Figure 3: The N-terminal histidine-rich region of β-neurexin1/2/3 and S4 inserts of α/β-neurexin1/2 are responsible for Aβ42 oligomer interaction. | Scientific Reports

Figure 3: The N-terminal histidine-rich region of β-neurexin1/2/3 and S4 inserts of α/β-neurexin1/2 are responsible for Aβ42 oligomer interaction.

From: Amyloid-β Oligomers Interact with Neurexin and Diminish Neurexin-mediated Excitatory Presynaptic Organization

Figure 3

(a) Representative images showing the binding of biotin-Aβ42 oligomers (250 nM, monomer equivalent) to COS-7 cells expressing the indicated isoform of extracellularly HA-tagged NRX. S4(−) and S4(+) indicate without and with an insert at splicing site 4, respectively. HA fluorescent signals correspond to surface HA. Note that in assays with S4-negative isoforms, there is no bound biotin-Aβ42 oligomer signal on cells expressing α-NRX1, 2, or 3 whereas cells expressing β-NRX1, 2, and 3 all have significant bound biotin-Aβ42 oligomer signal. Cells expressing β-NRX1, 2, and 3 lacking the histidine-rich domain (∆HRD) have no biotin-Aβ42 oligomer binding signal. Cells expressing S4-positive isoforms of α-NRX1 or 2 or β-NRX1, 2, or 3 have significant bound biotin-Aβ42 oligomers. Scale bar represents 30 μm. (b) Quantification of bound biotin-Aβ42 oligomers for each NRX construct. n = 30 cells for each construct from three independent experiments, one-way ANOVA, P < 0001. *P < 0.01 and ***P < 0.0001 compared with HA-CD4 and §P < 0.0001 between S4(−) and S4(+) by Bonferroni multiple comparisons tests. Data are presented as mean ± SEM.

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