Ian G. Ganley

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

This study identifies NLRX1 as a druggable, CypD-independent regulator of mitochondrial permeability transition using chemical probes and genetic approaches.

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 shows that AMPK senses NAD levels, with NAD binding to the gamma subunit and modulating AMPK activity, which affects metabolic pathways like mTORC1 and autophagy.

The paper identifies a new mechanism of kinase inhibition through electrophilic modifications, revealing aspartate conjugation of ULK1 by a chloroacetamide warhead.

This study shows that activating AMPK reduces excessive mitophagy and restores mitochondrial function in FBXL4-related mitochondrial DNA depletion syndrome models.

This study identifies the mitochondria-lysosome axis as critical for maintaining the function of neonatal lysosome-rich enterocytes and preventing premature differentiation.

The paper identifies two mitophagy peaks during retinal development, one PINK1-independent and one PINK1-dependent, linked to oxidative stress and RGC differentiation.

This study shows antigen and cytokines repress autophagy in CD8 T cells, shaping mitochondrial function, migration, and effector machinery through differential proteome pruning.

This study examines PINK1-PRKN signaling in mice during aging, showing increased gene expression and enzymatic activity in multiple tissues, with the heart showing the most pronounced activation.

The paper shows that PINK1 loss reduces mitophagy in skeletal muscle, which is restored by a POLGD257A mutation, highlighting skeletal muscle as a model for studying PINK1-dependent mitophagy.

This study compares Type I and Type II LRRK2 inhibitors, showing Type II compounds are more potent against wild-type LRRK2 and fail to dephosphorylate specific biomarker sites, suggesting conformational selectivity.