Extended Data Fig. 6: Lis1 reduces the stall force of the tail-truncated dynein.
From: Lis1 slows force-induced detachment of cytoplasmic dynein from microtubules
a) Representative trajectories of beads driven by tail-truncated dynein constructs dimerized with a Glutathione S-transferase (GST) tag (GFP-GST-Dyn331kDa and GFP-GST-Dyn314kDa) in the presence and absence of 300 nM Lis1. Assays were performed in 2 mM ATP. Red arrowheads represent the detachment of the motor from the microtubule followed by the snapping back of the bead to the trap center. b) Stall force histograms of Dyn331kDa and Dyn314kDa in the presence and absence of 300 nM Lis1 (mean ± s.e.m.; p = 2 × 10−7 for Dyn331kDa and 0.006 for Dyn314kDa, two-tailed t-test). c) Stall times of Dyn331kDa and Dyn314kDa in the presence and absence of 300 nM Lis1. Fitting to a double exponential decay (solid curves) reveals the weighted average of stall time (±s.e.).
