James H. Hurley

This study determines the structure of DFCP1 and shows it forms a barrier that concentrates PI3P for lysosomal repair.

The paper investigates how mitochondrial architecture changes during mtRNA surveillance failure, revealing stress body formation and spatial reorganization of mitochondrial components.

This study identifies a stepwise pathway for ULK1 recruitment to membranes during autophagy, involving WIPI proteins and a PVP motif in ULK1.

This paper determines the cryo-EM structure of the PI3KC3-C2 complex with Rubicon's PIKBD domain, revealing how Rubicon selectively inhibits PI3KC3-C2 to regulate endolysosome maturation and mitophagy.

This study investigates the role of lysosomal components in tau seeding and finds that the PITT pathway and VPS13C are strongly involved in tau spread, while CASM and ALG-2 have more limited roles.

This paper determines the crystal structures of DFCP1's ATPase domain with ADP and ATP analogues, revealing structural elements that regulate ATP hydrolysis and omegasome dynamics.

This study determines the cryo-EM structure of mTORC1 on the lysosomal membrane, showing how growth factor and nutrient signals integrate through three-step recruitment and membrane engagement.

Cryo-ET of Parkin-expressing U2OS cells shows oligomycin/antimycin depolarization moves some ATP synthase to the inner boundary membrane, abolishes matrix calcium granules, and favors closed prohibitin domes.

The paper challenges a previously proposed structure of the prohibitin complex by showing that symmetry assumptions led to incorrect modeling of an asymmetric conformation.

The paper reveals how HIV-1 Nef modulates AP-1 trimerization through cargo dynamics and phosphorylation to regulate tetherin and MHC-I downregulation.