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

作者：Eriksson Maria; Samuelsson Helena; Bjorklund Stefan; Tortosa Elena; Avila Jesus; Samuelsson Eva Britt; Benedikz Eirikur; Sundstrom Erik^*

来源：Neuroscience Letters, 2010, 475(1): 33-37.

DOI：10.1016/j.neulet.2010.03.039

• N-methyl-D-aspartate receptor (NMDAR)
• NR3A
• Microtubule associated-proteins 1B (MAP1B) and 1S (MAP1S/C19ORF5)
• Knock out mice
• Protein interactions
• Subcellular localization

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.

• 出版日期2010-5-7