Maja Radulovic
@majarad.bsky.social
Project leader at Dept. of Molecular Cell Biology/Stenmark lab, Oslo University Hospital 🧪🔬 https://www.ous-research.no/home/stenmark/Group%20members/16509
A TBK1/ULK1 signalling axis couples lysosomal stress to TFEB activation www.nature.com/articles/s41...
A TBK1/ULK1 signalling axis couples lysosomal stress to TFEB activation - Nature
Proteomic and phosphoproteomic analyses of lysosomes identify a nutrient-independent regulatory arm of mTORC1 signalling that mediates lysosomal adaptation to stress and whose deregulation underl...
nature.com
Hey! Submit your papers, and spread the word, this will be great! Thanks for inviting us @jcellsci.bsky.social and great to work with @pihanson.bsky.social on this issue!
Journal of Cell Science@jcellsci.bsky.social · 2w agoOur second special issue for 2027 will focus on the topic of membrane dynamics and repair. We invite you to submit your latest research to this issue, which will be coordinated by our Guest Editors @jezcarlton.bsky.social and @pihanson.bsky.social. journals.biologists.com/jcs/pages/me...
☕ @majarad.bsky.social et al. show that phosphatidylinositol 3-phosphate (PI3P), produced by the phosphatidylinositol 3-kinase PIK3C3, is formed on ER domains after lysosome damage. ER domain PI3P helps to recruit the ATPase DFCP1, which promotes lysosome repair. www.nature.com/articles/s41...
DFCP1-containing ER microdomains mediate lysosomal membrane repair - Nature Cell Biology
Radulovic et al. show that phosphatidylinositol 3-phosphate (PI3P), produced by the phosphatidylinositol 3-kinase PIK3C3, is formed on ER domains after lysosome damage. ER domain PI3P helps to recruit...
nature.com
Our study on DFCP1 and lysosome membrane repair is live! We uncover a previously unrecognized role for omegasomes in the cellular response to lysosomal membrane damage, revealing another layer of regulation in how damaged lysosomes are repaired. www.nature.com/articles/s41...
DFCP1-containing ER microdomains mediate lysosomal membrane repair - Nature Cell Biology
Radulovic et al. show that phosphatidylinositol 3-phosphate (PI3P), produced by the phosphatidylinositol 3-kinase PIK3C3, is formed on ER domains after lysosome damage. ER domain PI3P helps to recruit...
nature.com
The ULK1 complex triggers autophagy on membranes, but with no typical membrane binding domains, how does it get there? See the answer in a brilliant collective effort out now in Science Advances: www.science.org/doi/10.1126/....
Very proud to see this paper out. This is an incredible collaboration with the labs of Wes Sundquist and Adam Frost. @uofubiochem.bsky.social @kingslsm.bsky.social www.nature.com/articles/s41...
ESCRT-III assembles around mis-segregated DNA to protect genome stability - Nature Structural & Molecular Biology
The authors show that persistent ultrafine DNA bridges become coated by membranes and the ESCRT-III proteins CHMP1B and IST1, which protect the genome within from damage.
nature.com
Endolysosomal damage promotes intraluminal protein condensate formation that limits cytosolic leakage https://www.biorxiv.org/content/10.64898/2026.05.25.726725v1
We offer a PostDoc position for a fully funded project on lipid-encoded #lipidtime protein quality-control checkpoints at the Golgi: great collaborators, excellent working & living conditions & benchspace with a view ;) Please share and repost!
Glad to share our new @cp-trendscellbio.bsky.social article! We discuss how repair condensates and lipid domains work together to restore lysosome integrity or deciding if it's time for lysophagy. #Lysosomes #Condensates #DamageSignature #Lipids #Ions Check it out: doi.org/10.1016/j.tc...
LLOMe has long been used to study lysosomal damage, yet how it works has remained a mystery. Using cryo-electron tomography, we show it forms amyloid structures inside lysosomes that mechanically rupture membranes – revealing a new paradigm for lysosomal failure. 🔗 doi.org/10.64898/202... #CryoET
In a new publication, Team Harper found that α-synuclein fibrils cause ESCRT-III loss through “collateral degradation,” weakening endolysosomes and promoting further aggregation🔬 🔗 Read the full #publication: bit.ly/4iPUayj
Grateful to @focalplane.bsky.social for inviting us to write about our last paper on lysosomal tubulation during the stress response (rupress.org/jcb/article/...)! focalplane.biologists.com/2025/12/11/d...
Damage done, tubules on - Studying membrane damaged-induced lysosomal tubulation - FocalPlane
Damage done, tubules on - Studying membrane damaged-induced lysosomal tubulation - Default
focalplane.biologists.com
Autolamellasomes: An Autophagy-Dependent Parallel Pathway for Bulk ER Degradation and Lysosome Biogenesis https://www.biorxiv.org/content/10.1101/2025.11.16.688694v1
Please RT. Post-doc opportunity alert! 💥 closing 10th December.. Come join our team (www.thelowlab.org) at Imperial, London, working on the structure and mechanism of bacterial secretion systems. For more details and to apply please see www.imperial.ac.uk/jobs/search-...
Lipid Landscape of human cells https://www.biorxiv.org/content/10.1101/2025.10.05.680593v1
VPS13C/PARK23 initiates lipid transfer and membrane remodeling for efficient lysosomal repair https://www.biorxiv.org/content/10.1101/2025.10.23.684214v1
🚨 We’re hiring a postdoc! 🚨 Interested in lysosomes, Parkinson’s disease, cell biology, microscopy — or all of the above? Come work with us at the Bonet-Ponce Lab! Reach out directly: luis.bonetponce@osumc.edu Learn more: bonetponcelab.com Let’s chat!
ER exit sites are dynamic ER subdomains that integrate signals, reshape membranes and steer secretion. Twelve groups in the field came together to map their diversity, regulation, unanswered questions and future directions. www.nature.com/articles/s41...
Towards a unified framework for the function of endoplasmic reticulum exit sites - Nature Reviews Molecular Cell Biology
Endoplasmic reticulum exit sites (ERES) are specialized ER subdomains that regulate the export of secreted cargo. This Roadmap explores how ERES integrate biochemical and mechanical signals to coordinate trafficking and proposes a multidisciplinary strategy to investigate their function, including in disease.
nature.com
Much needed good news!! Our paper is just out in @jcb.org. We found a crazy antagonistic motor function that explains the elongation/retraction phenotype we see during LRRK2-dependent lysosomal tubulation. I am especially proud of Tsion, Nuria, Mia and Irene's contribution. Check it out!
Journal of Cell Biology@jcb.org · last yr.@lysoluis.bsky.social, @markrcookson.bsky.social et al. show how two distinct pRAB effectors and RHD members, JIP4 and RILPL1, provide antagonistic motor force to regulate #lysosome tubulation. rupress.org/jcb/article/...
Happy to share an exciting study from Yihong Ye’s lab at NIH, with a minor contribution from our lab: ceroid lipofuscinosis-4 (CLN4)-linked DNAJC5 mutations cause lysosomal damage as a driver of neurodegeneration in iPSC-derived neurons. CHIP safeguards lysosomes via microautophagy 👉 rdcu.be/eChof
CHIP protects lysosomes from CLN4 mutant-induced membrane damage
Nature Cell Biology - Lee et al. use an aggregation-prone CLN4 mutant that causes lysosomal damage in neurons and show that in non-neurons, the ubiquitin ligase CHIP prevents CLN4-dependent...
rdcu.be
LYVAC/PDZD8 is a lysosomal vacuolator | Science www.science.org/doi/10.1126/...
LYVAC/PDZD8 is a lysosomal vacuolator
Lysosomal vacuolation is commonly found in many pathophysiological conditions, but its molecular mechanisms and functions remain largely unknown. Here, we show that the endoplasmic reticulum (ER)–anch...
science.org
Nature research paper: Quantitative imaging of lipid transport in mammalian cells go.nature.com/4mmSygd
Quantitative imaging of lipid transport in mammalian cells - Nature
Directional, non-vesicular lipid transport is responsible for fast, species-selective lipid sorting into organelle membranes.
go.nature.com
Interested in lysosome damage and repair pathways? Check out the latest updates.
Nature Reviews Molecular Cell Biology@natrevmcb.nature.com · last yr.New Online! Lysosomal membrane homeostasis and its importance in physiology and disease
Announcing a new @embo.org Workshop on "Intracellular mechanics and organelle mechanobiology" that we are organizing with Michael Krieg and Verena Ruprecht at @icfo.eu (Barcelona) on 16-20 February, 2026. Please, repost and spread the word! 🙏 #EMBOmechanobio meetings.embo.org/event/26-org...
Intracellular mechanics and organelle mechanobiology
Mechanobiology is an interdisciplinary field that emerges at the cross-section of biology, physics and engineering. It aims to understand how living cells, tissues and animals sense and respond to me…
meetings.embo.org
What a fantastic ESCRT meeting, the field is going strong and full of exciting science. Many thanks to @rouxlab.bsky.social @cellarchlab.com @jujumathieu.bsky.social @magromayor.bsky.social @majarad.bsky.social for organising such a a great event
The ESCRT complexes are a fascinating membrane cutting machine with roles in countless cell pathways, but they are also ubiquitous in disease and offer new opportunities as drug targets. See our new review with Alyssa Coyne, Marta Miączyńska, and Harald Stenmark at tinyurl.com/yex3trem
The expanding repertoire of ESCRT functions in cell biology and disease - Nature
This Review examines recently gained insights into the roles of ESCRT complexes in viral infection, immunity, cancer and neurological disease.
tinyurl.com
A short reminder that registrations for the EMBO ESCRT meeting 2025 in Montreux June 23rd-June27th are still opened! Please register online at meetings.embo.org/event/25-escrt
ESCRT function, evolutionary diversity and mechanism of action
The ESCRTs (Endosomal Sorting Complexes Required for Transport) were discovered in 2002 and became one of the most dynamic fields of research in membrane cell biology. ESCRTs are protein complexes fo…
meetings.embo.org
