Cytoplasmic dynein is involved in a diverse set of cellular functions including cargo transport and microtubule organization. Dynein's activity is controlled by regulatory proteins, such as Lis1 and Ndel1. In yeast, Lis1 facilitates plus-end tip localization of dynein. In vitro studies showed that Lis1 inhibits the motility of yeast cytoplasmic dynein, but the molecular mechanism of this regulation is not well understood. In this study, we studied the motility and force generation of Lis1-bound dynein at the single molecule level. We observed that Lis1 stably binds to dynein as it walks along a microtubule. One Lis1 dimer is recruited per motor domain of dynein. Dynein velocity decreases with the increasing stoichiometry of Lis1. Using an optical trap, we showed that Lis1 binding does not change the stall force of dynein, but it increases the stall duration. Lis1 binding also reduces the asymmetry in force-induced detachment of dynein from the microtubules regardless of its interaction with dynein's coiled-coil stalk.