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Portland Press, Biochemical Society Transactions, 4(30), p. 379-381, 2002

DOI: 10.1042/bst0300379

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

This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

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.