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| Item Type: | Article |
|---|---|
| Title: | Neuroligin 1 is dynamically exchanged at postsynaptic sites |
| Creators Name: | Schapitz, I.U. and Behrend, B. and Pechmann, Y. and Lappe-Siefke, C. and Kneussel, S.J. and Wallace, K.E. and Stempel, A.V. and Buck, F. and Grant, S.G.N. and Schweizer, M. and Schmitz, D. and Schwarz, J.R. and Holzbaur, E.L.F. and Kneussel, M. |
| Abstract: | Neuroligins are postsynaptic cell adhesion molecules that associate with presynaptic neurexins. Both factors form a transsynaptic connection, mediate signaling across the synapse, specify synaptic functions, and play a role in synapse formation. Neuroligin dysfunction impairs synaptic transmission, disrupts neuronal networks, and is thought to participate in cognitive diseases. Here we report that chemical treatment designed to induce long-term potentiation or long-term depression (LTD) induces neuroligin 1/3 turnover, leading to either increased or decreased surface membrane protein levels, respectively. Despite its structural role at a crucial transsynaptic position, GFP-neuroligin 1 leaves synapses in hippocampal neurons over time with chemical LTD-induced neuroligin internalization depending on an intact microtubule cytoskeleton. Accordingly, neuroligin 1 and its binding partner postsynaptic density protein-95 (PSD-95) associate with components of the dynein motor complex and undergo retrograde cotransport with a dynein subunit. Transgenic depletion of dynein function in mice causes postsynaptic NLG1/3 and PSD-95 enrichment. In parallel, PSD lengths and spine head sizes are significantly increased, a phenotype similar to that observed upon transgenic overexpression of NLG1 (Dahlhaus et al., 2010). Moreover, application of a competitive PSD-95 peptide and neuroligin 1 C-terminal mutagenesis each specifically alter neuroligin 1 surface membrane expression and interfere with its internalization. Our data suggest the concept that synaptic plasticity regulates neuroligin turnover through active cytoskeleton transport. |
| Keywords: | Biotinylation, Cultured Cells, Cytoskeleton, Dendritic Spines, Dyneins, Electrophysiology, Guanylate Kinase, Hippocampus, Immunohistochemistry, Immunoprecipitation, Intracellular Signaling Peptides and Proteins, Long-Term Potentiation, Long-Term Synaptic Depression, Mass Spectrometry, Membrane Proteins, Neuronal Cell Adhesion Molecules, Neurons, Synapses, Synaptic Transmission, Transfection, Animals, Mice |
| Source: | Journal of Neuroscience |
| ISSN: | 0270-6474 |
| Publisher: | Society for Neuroscience |
| Volume: | 30 |
| Number: | 38 |
| Page Range: | 12733-12744 |
| Date: | 22 September 2010 |
| Official Publication: | https://doi.org/10.1523/JNEUROSCI.0896-10.2010 |
| PubMed: | View item in PubMed |
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