Journal
MOLECULAR AND CELLULAR NEUROSCIENCE
Volume 42, Issue 4, Pages 466-483Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.mcn.2009.09.010
Keywords
Synapse; Development; Plasticity; Scaffold; Adhesion; Glutamate receptor
Categories
Funding
- National Institute of Neurological Disorders [R01NS065795]
- Autism Speaks
- American Psychological Association [NIH APA DPN T32 MH18882-22]
- [R03MHO85224]
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Cell adhesion molecules have been implicated as key organizers of synaptic structures, but there is still a need to determine how these molecules facilitate neurotransmitter receptor recruitment to developing synapses. Here, we identify erythrocyte protein band 4.1-like 3 (protein 4.1B) as an intracellular effector molecule of Synaptic Cell Adhesion Molecule I (SynCAM1) that is sufficient to recruit NMDA-type receptors (NMDARs) to SynCAM1 adhesion sites in COS7 cells. Protein 4.1B in conjunction with SynCAM1 also increased the frequency of NMDAR-mediated mEPSCs and area of presynaptic contact in an HEK293 cell/neuron co-culture assay. Studies in cultured hippocampal neurons reveal that manipulation of protein 4.1B expression levels specifically affects NMDAR-mediated activity and localization. Finally, further experimentation in COS7 cells show that SynCAM1 may also interact with protein 4.1 N to specifically effect AMPA type receptor (AMPAR) recruitment. Thus. SynCAM1 may recruit both AMPARs and NMDARs by independent mechanisms during synapse formation. (C) 2009 Elsevier Inc. All rights reserved.
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