John P. Gillies

The paper shows that Pericentrin contains an internal sequence that directly activates dynein for co-translational transport, challenging the notion that dynein relies solely on N-terminal adaptors.

This study engineers synthetic cargo adaptors to investigate how they modulate dynein activation and transport properties in vitro and in cells.

This study identifies occludin's role as a dynein adaptor regulating vascular permeability and collateral angiogenesis through phosphorylation-dependent trafficking.

This study identifies KIF5B as a key component of the force-generating machinery for meiotic chromosome movements, interacting with the KASH5-LINC complex.

The paper identifies CCSer2 as a protein that gates dynein activity at the cell periphery by inhibiting its regulator Ndel1, enabling spatially restricted dynein activation.

The paper investigates how different cargo adaptors influence the kinetics and mechanism of dynein-dynactin complex formation, revealing distinct assembly pathways and stable tripartite complexes.