IgSF21 promotes differentiation of inhibitory synapses via binding to neurexin2α

Yuko Tanabe, Yusuke Naito, Cristina Vasuta, Alfred Kihoon Lee, Youssouf Soumounou, Michael W. Linhoff and Hideto Takahashi ()
Additional contact information
Yuko Tanabe: Institut de RecherchesCliniques de Montréal
Yusuke Naito: Institut de RecherchesCliniques de Montréal
Cristina Vasuta: Institut de RecherchesCliniques de Montréal
Alfred Kihoon Lee: Institut de RecherchesCliniques de Montréal
Youssouf Soumounou: Institut de RecherchesCliniques de Montréal
Michael W. Linhoff: Washington University School of Medicine
Hideto Takahashi: Institut de RecherchesCliniques de Montréal

Nature Communications, 2017, vol. 8, issue 1, 1-15

Abstract: Abstract Coordinated development of excitatory and inhibitory synapses is essential for higher brain function, and impairment in this development is associated with neuropsychiatric disorders. In contrast to the large body of accumulated evidence regarding excitatory synapse development, little is known about synaptic adhesion and organization mechanisms underlying inhibitory synapse development. Through unbiased expression screens and proteomics, we identified immunoglobulin superfamily member 21 (IgSF21) as a neurexin2α-interacting membrane protein that selectively induces inhibitory presynaptic differentiation. IgSF21 localizes postsynaptically and recruits axonal neurexin2α in a trans-interaction manner. Deleting IgSF21 in mice impairs inhibitory presynaptic organization, especially in the hippocampal CA1 stratum radiatum, and also diminishes GABA-mediated synaptic transmission in hippocampal CA1 neurons without affecting their excitatory synapses. Finally, mice lacking IgSF21 show a sensorimotor gating deficit. These findings suggest that IgSF21 selectively regulates inhibitory presynaptic differentiation through interacting with presynaptic neurexin2α and plays a crucial role in synaptic inhibition in the brain.

Date: 2017
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/s41467-017-00333-w Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-00333-w

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-017-00333-w

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().