A 3.1 Å structure of cytoplasmic dynein-1 in complex with its regulator Lis1 reveals the interfaces between dynein and Lis1, all of which are important for dynein function in vitro and in vivo.

Unlike other cytoskeletal motors that produce torque in a specific direction, cytoplasmic dynein generates torque in either direction, resulting in bidirectional helical motility along microtubules.

Using a proximity-dependent labeling approach in living cells, the human cytoplasmic dynein-1 interactome was identified and a new family of dynein activators, ninein and ninein-like, was discovered.

The motor domains of dynein are sufficient to crosslink microtubules and slide them antiparallel to each other.

Cortical dynein performs bulk cytoplasmic transport by gliding microtubules along the cell cortex and through the ring canals to the oocyte.

The combinatorial assembly of different adaptor complexes is a mechanism that dynein uses to interact with multiple cargos.

Analyses of the chemical structure of ciliobrevins led to dynein inhibitors with improved properties and higher potency.

Relion was used to solve structures of microtubules decorated with dynein microtubule-binding domains revealing that an axonemal dynein distorts the microtubule cross-sectional curvature.

During cilium-generated signaling, ciliary membrane protein trafficking is unidirectional and ciliary membrane protein composition is regulated through action in the cytoplasm of the retrograde intraflagelllar transport (IFT) motor and shedding of ciliary ectosomes.

A mutagenesis screen in budding yeast sheds light on dynein regulation and function, and reveals the molecular basis for disease in patients suffering from neuropathies caused by dynein dysfunction.