University of Massachusetts Medical School Faculty Publications
UMMS Affiliation
Brudnick Neuropsychiatric Research Institute, Department of Psychiatry
Publication Date
2013-02-20
Document Type
Article
Subjects
Animals; Cell Adhesion Molecules, Neuronal; Cells, Cultured; Female; HEK293 Cells; Hippocampus; Humans; Interneurons; Male; Nerve Tissue Proteins; Neural Inhibition; Organ Culture Techniques; Presynaptic Terminals; Protein Binding; Protein Isoforms; Pyramidal Cells; Rats; Receptors, Cell Surface; Synapses
Disciplines
Amino Acids, Peptides, and Proteins | Investigative Techniques | Molecular and Cellular Neuroscience | Nervous System | Neuroscience and Neurobiology
Abstract
Synaptic transmission depends on the matching and alignment of presynaptically released transmitters and postsynaptic neurotransmitter receptors. Neuroligin (NL) and Neurexin (Nrxn) proteins are trans-synaptic adhesion molecules that are important in validation and maturation of specific synapses. NL isoforms NL1 and NL2 have specific functional roles in excitatory and inhibitory synapses, respectively, but the molecular basis behind this distinction is still unclear. We show here that the extracellular domain of NL2 confers its unique ability to enhance inhibitory synaptic function when overexpressed in rat hippocampal pyramidal neurons, whereas NL1 normally only promotes excitatory synapses. This specificity is conferred by presynaptic Nrxn isoforms, as NL1 can also induce functional inhibitory synapse connections when the presynaptic interneurons ectopically express an Nrxn isoform that binds to NL1. Our results indicate that trans-synaptic interaction with differentially expressed presynaptic Nrxns underlies the distinct functions of NL1 and NL2, and is sufficient to induce functional inhibitory synapse formation.
Rights and Permissions
Publisher PDF posted as allowed by the publisher's author rights policy at http://www.jneurosci.org/site/misc/ifa_policies.xhtml#copyright.
DOI of Published Version
10.1523/JNEUROSCI.1811-12.2013
Source
J Neurosci. 2013 Feb 20;33(8):3612-23. doi: 10.1523/JNEUROSCI.1811-12.2013. Link to article on publisher's site
Related Resources
Journal/Book/Conference Title
The Journal of neuroscience : the official journal of the Society for Neuroscience
PubMed ID
23426688
Repository Citation
Futai K, Doty CD, Baek B, Ryu J, Sheng M. (2013). Specific trans-synaptic interaction with inhibitory interneuronal neurexin underlies differential ability of neuroligins to induce functional inhibitory synapses. University of Massachusetts Medical School Faculty Publications. https://doi.org/10.1523/JNEUROSCI.1811-12.2013. Retrieved from https://escholarship.umassmed.edu/faculty_pubs/180
Included in
Amino Acids, Peptides, and Proteins Commons, Investigative Techniques Commons, Molecular and Cellular Neuroscience Commons, Nervous System Commons