Fig. 6: NEDD4-1 is required for caPAK4-induced α-synuclein degradation in SHSY-5Y cells. | Cell Death & Disease

Fig. 6: NEDD4-1 is required for caPAK4-induced α-synuclein degradation in SHSY-5Y cells.

From: p21-activated kinase 4 controls the aggregation of α-synuclein by reducing the monomeric and aggregated forms of α-synuclein: involvement of the E3 ubiquitin ligase NEDD4-1

Fig. 6: NEDD4-1 is required for caPAK4-induced α-synuclein degradation in SHSY-5Y cells.The alternative text for this image may have been generated using AI.

A Immunoblotting for α-synuclein in SH-SY5Y cells transfected with plasmids encoding vector alone or human Myc-caPAK4. B Quantification of α-synuclein intensity in blot A normalized to GAPDH. C In vitro ubiquitination of α-synuclein. D Immunoprecipitation (IP) and immunoblotting for the indicated E3 ligases. E, F Immunoprecipitation (IP) and immunoblotting. SH-SY5Y cell lysates were immunoprecipitated with anti-PAK4 or anti-NEDD4-1 (E)/anti-NEDD4-2 (F) antibodies followed by immunoblotting for PAK4, NEDD4-1, and GAPDH. G Immunoblotting for α-synuclein in SH-SY5Y cells following incubation with the indicated E3 ligase inhibitors. H Quantification of the α-synuclein signal in the blot E normalized to GAPDH. I Immunoblotting for α-synuclein in SH-SY5Y cells transfected with NEDD4-1 siRNAs. J Quantification of α-synuclein levels in the blot shown (I) normalized to GAPDH. The data are presented as the mean ± SEM. *P < 0.01. Two-way ANOVA (B, H, J) was used for statistical analysis followed by Tukey’s multiple comparisons test.

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