4.4 Article

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

期刊

NEUROSCIENCE LETTERS
卷 475, 期 1, 页码 33-37

出版社

ELSEVIER IRELAND LTD
DOI: 10.1016/j.neulet.2010.03.039

关键词

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

资金

  1. Swedish Research Council
  2. Marianne and Marcus Wallenberg Foundation
  3. Karolinska Institutet

向作者/读者索取更多资源

Incorporation of the N-methyl-D-aspartate receptor (NMDAR) subunit NR3A into functional NMDARs results in reduced channel conductance and Ca2+ 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. (C) 2010 Elsevier Ireland Ltd. All rights reserved.

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