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

Maria Eriksson, Helena Samuelsson, Eva-Britt Samuelsson, Leyuan Liu, Wallace L McKeehan, Eirikur Benedikz, Erik Sundström

Research output: Contribution to journalJournal articleResearchpeer-review


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.
Original languageEnglish
JournalBiochemical and Biophysical Research Communications
Issue number1
Pages (from-to)127-32
Number of pages6
Publication statusPublished - 2007


  • Animals
  • Binding Sites
  • Brain
  • Cells, Cultured
  • Central Nervous System
  • Humans
  • Microtubule-Associated Proteins
  • Neurons
  • Rats
  • Rats, Sprague-Dawley
  • Receptors, N-Methyl-D-Aspartate


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