Abstract

Dynactin and cargo adapter proteins dramatically increase the processive motility of human cytoplasmic dynein towards the microtubule minus end, but until now their effect on dynein's force generation remained unknown. Using an optical trap, we confirm that dynein alone is a weak motor and show that dynein's association with dynactin and BICD2N substantially increases its stall force. We propose that activated dynein complexes are strong motors that generate forces comparable to those of plus end-directed kinesins.

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