The NR2D subunit of the NMDA receptor inhibits c-Abl tyrosine kinase activity, an effect that is mediated via the proline rich region of the NR2D subunit and the SH3 region of Abl. Similar effects on Abl activity have been observed with the NR2B subunit. To determine if the NR2B subunit forms a stable complex with Abl, co-immunoprecipitation experiments were performed on transfected 293T human embryonic kidney cells and whole rat brain lysates from embryonic and neonatal rats. Immunoprecipitation of Abl from co-transfected cells failed to co-precipitate the NR2B subunit. Similarly, immunoprecipitation of the NR2B subunit failed to co-precipitate Abl. Comparable results were also seen in whole rat brain lysates from embryonic and neonatal rats. These data demonstrate that in contrast to the NR2D subunit, the NR2B subunit does not form a stable, co-immunoprecipitatable complex with Abl, suggesting Abl inhibition by the NR2B subunit may be due to transient interactions between the two proteins.
Amanda Everhart, ’02 Anchorage, AK
Major: Biochemistry and Molecular Biology
Sponsor: Barbara Christie-Pope