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.
Milne
F C
FC
MRC Protein Phosphorylation Unit, School of Life Sciences, University of Dundee, Dundee DD1 5EH, Scotland, UK.
Moorhead
G
G
Pozuelo Rubio
M
M
Wong
B
B
Kulma
A
A
Harthill
J E
JE
Villadsen
D
D
Cotelle
V
V
MacKintosh
C
C
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