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.
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
J. Biol. Chem.
Date: Jan. 04, 2008
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