Isoforms of 14‐3‐3 protein can form homo‐ and heterodimers in vivo and in vitro: implications for function as adapter proteins

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Abstract
14‐3‐3 proteins play a role in many cellular functions: they bind to and regulate several proteins which are critical for cell proliferation and differentiation. 14‐3‐3 proteins exist as dimers, and in this study we have shown that diverse 14‐3‐3 proteins can form both homo‐ and heterodimers in vitro (by crosslinking studies) and in vivo (by coimmunoprecipitation and Western blot analysis); this interaction is mediated solely through the N‐terminal domain of the proteins. The composition of 14‐3‐3 dimers within a cell may play a key part in the role of this family of proteins as modulators or adapters which facilitate the interaction of distinct components of signalling pathways.