Fig. 4: Syn1 palmitoylation facilitates its binding with F-actin but not SVs. | Cell Death & Disease

Fig. 4: Syn1 palmitoylation facilitates its binding with F-actin but not SVs.

From: Crosstalk of Synapsin1 palmitoylation and phosphorylation controls the dynamicity of synaptic vesicles in neurons

Fig. 4: Syn1 palmitoylation facilitates its binding with F-actin but not SVs.

A, B SVs were extracted from WT mice brain and incubated with purified Syn1-flag or its mutants for affinity-binding assay. p > 0.1, one-way ANOVA, n = 4 biological replicates. C, D purified Syn1-WT and Syn1-3CA were incubated with actin and subjected for F-actin-binding assay (n = 4 biological replicates, ****p < 0.0001). E, F purified Syn1-flag treated with or without HA (0.5 M for 2 h) was subjected for F-actin-binding assay (n = 3 biological replicates, ****p < 0.0001). G–L purified Syn1-C360/370 A (G, H, **p = 0.0030), Syn1-C223/370 A (I, J, **p = 0.0018), or Syn1-C223/360 A (K, L **p = 0.0066) were treated with or without HA (0.5 M for 2 h) and subjected for F-actin-binding assays (n = 3 biological replicates). M, N YFPn-Syn1-WT and YFPn-Syn1-3CA were coexpressed with YFPc-β-actin in HEK-293T cell for BiFC assays and the YFP fluorescence was quantified (n = 31–46 cells from 4 biological repeats). Scale bar, 10 μm. One-way ANOVA, ****p < 0.0001. n.s., not significant. Data are mean ± s.e.m.

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