Fig. 2: The increased binding affinity of NDP52GE towards LC3C strictly depends on the cLIR motif. | Cell Death & Disease

Fig. 2: The increased binding affinity of NDP52GE towards LC3C strictly depends on the cLIR motif.

From: A variant of the autophagic receptor NDP52 counteracts phospho-TAU accumulation and emerges as a protective factor for Alzheimer’s disease

Fig. 2

A Schematic representation of the human NDP52WT protein, the human variant NDP52GE, and the NDP52 mutants used in this study. The G140E aminoacidic substitution is highlighted, and the position relative to cLIR motif as well as the LIR-like motif are shown in the expanded dotted area. SKICH skeletal muscle and kidney-enriched inositol phosphatase carboxyl homology, cLIR non-canonical LC3-interacting region, LIR LC3-interacting region, UBZ ubiquitin-binding zinc finger. Lysates of SH-SY5Y cells expressing the indicated FLAG- and HA-tagged proteins were immunoprecipitated with anti-HA (B) or anti-FLAG (C) beads. Samples were analyzed by Western blot using the indicated antibodies. The graphs report the amount of the indicated FLAG-NDP52 protein coprecipitated by the corresponding HA-LC3C protein. Data were expressed as percentage variation over FLAG-NDP52WT. Images and data are representative of three independent experiments. ****p-value < 0.0001; ***p-value < 0.001; **p-value < 0.01: *p-value < 0.05 (Ordinary One-way ANOVA, Turkey’s multiple comparisons test).

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