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

Abstract:

: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.

journal_name

Neurosci Lett

journal_title

Neuroscience letters

authors

Eriksson M,Samuelsson H,Björklund S,Tortosa E,Avila J,Samuelsson EB,Benedikz E,Sundström E

doi

10.1016/j.neulet.2010.03.039

subject

Has Abstract

pub_date

2010-05-07 00:00:00

pages

33-7

issue

1

eissn

0304-3940

issn

1872-7972

pii

S0304-3940(10)00336-8

journal_volume

475

pub_type

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