Affinity purification of diverse plant and human 14-3-3-binding partners

F. C. Milne, G. Moorhead, M. Pozuelo-Rubio, B. Wong, A. Kulma, J. E. Harthill, D. Villadsen, V. Cotelle, C. MacKintosh

    Research output: Contribution to journalArticlepeer-review

    19 Citations (Scopus)


    Many proteins that bind to a 14-3-3 column in competition with a 14-3-3-binding phospho-peptide have been purified from plant and mammalian cells and tissues. New 14-3-3 targets include enzymes of biosynthetic metabolism, vesicle trafficking, cell signalling and chromatin function. These findings indicate central regulatory roles for 14-3-3s in partitioning carbon among the pathways of sugar, amino acid, nucleotide and protein biosynthesis in plants. Our results also suggest that the current perception that 14-3-3s bind predominantly to signalling proteins in mammalian cells is incorrect, and has probably arisen because of the intensity of research on mammalian signalling and for technical reasons.

    Original languageEnglish
    Pages (from-to)379-381
    Number of pages3
    JournalBiochemical Society Transactions
    Issue number4
    Publication statusPublished - Aug 2002
    Event676th Biochemical Society Meeting - Edinburgh, United Kingdom
    Duration: 8 Apr 200210 Apr 2002


    • 14-3-3 proteins
    • Nitrate reductase
    • Vesicle trafficking


    Dive into the research topics of 'Affinity purification of diverse plant and human 14-3-3-binding partners'. Together they form a unique fingerprint.

    Cite this