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Neurosci Lett. 2010 May 7;475(1):33-7. doi: 10.1016/j.neulet.2010.03.039. Epub 2010 Mar 19.

MAP1B binds to the NMDA receptor subunit NR3A and affects NR3A protein concentrations.

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Division of Neurodegeneration, Department of Neurobiology, Care Sciences and Society, Karolinska Institutet, Novum, 141 86 Stockholm, Sweden.


Incorporation of the N-methyl-d-aspartate receptor (NMDAR) subunit NR3A into functional NMDARs results in reduced channel conductance and Ca(2+) permeability. To further investigate the function of NR3A, we have set out to characterize its intracellular binding partners. Here, we report a novel protein interaction between NR3A and microtubule associated-protein (MAP) 1B, which both are localized to dendritic shafts and filopodia. NR3A protein levels were increased in MAP1B deficient (-/-) mice, with a corresponding decrease in NR1 levels, but the fraction of filopodia immunoreactive for NR3A was equal in cells from -/- and wild type (WT) mice. NR3A has previously been shown to interact with another member of the MAP1 family, MAP1S. We showed that MAP1S binds to microtubules in a similar manner as MAP1B, and suggest that MAP1S and MAP1B both are involved in regulating trafficking of NR3A-containing NMDAR.

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