High impact information on Nlgn1

• Alternative splicing controls selective trans-synaptic interactions of the neuroligin-neurexin complex [1].
• The second group consists of stationary nonsynaptic scaffold complexes that mainly contain neuroligin-1, can recruit synaptophysin-containing axonal transport vesicles, and are readily transformed to functional presynaptic contacts that recycle the vital dye FM 4-64 [2].
• Neuroligin 1 is a postsynaptic cell-adhesion molecule of excitatory synapses [3].
• Double immunofluorescence labeling revealed that neuroligin 1 colocalizes with glutamatergic but not gamma-aminobutyric acid (GABA)ergic synapses [3].
• Thus neuroligin 1 is a synaptic cell-adhesion molecule that is enriched in postsynaptic densities where it may recruit receptors, channels, and signal-transduction molecules to synaptic sites of cell adhesion [3].

Biological context of Nlgn1

• Synaptic cell adhesion and synaptogenesis are thought to involve the interaction of neuroligin, a postsynaptic transmembrane protein, with its presynaptic ligand neurexin [4].
• Using expression of GFP-tagged versions of neuroligin in cultured hippocampal neurons, we find that neuroligin is targeted to synapses via intracellular sequences distinct from its SAP90/PSD95 binding site [4].
• We conclude that neurexin 1beta and neuroligin 1 (and, by extension, other beta-neurexins and neuroligins) function as heterophilic cell adhesion molecules in a Ca2+-dependent reaction that is regulated by alternative splicing of beta-neurexins [5].
• Structural characterization of recombinant soluble rat neuroligin 1: mapping of secondary structure and glycosylation by mass spectrometry [6].

Anatomical context of Nlgn1

• Moreover, overexpression of the homologous neurexin I ligand, neuroligin-1, restored both neurite extension and expression of neurexin Ialpha [7].
• A cytoplasmic motif targets neuroligin-1 exclusively to dendrites of cultured hippocampal neurons [8].

Associations of Nlgn1 with chemical compounds

• Next, we examined the relationship between neuroligin and synaptic cell adhesion molecules or glutamate receptor subunits with respect to PDZ-mediated interactions [9].
• Synaptic scaffolding molecule (S-SCAM) has six PDZ domains through which it interacts with N-methyl-d-aspartate receptors and neuroligin at synaptic junctions [10].
• We describe beta-cell expression of the neuroligins, neurexins, and SynCAM, and show that neuroligin expression affects insulin secretion in INS-1 beta-cells and rat islet cells [11].

Physical interactions of Nlgn1

• Neuroligin also interacts with SAP90/PSD95, a multidomain scaffolding protein thought to recruit proteins to postsynaptic sites [4].
• Structure-based mutations of neuroligin-1 at the interface disrupt binding to neurexin-1 beta, but not the folding of neuroligin-1 and confirm the validity of the binding interface of the neuroligin-1/neurexin-1 beta complex [12].

Regulatory relationships of Nlgn1

• Overexpressed neuroligin blocked synaptic accumulation of PSD-95 but not of S-SCAM [13].

Other interactions of Nlgn1

• In contrast, Syndecan2 and IgSF4 show no overlap with the PDZ-domain specificity of neuroligin, instead, they bind to GRIP and syntenin [9].
• Synaptic scaffolding molecule is involved in the synaptic clustering of neuroligin [13].

Analytical, diagnostic and therapeutic context of Nlgn1

• Quantitative immunogold electron microscopy demonstrated that neuroligin 1 is clustered in synaptic clefts and postsynaptic densities [3].

References