Identification of 14-3-3epsilon substrates from embryonic murine brain

J Proteome Res. 2006 Sep;5(9):2372-9. doi: 10.1021/pr060206k.

Abstract

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.

Publication types

  • Comparative Study
  • Research Support, N.I.H., Extramural

MeSH terms

  • 14-3-3 Proteins / analysis
  • 14-3-3 Proteins / metabolism*
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Brain / embryology*
  • Brain / metabolism*
  • COS Cells
  • Chlorocebus aethiops
  • Endopeptidases / genetics
  • Endopeptidases / metabolism*
  • Endosomal Sorting Complexes Required for Transport
  • Mass Spectrometry
  • Mice
  • Microscopy, Fluorescence
  • Molecular Sequence Data
  • Phosphorylation
  • Ubiquitin Thiolesterase

Substances

  • 14-3-3 Proteins
  • Endosomal Sorting Complexes Required for Transport
  • Endopeptidases
  • Ubiquitin Thiolesterase
  • Usp8 protein, mouse
  • ubiquitin isopeptidase