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Mind bomb-2 is an E3 ligase that ubiquitinates the N-methyl-D-aspartate receptor NR2B subunit in a phosphorylation-dependent manner.

The N-methyl-D-aspartate receptor (NMDAR) plays a critical role in synaptic plasticity. Post-translational modifications of NMDARs, such as phosphorylation, alter both the activity and trafficking properties of NMDARs. Ubiquitination is increasingly being recognized as another post-translational modification that can alter synaptic protein composition and function. We identified Mind bomb-2 as an E3 ubiquitin ligase that interacts with and ubiquitinates the NR2B subunit of the NMDAR in mammalian cells. The protein-protein interaction and the ubiquitination of the NR2B subunit were found to be enhanced in a Fyn phosphorylation-dependent manner. Immunocytochemical studies reveal that Mind bomb-2 is localized to postsynaptic sites and colocalizes with the NMDAR in apical dendrites of hippocampal neurons. Furthermore, we show that NMDAR activity is down-regulated by Mind bomb-2. These results identify a specific E3 ubiquitin ligase as a novel interactant with the NR2B subunit and suggest a possible mechanism for the regulation of NMDAR function involving both phosphorylation and ubiquitination.

Pubmed ID: 17962190


  • Jurd R
  • Thornton C
  • Wang J
  • Luong K
  • Phamluong K
  • Kharazia V
  • Gibb SL
  • Ron D


The Journal of biological chemistry

Publication Data

January 4, 2008

Associated Grants

  • Agency: NIAAA NIH HHS, Id: R01 AA 013438-01A1
  • Agency: NIAAA NIH HHS, Id: R01 AA013438
  • Agency: NIAAA NIH HHS, Id: R01 AA013438-01A1

Mesh Terms

  • Animals
  • Cell Line
  • Cells, Cultured
  • Hippocampus
  • Humans
  • Immunoprecipitation
  • In Situ Hybridization
  • Models, Biological
  • Neurons
  • Phosphorylation
  • Protein Binding
  • Protein Processing, Post-Translational
  • Proto-Oncogene Proteins c-fyn
  • Rats
  • Receptors, N-Methyl-D-Aspartate
  • Two-Hybrid System Techniques
  • Ubiquitin
  • Ubiquitin-Protein Ligases
  • Ubiquitination