Chris Lupton
@luptoncj.bsky.social
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📥 336
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#CryoEM
and structural biology at Monash University
Very well deserved! A great reward for a a lot of hard work 😊
add a skeleton here at some point
3 months ago
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reposted by
Chris Lupton
Mike Martynowycz
4 months ago
Seed to sub-Å! We just solved crambin at 0.85Å with
#MicroED
straight from spontaneous nanocrystals, phased ab-initio from a 5-res helix. Video shows diffraction ➜ ugly start map ➜ beautiful spheres. Preprint:
www.biorxiv.org/content/10.1...
#StructuralBiology
#CryoEM
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Awesome talk from
@bradleyspicer.bsky.social
telling us all about his work on insecticidal proteins. Very cool stuff!
#lorneproteins2025
8 months ago
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reposted by
Chris Lupton
Bradley Spicer
9 months ago
🚨 Save the Date! 🚨 I'm thrilled to announce the Prato Conference on Pore Forming Proteins, happening this June in the stunning city of Prato, Italy! 🙏 Please share or repost this to help us reach as many people as possible—especially those who would love to attend!
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reposted by
Chris Lupton
Chen Davidovich
9 months ago
We used cryoET and biophysical approaches in vitro together with molecular biology in differentiated cells to show that chromatin compacted by PRC1-CBX8 is porous and accessible while PRC1 is dynamic in it. 🧪🧬
#cryoET
#Epigenetics
#Polycomb
www.nature.com/articles/s41...
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Dynamic PRC1–CBX8 stabilizes a porous structure of chromatin condensates - Nature Structural & Molecular Biology
Here the authors show that a gene-inactivating protein complex packs inactive genes into a dynamic and accessible structure. The study challenges the traditional views that restricted accessibility an...
https://www.nature.com/articles/s41594-024-01457-6
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reposted by
Chris Lupton
Evan Healy
9 months ago
🧵 1/ We’re excited to share that our new paper with
@adrianbracken.bsky.social
lab is out 🎉 In this study (which began over 10 years ago!), we explore the biology of PRC2 and PRC1 in non-dividing cells. We also explore the effects of PRC2 inhibitor drugs on these cells. Here’s what we found👇
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Very cool! 😁
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11 months ago
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Great to see our work on the
#cryoem
structure of the human TSC:WIPI3 lysosomal recruitment complex! Awesome effort from co-authors
@charlesbj.bsky.social
and Laura D'Andrea with
@drellisdon.bsky.social
doing the heavy lifting leading the project.
www.science.org/doi/10.1126/...
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Structure of the human TSC:WIPI3 lysosomal recruitment complex
The complete TSC structure reveals how lysosomal targeting proteins and phosphoinositides coordinate mTORC1 inhibition.
https://www.science.org/doi/10.1126/sciadv.adr5807
11 months ago
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reposted by
Chris Lupton
Andrew Ellisdon
11 months ago
Our latest study is now online at Science Advances! We report the structure of the gigantic TSC:WIPI3 complex revealing new insights into lysosomal docking and dysregulation in disease.
#cryoEM
#mTOR
🧪
www.science.org/doi/10.1126/...
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reposted by
Chris Lupton
Andrew Ellisdon
about 1 year ago
Excited to see our latest study published! We report several structures of the intriguing LYCHOS (GPR155) protein revealing a chimeric structure of a GPCR and a PIN-like transporter domain
#cryoEM
#mTOR
#GPCR
#auxin
www.nature.com/articles/s41...
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LYCHOS is a human hybrid of a plant-like PIN transporter and a GPCR - Nature
Cryo-electron microscopy structures of the human lysosomal transmembrane protein LYCHOS show that it comprises a transporter-like domain fused to a G-protein-coupled receptor, and that the transporter...
https://www.nature.com/articles/s41586-024-08012-9
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reposted by
Chris Lupton
Charles Bayly-Jones
11 months ago
🚨 Our story on the TSC:WIPI3 lysosomal-recruitment complex is now live in Science Advances. Equal-first co-authors
@luptoncj.bsky.social
& Laura D'Andrea. Work lead by
@drellisdon.bsky.social
. Funding from
@deptofdefense.bsky.social
& Australian Research Council.
www.science.org/doi/10.1126/...
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reposted by
Chris Lupton
Charles Bayly-Jones
11 months ago
Another really nice highlight of our recent work. Arun et al raise interesting points about membrane cross talk and next-steps for LYCHOS.
www.cell.com/cell/abstrac...
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Bound by the love for cholesterol: A transporter meets a GPCR
In a recent issue of Nature, Bayly-Jones et al. report the cryo-EM structures of a lysosomal cholesterol sensor, LYCHOS, also known as GPR155, which reveals a unique fusion of a plant auxin-transporte...
https://www.cell.com/cell/abstract/S0092-8674(24)01215-7
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Very cool to see our work on the
#cryoEM
structure of LYCHOS as the Editor's Choice in Science Signalling! Thanks
@jffoley.bsky.social
!!
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11 months ago
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