Jeeyun Chung

Congratulations 🤩🥳

CLCC1 promotes hepatic neutral lipid flux and nuclear pore complex assembly - Nature CRISPR–Cas9 screening identifies CLCC1 as a factor that increases neutral lipid flux to prevent hepatic steatosis and promotes nuclear pore complex assembly by promoting membrane bending and fusi...

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...

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

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

Membrane editing with proximity labeling reveals regulators of lipid homeostasis - Nature Chemical Biology Coupling an optogenetic lipid-modifying enzyme with proximity labeling reveals protein networks and mechanisms regulating lipid homeostasis in the membranes of target organelles.

Thrilled to share our latest study, led by @reikatei.bsky.social, in @natchembio.nature.com! We began by asking a simple question—how do cells know if they have too much of a lipid in a particular membrane, and how do they respond to rectify this imbalance?
www.nature.com/articles/s41...
More info 👇

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!

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!

ExoSloNano: multimodal nanogold labels for identification of macromolecules in live cells and cryo-electron tomograms - Nature Methods The ExoSloNano system facilitates nanogold probe-based labeling of specific proteins of a wide range of sizes in live cells for cryo-electron tomography and correlative light and electron microscopy s...

ExoSloNano: nanogold probe-based labeling of proteins in live cells for cryo-ET and CLEM. @lindseynyoung.bsky.social @thevillalab.bsky.social

www.nature.com/articles/s41...

The new version of TrackMate, the v8.1 has just been released. It builds upon the recent v8, linked below, and offers two main improvements 👇

I am thrilled to share our latest work led by @zurisullivan.bsky.social in collaboration with @moffittlab.bsky.social ! We find that the brain encodes distinct, pathogen-specific sickness states across behavior, physiology, neural activity, and gene expression 1/6

www.biorxiv.org/content/10.6...

Our red calcium indicator, FRCaMPi, and its soma-localized version, SomaFRCaMPi, are now available from @addgene.bsky.social in various vectors, along with all the sensors used for benchmarking. www.addgene.org/browse/artic...

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.

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

Adipogenin promotes the development of lipid droplets by binding a dodecameric seipin complex The microprotein adipogenin (Adig) is predominantly expressed in adipose tissues. Here, we found that Adig interacts with seipin to form a stable, rigid complex. We present the structure of the seipin...

New paper in Science identifying adipogenin as a critical seipin regulator in LD biogenesis. So glad our lab could help a little in this monumental study. Congrats to all authors!

www.science.org/doi/10.1126/...

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.

I am extremely grateful and deeply honored to be conferred the new title of Xander University Professor by @harvard.edu
🙏
🧠🧪🧬

A new, nerdy paper. We figured out (some) of the rules underlying cell-permeability of probes and designed ligands that light up, grab, and move proteins around. Awesome @hhmijanelia.bsky.social x @uwmadison.bsky.social x @stjuderesearch.bsky.social collaboration! www.pnas.org/doi/10.1073/...

During these uncertain times, I’m very happy to see that my institution, @scripps.edu has an open tenure-track Assistant Professor position. Any field in Chemistry or Biology is welcome. I’d especially love to see fellow neuroscientists apply. Please repost!

apply.interfolio.com/174756

🌟 Thrilled to share that my lab’s first publication is now out in @natmetabolism.nature.com. Congrats to the team 🎉

🧠 We discovered that neurons use endogenous fatty acids as an energy fuel, challenging long-standing models of sugars being the exclusive energy source for neurons. 1/3

Wonderful to see our paper on the #organelle signatures of #neurons and #astrocytes out in final form - congratulations, Shannon Rhoads and team!🎉 t.co/BPxKlbU6Ou

Our protocol for gene editing is online and all plasmids are on @addgene.bsky.social! CRISPR away everybody and get in touch if you need anything 🤩

Neural Circuit and Molecular Mechanism Underlying Social Hierarchy Identified - Harvard University - Department of Molecular & Cellular Biology The formation of social hierarchies is a fundamental aspect of group living, reducing conflict and guiding behavior across species—from animals to humans. Yet, the precise neural and molecular […]

Neural Circuit and Molecular Mechanism Underlying Social Hierarchy Identified 🧠 🧪🧬 🔬 #AcademicSky #higherEd
www.mcb.harvard.edu/department/n... @dulaclab.bsky.social @neurovenki.bsky.social @naoshigeuchida.bsky.social @cellpress.bsky.social ss.bsky.social‬ @harvardbrainsci.bsky.social

Congratulations Sarah 🤩🥳

Yay, congrats 🥳

Thrilled to share a new preprint! 📝 🎉 Lewis lab PhD student Casadora wondered: Do mtDNA synthesis and lipid droplet biogenesis co-occur at the same membrane contact sites? Or can we discern distinct ER-mito contact classes? Evidence suggests the latter, relevant in overnutrition!

Congratulations Jeremy 🥳

Huge thanks to @gthibault.bsky.social and Julie Hollien for organizing a warm, welcoming FASEB ER meeting filled with incredible science! Excited that I will carry the torch as a co-organizer for the 2027 meeting….can’t wait! @faseborg.bsky.social

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

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...

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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Congratulations James! 🥳

Congratulations!!!!