Jeeyun Chung

@jeeyunc.bsky.social

Assistant professor at Harvard MCB. Interested in lipid storage mechanisms and neuronal lipid metabolism. jeeyunchunglab.org

What do lipid droplets do in neurons? Thrilled to share the 🌟1st preprint from my lab, led by Eleni Katafygiotou, showing activity-dependent formation of neuronal LDs in vitro and in vivo, and the impact of LD modulation on neuronal function and behavior. #lipidtime www.biorxiv.org/content/10.6...

Activity-dependent lipid droplet biogenesis and turnover regulate synaptic integrity

Lipid droplets (LDs) are conserved organelles that buffer lipid storage and stress, yet their dynamics and functions in neurons remain largely unknown. Here, we report activity-dependent dynamics of n...

biorxiv.org

Happy to share our review of seipin as a lipid rheostat, not just a #lipiddroplet biogenesis factor. Its flexible structure, with cofactors and ligands, integrates metabolic cues at organelle contacts, coordinating lipid storage, membrane synthesis, and signaling. rupress.org/jcb/article/...

Seipin: A central lipid rheostat

Thiam and Carpentier review seipin as a conformationally dynamic lipid rheostat that steers lipid fate and preserves cellular metabolic balance.

rupress.org

Awesome paper and super useful resource of CRISPR-based screens to identify regulators of #LipidDroplet biology under different metabolic conditions: crisprlipid.org

James Olzmann@olzmannlab.bsky.social · 5mo ago

Sooo happy to share our new paper in @nature.com “CLCC1 promotes hepatic neutral lipid flux and nuclear pore complex assembly.” A terrific collaboration with @arrudalab.bsky.social, led by co–first authors Alyssa Mathiowetz and Emily Maymand. www.nature.com/articles/s41...

Cells come in many shapes and sizes, with diverse physiological functions. But how do #organelles and their interaction networks remodel during #differentiation of stem cells into different cell types? Here’s what we discovered about neuronal differentiation: 1/13

bioRxiv Cell Biology@biorxiv-cellbio.bsky.social · 6mo ago

Organelle communication networks rewire to support lipid metabolism during neuronal differentiation https://www.biorxiv.org/content/10.64898/2026.02.10.704675v1

Registration is open for the FASEB #LipidDroplet meeting in Scottsdale, July 26-30! This is THE premier North American conference on LDs, you do not want to miss it!

Henne lab@hennelab.bsky.social · 7mo ago

Interested in lipids? Join us @ the 2026 FASEB Lipid Droplet: From Mechanisms to Disease Conference (July 26-30, Scottsdale, AZ). Registration is now open! events.faseb.org/event/Lipid-... We are co-locating with the FASEB Phospholipids SRC! Register for one to enjoy BOTH meetings!

Fat storage in the body relies on specialized structures called lipid droplets. In a new Science study, researchers identified the microprotein adipogenin as a regulator of adipocyte lipid droplet size, revealing a key mechanism in lipid homeostasis. Learn more this week: https://scim.ag/4nFEGO7

Lipid droplet growth is orchestrated by the seipin complex, which provides a structural platform for droplet nucleation and expansion. The microprotein adipogenin fine-tunes seipin’s conformation, remodeling its architecture to regulate lipid storage capacity. This modulation results in the formation of fewer but larger lipid droplets, revealing a key mechanism in lipid homeostasis.

Zara Weinberg passed away earlier this week. She joined my lab earlier this year when her postdoc lab formally closed. She was a brilliant scientist, supportive mentor, dear friend, avid music fan, rabid believer in public transit, open science champion, and above all just an amazing human.

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I am excited to share our new preprint! Led by @laylanassar.bsky.social , we have found a new JIP4-dependent mechanism that controls the efflux of cystine from lysosomes. Our findings have implications for both lysosome biology and human disease: doi.org/10.1101/2025...

JIP4 deficiency causes a novel lysosome storage disease arising from impaired cystine efflux

Lysosomes break down macromolecules, clear cellular waste and recycle nutrients such as cystine. We describe a novel mechanism whereby JIP4 regulates lysosomal cystine storage by controlling the abundance of cystinosin (CTNS), the transporter responsible for lysosomal cystine efflux. To this end, JIP4, previously characterized as a motor adaptor and kinase signaling scaffold, suppresses TMEM55B-dependent ubiquitylation of CTNS. Loss of JIP4 reduces CTNS protein levels, leading to lysosomal cystine accumulation and lysosomal storage defects that phenocopy loss of CTNS in both human cells and the renal proximal tubules of JIP4 knockout mice. These phenotypes mirror cystinosis, the lysosomal storage disease caused by CTNS loss-of-function. Our findings thus reveal a fundamental process that controls the efflux of lysosomal cystine and has relevance to understanding human disease arising from JIP4 mutations. ### Competing Interest Statement The authors have declared no competing interest. NIH, AG085824, AG062210, R35GM150619 Michael J. Fox Foundation, https://ror.org/03arq3225, ASAP-000580

doi.org