πππ’ππ§ππ£ππ¨ ππ£π π©ππππ§ π‘ππ₯πππ¨ ππ£π π₯π§π€π©πππ£π¨ ππ£ π€π§πππ£ππ‘π‘π πππ€πππ£ππ¨ππ¨ - Spetses, Greece - May 2026 | Utrecht University
Utrecht University
CALLING PHDs AND POSTDOCS! Apply for the 20th FEBS/EMBO summer school on Membranes lipids & proteins in organelle biogenesis! Spend a glorious week with leaders in the field on the beautiful island of Spetses in Greece this May. Registration: spetses2026.sites.uu.nl @embo.org @febspress.bsky.social
20.02.2026 11:16
π 11
π 10
π¬ 0
π 1
I just checked in at @keystonesymposia.bsky.social #KSMembrane2026 #KSAutophagy2026 Looking forward to it!
03.02.2026 00:18
π 4
π 1
π¬ 0
π 0
Cathepsin CβCatalyzed Ligation Generates Intralysosomal Amyloid Fibrils from Dipeptide Esters
Amyloid fibril-associated endolysosomal dysfunction is implicated in multiple neurodegenerative diseases. We report the rapid generation of intralysosomal amyloid fibrils by simply treating cells with certain dipeptide methyl esters. Cathepsin C mediates the ligation of dipeptides into oligopeptides that, sequence-dependently, self-assemble into amyloid fibrils. Progressive fibril growth, not fibril deposition, mediates lysosomal membrane permeabilization. Cryo-electron tomography studies reveal intralysosomal fibrils and broken lysosomal membranes upon dipeptide treatment. Certain oligopeptide fibril structures are competent to cross-seed the aggregation of neurodegeneration-associated Tau(P301S) at lysosomal sites. Similarly, the degree of lysosomal membrane permeabilization and ESCRT-repair response can be tuned with dipeptide sequence variation. The presented Cathepsin C-dependent amyloid fibril formation approach lends itself toward the development of novel tools to further probe lysosomal biology and pathobiology. ### Competing Interest Statement The authors have declared no competing interest. National Institute on Aging, https://ror.org/049v75w11, RF1AG073418 National Center for Advancing Translational Sciences, https://ror.org/04pw6fb54 Department of Education, USA, P031S240270 Freedom Together Foundation Chan Zuckerberg Initiative (United States), CZII-2023β327779 George E. Hewitt Foundation for Medical Research
www.biorxiv.org/content/10.6...
20.01.2026 15:37
π 1
π 0
π¬ 0
π 0
Cathepsin-dependent amyloid formation drives mechanical rupture of lysosomal membranes
Lysosomal membrane integrity is essential for cellular homeostasis, and its failure drives lysosomal storage disorders (LSD) and neurodegeneration. The dipeptide L-leucyl-L-leucine methyl ester (LLOMe) is widely used to model lysosomal damage, yet its mechanism remains poorly understood. The prevailing view holds that LLOMe polymerizes into membrane-permeabilizing peptide chains within the lysosomal lumen. Using cryo-electron tomography in cultured cells and primary neurons, we visualized the structural basis of LLOMe-induced lysosomal damage. We reveal that LLOMe forms amyloid structures within lysosomes that directly interact with and rupture the limiting membrane through mechanical stress. In vitro reconstitution confirms this amyloid-mediated mechanism. These findings establish a structural paradigm for lysosomal membrane disruption and provide insights into how disease-relevant protein aggregates, implicated in neurodegeneration and LSD, may compromise lysosomal integrity. ### Competing Interest Statement J.W.H. is a co-founder of Caraway Therapeutics, a subsidiary of Merck & Co., Inc., Rahway, NJ, USA (Caraway) and is a scientific advisory board member for Lyterian Therapeutics. Aligning Science Across Parkinson's, https://ror.org/03zj4c476, ASAP-000350, ASAP-000282, ASAP-024268 Boehringer Ingelheim Fonds, https://ror.org/00dkye506 Deutsche Forschungsgemeinschaft, https://ror.org/018mejw64, GRK 2566/1 Pew Scholars Program NIH Common Fund, https://ror.org/001d55x84, RF1NS125674, R01NS110395 Fred and Joan Goldberg Post-doctoral Fellowship European Research Council, 101041982
www.biorxiv.org/content/10.6...
20.01.2026 15:37
π 2
π 0
π¬ 0
π 0
How does cytoplasmic crowding affect reaction rates? doi.org/10.1016/j.mo...
31.12.2025 07:34
π 2
π 0
π¬ 0
π 0
Organelles harbour pH gradients https://www.biorxiv.org/content/10.64898/2025.12.12.694065v1
16.12.2025 22:32
π 11
π 6
π¬ 0
π 1
Interested in an interdisciplinary PhD program at the intersection of cell biology, biophysics, and chemistry?
Please check out the available projects at Nanyang Technological University Singapore IDMxS, and feel free to reach out if you are considering applying! idmxs.org/opportunitie...
30.11.2025 11:03
π 2
π 0
π¬ 0
π 0
π― shoutout for this beautiful work by Kenji Maedaβs lab, who mapped 300 lipid species across 6 compartiments of humane cells. Besides uncovering general principles of lipid organization, the paper establishes a framework for exploring how lipid landscapes are regulated in physiology and disease ππΌ
26.10.2025 11:03
π 9
π 4
π¬ 0
π 0
New paper - MAPL strikes again! Interested in mitochondrial signalling, inflammation, lysosome biology, pyroptosis, and Parkinson's disease? Have a look, there's something for everyone! Feeling grateful! @mitocollier.bsky.social Funded by #CIHR, @asapresearch.parkinsonsroadmap.org.
rdcu.be/eKKz1 π¨π¦
14.10.2025 11:50
π 67
π 22
π¬ 4
π 3
The stunning results have to be credited to my great former and current group members!
@mpici.bsky.social @mangiarotti.bsky.social
30.09.2025 09:49
π 13
π 2
π¬ 0
π 0
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!
24.09.2025 15:49
π 12
π 6
π¬ 1
π 0
Bioimage Analysis Specialist | King's College London
BioImage analysis friends - King's are recruiting for a full-time, permanent facility position! Come and work with fun microscopes and fun people (and me!) - please share! www.kcl.ac.uk/jobs/126345-...
29.09.2025 09:48
π 63
π 79
π¬ 0
π 0
Membrane Dynamics, Repair and Disease | Keystone Symposia
Join us at the Keystone Symposia on Membrane Dynamics, Repair and Disease, February 2026, in Keystone, with field leaders!
Deadlines are approaching for @keystoneSymposia.bsky.social #Membrane Dynamics, Repair & Disease, this February in Keystone! See scholarship, abstract and discount reg dates: keysym.us/KSMembrane26 #KSMembrane26
05.08.2025 12:26
π 3
π 1
π¬ 0
π 0
Membrane Dynamics, Repair and Disease | Keystone Symposia
Join us at the Keystone Symposia on Membrane Dynamics, Repair and Disease, February 2026, in Keystone, with field leaders!
I'm excited to speak at @keystoneSymposia.bsky.social #Membrane Dynamics, Repair & Disease, this February! Join me to explore emerging research in Keystone! keysym.us/KSMembrane26 #KSMembrane26
05.08.2025 12:25
π 1
π 1
π¬ 0
π 0
Postdoc (4 years π€) Fellowship Alert! π¬ Are you a computational biologist passionate about cellular biology and quantitative live-cell imaging? Get in touch to learn more and apply! Full details in the attached flyer.
01.08.2025 08:51
π 0
π 0
π¬ 0
π 0
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...
09.06.2025 13:35
π 21
π 6
π¬ 1
π 0
