Mass spectrometric studies on mouse hippocampal synapsins Ia, IIa, and IIb and identification of a novel phosphorylation site at serine-546

J Proteome Res. 2007 Jul;6(7):2695-710. doi: 10.1021/pr070157r. Epub 2007 Jun 19.

Abstract

Synapsins are key phosphoproteins in the mammalian brain, and structural research on synapsins is still holding center stage. Proteins were extracted from hippocampal tissue and separated on two-dimensional gel electrophoresis (2-DE), and the spots were analyzed by MALDI-TOF-TOF and nano-LC-ESI-MS/MS. Synapsins Ia, IIa, and IIb were unambiguously identified and represented by 15 individual spots on 2-DE. Several serine phosphorylation sites were confirmed, and a novel phosphorylation site was observed at Ser-546 in synapsin IIa in all gels analyzed.

MeSH terms

  • Acetylation
  • Alternative Splicing
  • Amino Acid Sequence
  • Animals
  • Electrophoresis, Gel, Two-Dimensional
  • Hippocampus / chemistry*
  • Male
  • Methionine / chemistry
  • Methylation
  • Mice
  • Mice, Inbred C57BL
  • Molecular Sequence Data
  • Nanotechnology / methods
  • Phosphoproteins / chemistry*
  • Phosphorylation
  • Phosphoserine / analysis*
  • Protein Conformation
  • Protein Isoforms / chemistry
  • Protein Isoforms / genetics
  • Serine / chemistry*
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / methods
  • Synapsins / chemistry*
  • Synapsins / genetics

Substances

  • Phosphoproteins
  • Protein Isoforms
  • Synapsins
  • Phosphoserine
  • Serine
  • Methionine