Splice form dependence of β-neurexin/neuroligin binding interactions

Koehnke, J. , Katsamba, P. S., Ahlsen, G., Bahna, F., Vendome, J., Honig, B., Shapiro, L. and Jin, X. (2010) Splice form dependence of β-neurexin/neuroligin binding interactions. Neuron, 67(1), pp. 61-74. (doi: 10.1016/j.neuron.2010.06.001) (PMID:20624592) (PMCID:PMC2910870)

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Abstract

Alternatively spliced β-neurexins (β-NRXs) and neuroligins (NLs) are thought to have distinct extracellular binding affinities, potentially providing a β-NRX/NL synaptic recognition code. We utilized surface plasmon resonance to measure binding affinities between all combinations of alternatively spliced β-NRX 1-3 and NL 1-3 ectodomains. Binding was observed for all β-NRX/NL pairs. The presence of the NL1 B splice insertion lowers β-NRX binding affinity by ∼2-fold, while β-NRX splice insertion 4 has small effects that do not synergize with NL splicing. New structures of glycosylated β-NRXs 1 and 2 containing splice insertion 4 reveal that the insertion forms a new β strand that replaces the β10 strand, leaving the NL binding site intact. This helps to explain the limited effect of splice insert 4 on NRX/NL binding affinities. These results provide new structural insights and quantitative binding information to help determine whether and how splice isoform choice plays a role in β-NRX/NL-mediated synaptic recognition.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Koehnke, Dr Jesko
Authors: Koehnke, J., Katsamba, P. S., Ahlsen, G., Bahna, F., Vendome, J., Honig, B., Shapiro, L., and Jin, X.
College/School:College of Science and Engineering > School of Chemistry
Journal Name:Neuron
Publisher:Cell Press
ISSN:0896-6273
ISSN (Online):1097-4199

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