Affinity purification of diverse plant and human 14-3-3-binding partners.
Many proteins that bind to a 14-3-3 column in competition with a 14-3-3-binding phosphopeptide 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.
MRC Protein Phosphorylation Unit, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK.
F C
FC
Milne
G
G
Moorhead
M
M
Pozuelo Rubio
B
B
Wong
A
A
Kulma
J E
JE
Harthill
D
D
Villadsen
V
V
Cotelle
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C
MacKintosh
D048948:14-3-3 Proteins; D002843:Chromatin / Q000502:physiology; D002846:Chromatography, Affinity / Q000379:methods; D006801:Humans; D008027:Light; D020935:MAP Kinase Signaling System / Q000502:physiology; D010944:Plants / Q000201:enzymology*; D014446:Tyrosine 3-Monooxygenase / Q000302:isolation & purification*
D048948:14-3-3 Proteins; D002843:Chromatin; D014446:Tyrosine 3-Monooxygenase