Alessandra Ferrari

Congratulations James!! So well deserved! 🎉🎉

Dietary control of peripheral adipose storage capacity through membrane lipid remodelling - Nature Metabolism Dietary n-6 PUFAs enhance adipose tissue expandability through the PPARγ–LPCAT3 membrane remodelling axis.

Excited to share Chapter #1 of our LPCAT3 journey in adipose biology and membrane dynamics—born of a rewarding, years-long, espresso-fueled partnership with Prof. Yuta Shimanaka @shimachu64.bsky.social. www.nature.com/articles/s42...

Cocrystal structure reveals the mechanism of FSP1 inhibition by FSEN1 | PNAS FSP1 is an FAD-dependent oxidoreductase that uses NAD(P)H to regenerate the reduced forms of lipophilic quinone antioxidants, such as coenzyme Q10 ...

Thrilled this paper is out! We solved the first cocrystal structure of FSP1 with an inhibitor (FSEN1), providing mechanistic insight & a foundation for medchem. Led by Amalia Megarioti & Sitao Zhang. A terrific collaboration with Da Jia.
Brief Skytorial!
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These projects were led by two amazing scientists, Marc Tol and YutaShimanaka.
We had such a great time being postdocs in the Tontonoz lab together! Now Marc and Yuta will keep shaping the field of lipid metabolism from the Netherlands and from Japan. Ad maiora!

Dietary control of peripheral adipose storage capacity through membrane lipid remodelling Complex genetic and dietary cues contribute to the development of obesity, but how these are integrated on a molecular level is incompletely understood. Here, we show that PPARγ supports hypertrophic ...

Check out two great preprints from the Tontonoz lab, linking LPCAT3-mediated phospholipid remodeling to dietary fat intake and cold response
www.biorxiv.org/content/10.1...
www.biorxiv.org/content/10.1...

Our lab is hiring 1 PhD and 1 Postdoc to study the mechanism of lipid transport using computational methods (Molecular Dynamics, AI). Fully funded by @snsf-ch.bsky.social for 4 years, with amazing collaborators and excellent life and working conditions. Apply by email. Please share and repost!

The bridge-like lipid transport protein VPS13C/PARK23 mediates ER–lysosome contacts following lysosome damage Nature Cell Biology - Wang et al. show the recruitment of the lipid channel protein VPS13C and formation of VPS13C-dependent contacts between endoplasmic reticulum and lysosomes after lysosomal...

"The bridge-like lipid transport protein VPS13C/PARK23 mediates ER–lysosome contacts following lysosome damage" out now in Nature Cell Biology
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