Fig. 4: Interactions of p62-PB1 with other PB1 domain proteins.
From: Structural basis of p62/SQSTM1 helical filaments and their role in cellular cargo uptake
a Quantitative determination of PB1-binding affinities by isothermal titration calorimetry. Data represent mean and standard deviations from three independent experiments. b Representative electron micrographs of negatively stained p62-PB11–122 (left) incubated with human NBR1–PB1 (right). c Quantification of lengths of P62-PB11–122 filaments before and after incubation with NBR1–PB1. Source data are provided as a Source Data file. d Co-sedimentation assays of p62-PB11–122 with NBR1–PB1, PKCζ–PB1, MEK5–PB1, and MEKK3–PB1 (S = supernatant; P = pellet). Control experiments of p62-PB11–122 and the respective PB1 interactor alone are also shown. Source data are provided as a Source Data file. e Representative electron micrographs of negatively stained p62-PB11–122 with nanogold-labeled NBR1–PB1, PKCζ–PB1, MEK5–PB1, or MEKK3–PB1. f Quantification of p62-PB11–122 filaments displaying one or two nanogold-labeled PB1 interaction domains. Source data are provided as a Source Data file.
