Identification of 14-3-3epsilon substrates from embryonic murine brain.
Mice deficient in 14-3-3epsilon exhibit abnormal neuronal migration and die perinatally. We report here the first large-scale analysis of 14-3-3 interacting partners from primary animal tissue, identifying from embryonic murine brain 163 14-3-3epsilon interacting proteins and 85 phosphorylation sites on these proteins. Phosphorylation of the deubiquitinating enzyme USP8 at serine 680 was found essential for its interaction with 14-3-3epsilon and for maintaining USP8 in the cytosol.
Ballif
Bryan A
BA
Department of Cell Biology, Harvard Medical School, 240 Longwood Avenue, Boston, Massachusetts 02115, USA.
Cao
Zhongwei
Z
Schwartz
Daniel
D
Carraway
Kermit L
KL
Gygi
Steven P
SP
D048948:14-3-3 Proteins / Q000032:analysis / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D001921:Brain / Q000196:embryology* / Q000378:metabolism*; D019556:COS Cells; D002522:Chlorocebus aethiops; D010450:Endopeptidases / Q000235:genetics / Q000378:metabolism*; D056827:Endosomal Sorting Complexes Required for Transport; D013058:Mass Spectrometry; D051379:Mice; D008856:Microscopy, Fluorescence; D008969:Molecular Sequence Data; D010766:Phosphorylation; D043222:Ubiquitin Thiolesterase
D048948:14-3-3 Proteins; D056827:Endosomal Sorting Complexes Required for Transport; D010450:Endopeptidases; D043222:Ubiquitin Thiolesterase; C541536:Usp8 protein, mouse; C091939:ubiquitin isopeptidase