Maya Schuldiner

The paper shows that Swe1 delays cell cycle progression when mitochondrial inheritance is impaired, helping maintain mitochondrial homeostasis in budding yeast.

This study identifies Vlf1 as a vacuolar lipophagy regulator in S. cerevisiae, showing its localization to the vacuole and interaction with Atg15, with effects on autophagy levels.

The paper identifies lysophosphatidylcholine (LysoPC) as a spatial regulator of DAG and sterols in yeast through a genome-wide screen and lipidomic analysis.

The paper identifies Pex9's role in regulating TORC2 during oxidative stress in yeast, revealing a non-canonical signaling pathway independent of Yap1 and Skn7.

The paper investigates the role of protein O-mannosylation in ERAD using yeast genome-wide screens, revealing it generates ERAD cues for misfolded proteins.

The paper develops hMultiCLEM, a high-resolution screening pipeline combining EM and multiplexed human cell pools to identify proteins affecting mitochondrial cristae shape, uncovering MISHA linked to Meniere's disease.

This study reveals the structural and functional role of Pex8 in peroxisomal cargo translocation by interacting with Pex5, facilitating receptor recycling.

The paper presents a cryo-EM structure of the EMC:Spf1 supercomplex, showing how it integrates TMD insertion and dislocation activities for membrane protein quality control.

This study identifies PEX39 as a cytosolic peroxin that facilitates PTS2-protein import by interacting with PEX7 and stabilizing its binding to cargo.

The paper creates a proteome-wide yeast library with HA tags to study protein function, size, abundance, and localization.

This study shows that Pex3 promotes peroxisome-peroxisome and peroxisome-lipid droplet contact sites in yeast and flies, independent of other known Pex3 partners.

The paper identifies an unconventional Pex5-Eci1 interaction interface that enables PTS1-independent peroxisomal import of Eci1 in yeast.

This study investigates how mitochondrial inner membrane remodeling drives organelle shape changes, linking cristae formation to mitochondrial morphology and function.

The paper profiles the LAM family of contact site tethers to understand their localization and function, revealing unique and shared roles through proximity labeling.

This study identifies Mpf1 as a novel factor influencing the dual targeting of tail-anchored proteins between mitochondria and peroxisomes in yeast.

The paper develops a pipeline to identify condition-specific enzymes in yeast, revealing a function for the uncharacterized Bdh2 alcohol dehydrogenase.

The paper introduces an AID library for on-demand protein depletion in yeast, enabling systematic study of protein function and uncovering new roles in cell cycle and mitochondrial processes.

This study identifies Yet3 as a protein that recruits sterol biosynthesis enzymes to ER contact sites, enabling on-demand sterol production and influencing organellar structure and function.

The paper identifies an amphipathic helix as a targeting motif for ER surface proteins in yeast and humans, showing its conservation and role in membrane localization.

The paper uses a bi-genomic split-GFP assay to identify mitochondrial matrix and inner membrane proteins, revealing 50 previously unvisualized proteins and characterizing dually localized proteins.

This study investigates the antifungal mechanism of cymoxanil, finding it disrupts plasma membrane potential and inhibits proton pumps in yeast, suggesting a mode of action involving membrane transport and acidification.

The paper develops ABOLISH, a method to reduce endogenous biotinylation in yeast, enabling more accurate detection of both stable and transient protein interactions using biotin ligases.

The paper shows that RNA-controlled shuttling of Xrn1 and its decay factors regulates mRNA synthesis and decay, revealing a novel nuclear-initiated cytoplasmic decay pathway.

The paper identifies Bfr1 as a regulator of Pmt1 and Pmt2 translation, affecting unfolded protein O-mannosylation in yeast.

The paper identifies a redox-sensitive site in Cdc48 that regulates its localization and activity during oxidative stress and aging in yeast.

The paper uses a split mDHFR PCA assay to assess how disease-causing mutations in OXPHOS complex I subunits affect their physical interactions.

The paper describes a yeast hybrid with increased growth rate and biomass yield under various conditions, but identifies genetic perturbations and regulatory disruptions associated with heterosis.