Characterizing the novel protein p33MONOX

Mol Cell Biochem. 2011 Apr;350(1-2):127-34. doi: 10.1007/s11010-010-0690-4. Epub 2010 Dec 14.

Abstract

The novel protein p33MONOX (p33Monooxygenase) was over-expressed in neuroblastoma cells demonstrating its inhibitory effect on the phosphorylation of the App (amyloid precursor protein) and Bcl2 (B-cell lymphoma 2) proteins but mediating higher activation of Mapk1/3 (mitogen-activated protein kinase 1/3). We employed a variety of cell biology techniques to show the localization of p33MONOX to the cytoplasm of pyramidal neurons in the mouse brain hippocampus. We also carried out a yeast-two-hybrid screening plus co-immunoprecipitation and bio-informatics to determine COBRA1 (cofactor of BRCA1 (breast cancer type 1)), NOL12 (nucleolar protein 12), and PRNP (prion protein) as p33MONOX-interacting proteins. Bio-computational analyses revealed a flavine-containing monooxygenase (FMO)-1 motif, thus linking p33MONOX to a group of previously characterized proteins, the MICALs (molecule interacting with CasL). Concluding, p33MONOX might regulate pre- and post-transcriptional control of dynamic processes related to growth cone guidance.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Axons / metabolism
  • Axons / physiology
  • Cells, Cultured
  • Cloning, Molecular
  • Humans
  • Mice
  • Mice, Inbred C57BL
  • Mixed Function Oxygenases / genetics*
  • Mixed Function Oxygenases / isolation & purification*
  • Mixed Function Oxygenases / physiology
  • Molecular Sequence Data
  • Nerve Tissue Proteins / genetics*
  • Nerve Tissue Proteins / isolation & purification*
  • PC12 Cells
  • Pyramidal Cells / metabolism
  • Pyramidal Cells / physiology
  • Rats
  • Sequence Analysis, Protein
  • Transfection

Substances

  • Nerve Tissue Proteins
  • KIAA1191 protein, human
  • LOC306766 protein, rat
  • Mixed Function Oxygenases
  • p33MONOX protein, mouse