p25 and its associated dynactin complex are important for the physical interaction between dynein and early endosomes. (A) Although S-tagged dynein IC was able to pull down GFP-RabA in wild-type extracts in the absence of detergent, the amount of pulled-down GFP-RabA in Arp1-depleted extracts was significantly decreased. (B) A quantitative analysis of the Western results. All the values were relative to wild-type values, which were set as 1. Mean and standard deviation values were based on results from three independent pull-down experiments (P < 0.001). (C) The protein levels of GFP-RabA in the wild type and alcA-Arp1 extracts were similar before the pull-down assay. (D) Although S-tagged dynein IC was able to pull down GFP-RabA in wild-type extracts in the absence of detergent, the amount of pulled-down GFP-RabA in Δp25 extracts was significantly decreased. (E) A quantitative analysis of the Western results. All the values were relative to wild-type values, which were set as 1. Mean and standard deviation values (error bars) were based on results from three independent pull-down experiments (P < 0.001). (F) The protein levels of GFP-RabA in the wild-type and Δp25 extracts were similar before the pull-down assay.