Isoforms of 14-3-3 protein can form homo- and heterodimers in vivo and in vitro: implications for function as adapter proteins.
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 cross-linking 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.
Jones
D H
DH
Division of Protein Structure, National Institute for Medical Research, London, UK.
Ley
S
S
Aitken
A
A
D048948:14-3-3 Proteins; D001483:Base Sequence; D002460:Cell Line; D003001:Cloning, Molecular; D003432:Cross-Linking Reagents; D004926:Escherichia coli; D006801:Humans; D008969:Molecular Sequence Data; D011506:Proteins / Q000737:chemistry* / Q000502:physiology*; D015398:Signal Transduction / Q000502:physiology; D013329:Structure-Activity Relationship; D014446:Tyrosine 3-Monooxygenase
D048948:14-3-3 Proteins; D003432:Cross-Linking Reagents; D011506:Proteins; D014446:Tyrosine 3-Monooxygenase