Binding of 14-3-3 Protein to the Plasma Membrane H+-ATPase AHA2 Involves the Three C-terminal Residues Tyr946-Thr-Val and Requires Phosphorylation of Thr947

Myeloid-Related Protein-14 Is a p38 MAPK Substrate in Human Neutrophils

“…4C). Appearance of a peptide with this m/z in addition to the mass plus hydrogen ϩ 80 precursor ion confirms that the posttranslational modification on the peptide was phosphorylation (41)(42)(43)(44). As Thr 113 is the only residue in the peptide that could serve as a phosphate acceptor from p38 MAPK, these data suggest that p38 MAPK phosphorylates MRP-14 on Thr 113 .…”

Role of the plasma membrane H+-ATPase in the regulation of organic acid exudation under aluminum toxicity and phosphorus deficiency

“…42 The association of 14-3-3 proteins with the phosphothreonine-containing sequence of the plasma membrane H C -ATPase maintains the phosphorylation state and results in its activation. 43,44 The 14-3-3 proteins, which are members of a highly conserved protein family with regulatory roles in all eukaryotes, interact with phosphorylated target proteins such as nitrate reductase, sucrose-phosphate synthase and plasma membrane H C -ATPase. 45 In broad bean and soybean roots, 50 mM Al increased the phosphorylation levels of the plasma membrane and its interaction with the 14-3-3 protein with a time dependent manner in Al-resistance cultivars but not in Al-sensitive cultivars.…”

Yeast 14‐3‐3 proteins

“…48 In addition, several apparently unrelated motifs for binding 14-3-3 proteins have been described. 2,11,16,22,32,46,47 For the yeast proteins that bind to 14-3-3 proteins, consensus sequences as mentioned above have not yet been reported and it is unclear which sequences are responsible for binding in yeast. Interestingly, the heterologous Raf-1p, which binds S. cerevisiae 14-3-3 proteins, contains a functional RSXpSXP motif.…”