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. 2024 Jan 1;33(1):e4840. doi: 10.1002/pro.4840

FIGURE 3.

FIGURE 3

Role of PB1 and ZZ domains of p62/SQSTM1 on the interaction with LC3B using AlphaScreen. (a) Deletion of the UBA domain does not affect the total binding of the protein to LC3B, although the different shape of the curves could indicate a modest contribution to binding. (b) Deletion of the PB1 domain results in decreased interaction with LC3B. (c) Mutations at either side of the PB1 domain renders proteins with increased interaction with LC3B. (d) Deletion of the PB1 and ZZ domains vastly enhances interaction with LC3B. (e) Disruption of the ZZ domain by mutagenesis of key cysteines residues enhances interaction with LC3B. (f) Phosphorylation‐mimicking mutation at Thr138 renders a protein with increased interaction with LC3B. The data are representative of two independent experiments.