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Neuroligin-1 performs neurexin-dependent and neurexin-independent functions in synapse validation
Ko, Jaewon,Zhang, Chen,Arac, Demet,Boucard, Antony A,Brunger, Axel T,Sü,dhof, Thomas C Wiley (John WileySons) 2009 The EMBO journal Vol.28 No.20
<P>Postsynaptic neuroligins are thought to perform essential functions in synapse validation and synaptic transmission by binding to, and dimerizing, presynaptic alpha- and beta-neurexins. To test this hypothesis, we examined the functional effects of neuroligin-1 mutations that impair only alpha-neurexin binding, block both alpha- and beta-neurexin binding, or abolish neuroligin-1 dimerization. Abolishing alpha-neurexin binding abrogated neuroligin-induced generation of neuronal synapses onto transfected non-neuronal cells in the so-called artificial synapse-formation assay, even though beta-neurexin binding was retained. Thus, in this assay, neuroligin-1 induces apparent synapse formation by binding to presynaptic alpha-neurexins. In transfected neurons, however, neither alpha- nor beta-neurexin binding was essential for the ability of postsynaptic neuroligin-1 to dramatically increase synapse density, suggesting a neurexin-independent mechanism of synapse formation. Moreover, neuroligin-1 dimerization was not required for either the non-neuronal or the neuronal synapse-formation assay. Nevertheless, both alpha-neurexin binding and neuroligin-1 dimerization were essential for the increase in apparent synapse size that is induced by neuroligin-1 in transfected neurons. Thus, neuroligin-1 performs diverse synaptic functions by mechanisms that include as essential components of alpha-neurexin binding and neuroligin dimerization, but extend beyond these activities.</P>
Cross section data sets for electron collisions with H2, O2, CO, CO2, N2O and H2O
Anzai, K.,Kato, H.,Hoshino, M.,Tanaka, H.,Itikawa, Y.,Campbell, L.,Brunger, M. J.,Buckman, S. J.,Cho, H.,Blanco, F.,Garcia, G.,Limã,o-Vieira, P.,Ingó,lfsson, O. Springer-Verlag 2012 European Physical Journal D Vol.66 No.2