Juan Ortiz Mateu

Providing order amongst constant traffic: #LMBResearch from Sean Munro (@cellbiol-mrclmb.bsky.social) with John Briggs (@mpibiochem.bsky.social) reveals how GOLPH3 allows COPI vesicles to distinguish between Golgi residents & ER-bound proteins.
Read more: www2.mrc-lmb.cam.ac.uk/protein-sort...

Elaborate machinery for inserting proteins into the outer membrane of bacteria Bacteria in the gut use an unusual molecular apparatus to insert complex proteins into their outer membrane.

Elaborate machinery for inserting proteins into the outer membrane of bacteria www.nature.com/articles/d41...

The human ribosome modulates multidomain protein biogenesis by delaying cotranslational domain docking - Nature Structural & Molecular Biology By studying dynamic folding intermediates on the human ribosome, Pellowe et al. show that newly made domains help each other to fold but do not stably interact until synthesis is complete, avoiding in...

Our article on human multidomain protein biogenesis is now published in @natsmb.nature.com
www.nature.com/articles/s41...

27 simulations of capturing hundreds of lipid scrambling events reveal mechanisms of lipid translocation.

However, according to reviewers, more evidence is needed on outside-the-groove scramblase activity.
buff.ly/LTxy4yX

Exciting to see our protein binder design pipeline BindCraft published in its final form in @Nature ! This has been an amazing collaborative effort with Lennart, Christian, @sokrypton.org, Bruno and many other amazing lab members and collaborators.

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

A multichaperone condensate enhances protein folding in the endoplasmic reticulum - Nature Cell Biology Leder et al. show that the chaperones PDIA6, Hsp70 BiP, ERdj3, PDIA1 and Hsp90 form co-condensates within the endoplasmic reticulum, enhancing folding and preventing misfolding of client proteins.

💫NEW: @annaleder.bsky.social et al. show that the chaperones PDIA6, Hsp70 BiP, ERdj3, PDIA1 and Hsp90 form co-condensates within the endoplasmic reticulum, enhancing folding and preventing misfolding of client proteins. @masgu.bsky.social @hillerlab.bsky.social
bit.ly/47b3Mjk

Out today in @nature.com: Together with the Honigmann, Shevchenko, Drobot and Hof labs, we present a general workflow for imaging the localization and transport of individual lipids in cells and mapping their metabolism.
www.nature.com/articles/s41...

Check out our new preprint on the discovery of a molecular switch in NAC that mediates nascent chain sorting on the ribosome and prevents mitochondrial protein mistargeting by SRP. A great collaboration with the Shan Lab @Caltech and the Qi Lab @UVA: www.biorxiv.org/content/10.1...

Very excited to announce that my first, first author paper, is now on BioRxiv! In this paper we unambiguously show #COPII coated vesicles in unperturbed human cells for the very first time!!

Make my day and check it out!
www.biorxiv.org/content/10.1...

#Cryo-ET #TeamTomo #Cryo-CLEM ❄️🔬❄️🔬❄️🔬❄️🔬

ChimeraX daily builds can predict binding affinity of small molecules using Boltz 2 on your Mac, Windows or Linux computer. www.rbvi.ucsf.edu/chimerax/dat...

Proud to share our first lab pre-print: “SND3 is the membrane insertase within a fungal multipass translocon” where @tzujingyang.bsky.social solved the structure of a ribosome-associated SND3-translocon complex involved in ER membrane protein insertion ➡️ doi.org/10.1101/2025...

Folddisco finds similar (dis)continuous 3D motifs in large protein structure databases. Its efficient index enables fast uncharacterized active site annotation, protein conformational state analysis and PPI interface comparison. 1/9🧶🧬
📄 www.biorxiv.org/content/10.1...
🌐 search.foldseek.com/folddisco

Engineering of ATP synthase for enhancement of proton-to-ATP ratio - Nature Communications FoF1-ATP synthase converts proton motive force into ATP, with the H+/ATP ratio typically ranging from 2.7 to 5. Here, the authors engineered this enzyme to form multiple peripheral stalks, achieving a...

Engineered ATP synthase with multiple a-subunits!

Engineering of ATP synthase for enhancement of proton-to-ATP ratio
www.nature.com/articles/s41...

A cellular entity retaining only its replicative core: Hidden archaeal lineage with an ultra-reduced genome Defining the minimal genetic requirements for cellular life remains a fundamental question in biology. Genomic exploration continually reveals novel microbial lineages, often exhibiting extreme genome...

Joining the race to the bottom has never been cooler...
www.biorxiv.org/node/4580343...
www.biorxiv.org/content/10.1...

Happy to share an updated version of our work on the importance of the SARS-CoV-2 spike transmembrane domain in viral entry.

www.biorxiv.org/content/10.1...

🚨 New preprint!
Using U-ExM + in situ cryo-ET, we show how C2CD3 builds an in-to-out radial architecture connecting the distal centriole lumen to its appendages. Great collab with @cellarchlab.com @chgenoud.bsky.social @stearnslab.bsky.social 🙌. #TeamTomo #UExM
www.biorxiv.org/content/10.1...

Amazingly, this gave us a high-confidence transmembrane channel for both mouse and human NS3, with oleic acids forming a bilayer-like pattern.

Our group now call this the “fatty acid hack.”

The #alphafold predictions with and without fatty acids shown below 👇

#FluorescenceFriday (we are watching vimentin (HaloTag7) in U2OS cells co-stained with Nile Red) #livecell #longterm

Excited to unveil Boltz-2, our new model capable not only of predicting structures but also binding affinities! Boltz-2 is the first AI model to approach the performance of FEP simulations while being more than 1000x faster! All open-sourced under MIT license! A thread… 🤗🚀

In-cell discovery and characterization of a non-canonical bacterial protein translocation-folding complex Cryo-electron tomography has emerged as powerful technology for in-cell structural biology, and in combination with breakthroughs in protein structure prediction, offers a unique opportunity for illum...

This is just an excellent preprint by Rasmus Jensen and colleagues from Julia Mahamid's lab @embl.org - a tour de force of Cryogenic electron tomography to do in cell structural biology in which they discover a new complex and solve its structure and function! www.biorxiv.org/content/10.1...

Substrate-induced assembly and functional mechanism of the bacterial membrane protein insertase SecYEG-YidC The universally conserved Sec translocon and the YidC/Oxa1-type insertases mediate biogenesis of alpha-helical membrane proteins, but the molecular basis of their cooperation has remained disputed over decades. A recent discovery of a multi-subunit insertase in eukaryotes has raised the question about the architecture of the putative bacterial ortholog SecYEG-YidC and its functional mechanism. Here, we combine cryogenic electron microscopy with cell-free protein synthesis in nanodiscs to visualize biogenesis of the polytopic membrane protein NuoK, the subunit K of NADH-quinone oxidoreductase, that requires both SecYEG and YidC for insertion. We demonstrate that YidC is recruited to the back of the translocon at the late stage of the substrate insertion, in resemblance to the eukaryotic system, and in vivo experiments indicate that the complex assembly is vital for the cells. The nascent chain does not utilize the lateral gate of SecYEG, but enters the lipid membrane at the SecYE-YidC interface, with YidC being the primary insertase. SecYEG-YidC complex promotes folding of the nascent helices at the interface prior their insertion, so the examined cellular pathway follows the fundamental thermodynamic principles of membrane protein folding. Our data provide the first detailed insight on the elusive insertase machinery in the physiologically relevant environment, highlight the importance of the nascent chain for its assembly, and prove the evolutionary conservation of the gate-independent insertion route. ### Competing Interest Statement The authors have declared no competing interest. Deutsche Forschungsgemeinschaft, https://ror.org/018mejw64, Ke1879/3, 267205415 (CRC 1208) European Research Council, https://ror.org/0472cxd90, CRYOTRANSLATION

Very special feelings to announce this one... A project that started like 10 years ago is reaching the finish line, ready to shine. In a dream-team with @beckmannlab.bsky.social we solved the long-chased structure of the active membrane protein insertase SecYEG-YidC
www.biorxiv.org/content/10.1...

KIF2A stabilizes intercellular bridge #microtubules to maintain mouse embryonic stem cell #cytokinesis, say Lieke Stockmann, Sreya Basu, Niels Galjart and colleagues @erasmusmc.bsky.social: rupress.org/jcb/article/...

#CellCycle #CellDivision #Cytoskeleton #StemCells #Kinesins

✨✨ It's #glycotime for #HIV Env ✨✨

N-linked glycans modulate flexibility & MPER epitope exposure #glycotime

Huge effort by @shehata92.bsky.social @lcasalino88.bsky.social with cryoET of Env in VLPs by @thevillalab.bsky.social & team 💪

Would love feedback!

www.biorxiv.org/content/10.1...

A coronavirus assembly inhibitor that targets the viral membrane protein Nature - High-throughput screening and hit optimization have led to the development of a small molecule, CIM-834, that targets the SARS-CoV-2 membrane protein and blocks assembly of the virus.

A coronavirus assembly inhibitor that targets the viral membrane protein

A small-molecule SARS-CoV-2 inhibitor targeting the membrane protein

The COVID-19 pandemic has spurred the development of new antivirals against specific viruses,

www.nature.com/artic...

www.nature.com/artic...
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🤯 cryo-ET of copia viral-like particles lurking at the nuclear pore of intact Drosophila eggs!
Amazing work by @svenklumpe.bsky.social & more cool findings in this collaborative paper illuminating the replication cycle of an iconic retrotransposon!
www.cell.com/cell/fulltex...

🧬A new imaging technique developed by the Liu Lab uses a novel DNA barcode system to track hundreds of RNA & protein molecules in single cells within thick biological samples, providing a full picture of how these structures are organized inside tissues.
🔗 www.janelia.org/news/new-met...

Mature #HIV-1 contains >2000 copies of “spacer peptide 2”, but we didn’t know why. We now see that SP2 binds the matrix protein and triggers the change into its mature arrangement. Summary video from @margotriggi.bsky.social

Sequence-dependent scale for translocon-mediated insertion of interfacial helices in membranes A biological hydrophobicity scale reveals amino acid partition preferences in water, membrane surfaces, and transmembrane regions.

Thrilled to see over 10 years of hard work finally published!
It’s been an incredible effort and I’m so proud of our biological interfacial and TM scales👇🏻
Sequence-dependent scale for translocon-mediated insertion of interfacial helices in membranes | Science Advances www.science.org/doi/10.1126/...

💪New research led by @lorenabenedetti.bsky.social in the Lippincott-Schwartz Lab shows that subcellular structures similar to those that propagate signals that make muscles contract also transmit signals in the brain that may facilitate learning & memory 🧠
🔗 https://hhmi.news/4jMHbNY