The NMDAR subunit NR3A interacts with microtubule-associated protein 1S in the brain

Autor: Wallace L. McKeehan, Eva-Britt Samuelsson, Leyuan Liu, Maria Eriksson, Eirikur Benedikz, Erik Sundström, Helena Samuelsson
Rok vydání: 2007
Předmět:
Zdroj: Eriksson, M, Samuelsson, H, Samuelsson, E-B, Liu, L, McKeehan, W L, Benedikz, E & Sundström, E 2007, ' The NMDAR subunit NR3A interacts with microtubule-associated protein 1S in the brain ', Biochemical and Biophysical Research Communications, vol. 361, no. 1, pp. 127-32 . https://doi.org/10.1016/j.bbrc.2007.06.179
ISSN: 0006-291X
DOI: 10.1016/j.bbrc.2007.06.179
Popis: When screening a brain cDNA library, we found that the N-methyl-D-aspartate receptor subunit NR3A binds to microtubule-associated protein (MAP) 1S/chromosome 19 open reading frame 5 (C19ORF5). The interaction was confirmed in vitro and in vivo, and binding of MAP1S was localized to the membrane-proximal part of the NR3A C-terminus. MAP1S belongs to the same family as MAP1A and MAP1B, and was found to be abundant in both postnatal and adult rat brain. In hippocampal neurons the distribution-pattern of MAP1S resembled that of beta-tubulin III, but a fraction of the protein colocalized with synaptic markers synapsin and postsynaptic density protein 95 (PSD95), in beta-tubulin III-negative filopodia-like protrusions. There was coexistance between MAP1S and NR3A immunoreactivity in neurite shafts and occasionally in filopodia-like processes. MAP1S potentially links NR3A to the cytoskeleton, and may stabilize NR3A-containing receptors at the synapse and regulate their movement between synaptic and extrasynaptic sites.
Databáze: OpenAIRE
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