Florian Fröhlich

This study uses lysosomal proteomics and knockdowns to analyze the cargo spectra of GARP and EARP complexes, revealing their distinct roles in protein trafficking and their links to neurodegenerative disorders.

This study reports cryo-EM structures of human ABCA2, revealing its cholesterol transport mechanism and novel conformational changes.

This study shows that Ire1-dependent Membrane Stress Responses (MSR) help yeast cells grow when inter-organelle contacts are disrupted by compensating for lipid metabolism defects and modulating Ca2+ signaling.

This study identifies VPS13C/PARK23 as a key protein involved in lysosomal repair by facilitating lipid transfer and membrane remodeling in response to damage.

The paper shows ESCRT proteins, specifically Snf7 and Bro1, organize stress-induced ER-Golgi contacts in yeast by forming tubular ER subdomains and recruiting tethering proteins.

This study shows lipid droplets are the site of VLCFA activation by Fat1, with Fat1 targeting LDs via an amphipathic helix and using a hydrophobic cavity to access substrates.

The paper identifies Ldm1 and Ldo16 as actin-dependent lipid droplet motility mediators in yeast, showing their roles in LD movement and mitochondrial transport.

The paper identifies steric repulsion as a mechanism regulating ER-to-LD protein movement, showing high-affinity proteins exclude lower-affinity ones during adipocyte differentiation.

This study determines the structure of the yeast ceramide synthase complex using cryo-EM, revealing its active state and inhibition mechanism by fumonisin B1.

The paper determines the cryo-EM structure of the SPT-Orm2 complex and shows Orm2 has higher inhibitory potential than Orm1, despite similar structures.

The paper solves the structure of the CORVET tethering complex using cryo-EM and explains its role in promoting endosome fusion through interactions with Rab5 and PI3P.

This study shows that serine uptake via Gnp1 is critical for maintaining sphingolipid homeostasis in yeast by linking serine import to sphingolipid biosynthesis.