J. P. Gillies

HIV-1 binds dynein directly to hijack microtubule transport machinery

This study shows HIV-1 directly binds dynein to hijack microtubule transport for motility, bypassing traditional cargo adaptors.

Ndel1 modulates dynein activation in two distinct ways

This study identifies two distinct mechanisms by which Ndel1 inhibits dynein activation in vitro, contrasting with its role in promoting dynein activity in cells.

Lis1 binding regulates force-induced detachment of cytoplasmic dynein from microtubules

This study shows Lis1 binding to dynein affects force-induced detachment asymmetry and slows dynein movement without altering stall forces.

The KASH5 protein involved in meiotic chromosomal movements is a novel dynein activating adaptor

The paper identifies KASH5 as a dynein activating adaptor essential for meiotic chromosomal movements, showing it binds dynein and enables processive motility.

Structural Basis for Cytoplasmic Dynein-1 Regulation by Lis1

This study presents the first high-resolution structure of the yeast dynein-Lis1 complex, revealing molecular interactions essential for Lis1's regulation of dynein function across species.

Lis1 promotes the formation of maximally activated cytoplasmic dynein-1 complexes

This paper identifies Lis1's role in forming maximally activated dynein complexes by binding to dynein's motor domain, enhancing microtubule binding and velocity.