Abstract
Lissencephaly-1 (Lis1) is a key cofactor for dynein-mediated transport towards the minus-ends of microtubules. Recent studies have shown that Lis1 facilitates formation of processive dynein/dynactin/cargo adaptor complexes, but it is not required for subsequent motility. When Lis1 remains bound to the complex, it substantially slows down dynein motility, but the underlying mechanism is not well understood. To address this question, we studied the motility and force generation of yeast cytoplasmic dynein in the presence of Lis1.
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