Structural and functional studies reveal how a ubiquitous regulator of dynein keeps the microtubule-based motor in a persistent track-bound state.

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.

DCX negatively regulates dynein-mediated retrograde transport through two critical interactions by regulating dynein binding to microtubules and regulating the composition of dynein/dyactin/JIP3 motor complex.

Dynein bypasses obstacles on microtubules more efficiently than single kinesin, and kinesins overcome this limitation when transporting intracellular cargos in teams.

The dynein light intermediate chain is a member of the G protein superfamily and links the motor to several intracellular cargo adaptors.

In vitro reconstitution reveals how a system of molecules works together to transport the motor protein dynein to the start of its track.

DynAPs are liquid-like organelles that are partitioned into functional sub-domains.

Chaperoning defects in axonemal dynein subunits trigger proteostatic clearance of dynein motors opening up the possibility of trialling proteostasis modulators to treat the motile ciliopathy primary ciliary dyskinesia (PCD).

Structures of human cytoplasmic dynein-1 bound to its regulator LIS1 reveal the interfaces involved in forming the complex and provide a context for disease-linked mutations.

Evolution-guided functional analyses identify an activating adaptor of the dynein intracellular transportation machinery, NINL, as a novel component of the antiviral immune response and reveal a mechanism by which viruses antagonize NINL function in a species-specific manner.