteins for surface expression of membrane receptors.

Diverse functions of 14-3-3 proteins are directly coupled to their ability to interact with targeted peptide substrates. RSX(pS/pT)XP and RXPhiX(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...

Exoenzyme S of Pseudomonas aeruginosa: cellular targets and interaction with 14-3-3

Plant metabolism: Enzyme regulation by 14-3-3 proteins

14-3-3 proteins have been found to regulate the plant enzyme nitrate reductase by reversible phosphoserine binding. Plant plasma-membrane H(+)-ATPases, transporters that are activated by the phytotoxin fusicoccin, appear to be regulated in a similar fashion.