RT Journal Article
SR Electronic
T1 Silencing of Neuroligin Function by Postsynaptic Neurexins
JF The Journal of Neuroscience
JO J. Neurosci.
FD Society for Neuroscience
SP 2815
OP 2824
DO 10.1523/JNEUROSCI.0032-07.2007
VO 27
IS 11
A1 Taniguchi, Hiroki
A1 Gollan, Leora
A1 Scholl, Francisco G.
A1 Mahadomrongkul, Veeravan
A1 Dobler, Elizabeth
A1 Limthong, Nicolas
A1 Peck, Morgen
A1 Aoki, Chiye
A1 Scheiffele, Peter
YR 2007
UL http://www.jneurosci.org/content/27/11/2815.abstract
AB The formation of neuronal circuits during development involves a combination of synapse stabilization and elimination events. Synaptic adhesion molecules are thought to play an important role in synaptogenesis, and several trans-synaptic adhesion systems that promote the formation and maturation of synapses have been identified. The neuroligin–neurexin complex is a heterophilic adhesion system that promotes assembly and maturation of synapses through bidirectional signaling. In this protein complex, postsynaptic neuroligins are thought to interact trans-synaptically with presynaptic neurexins. However, the subcellular localization of neurexins has not been determined. Using immunoelectron microscopy, we found that endogenous neurexins and epitope-tagged neurexin-1β are localized to axons and presynaptic terminals in vivo. Unexpectedly, neurexins are also abundant in the postsynaptic density. cis-expression of neurexin-1β with neuroligin-1 inhibits trans-binding to recombinant neurexins, blocks the synaptogenic activity of neuroligin-1, and reduces the density of presynaptic terminals in cultured hippocampal neurons. Our results demonstrate that the function of neurexin proteins is more diverse than previously anticipated and suggest that postsynaptic cis-interactions might provide a novel mechanism for silencing the activity of a synaptic adhesion complex.