Phosphorylation-regulated binding between 14-3-3 and its target proteins. Each 14-3-3 monomer contains a binding site for a serine/threonine-phosphorylated 14-3-3 binding motif. Upon phosphorylation of target proteins, a 14-3-3 dimer can bind to 2 phosphorylated motifs in tandem in 1 target protein, modulating its conformation/structure. A 14-3-3 dimer can also bind to 2 separate phosphoproteins, acting as an adapter/scaffold for assembly of protein complexes. Phosphorylation of 14-3-3 at Thr²³³ and Ser¹⁸⁵ negatively regulates its ability to interact with target proteins. These features enable 14-3-3 to regulate protein function or transmit signals in a phosphorylation-dependent manner, which can be controlled by a single protein kinase/phosphatase pair or multiple protein kinases/phosphatases.