We are excited to share our new preprint which is now available to read on biorXiv: doi.org/10.64898/202... 🎉🎉🎉

Happy to finally share the amazing results of our long-term collaboration with Karin Reinisch’s lab on how bridge lipid-transfer proteins (BLTPs) cooperate with partner proteins to orchestrate lipid delivery. A quick thread (1/7) www.biorxiv.org/content/10.6...

The last chapter from my postdoc days is finally online! We solve structures of the ER membrane O-mannosyltransferase Pmt4 and uncover a functionally important cytosolic binding site for the Dol-P-Man substrate lipid - allosteric regulation or a long sought after Dol-P-Man flippase?? 🔄 rdcu.be/eUJfb

It’s out! Using cryo-ET in Dicty cells, we take a fresh in situ look at vaults. Surprisingly, we uncover vaults associated with ER and NE membranes, and find that many vaults enclose ribosomes in defined orientations, opening new avenues to their cellular function! www.biorxiv.org/lookup/conte...

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...

@attychang.bsky.social, @nanigrotjahn.bsky.social et al. show that cytoplasmic #ribosomes on #mitochondria alter the local membrane environment for protein import. rupress.org/jcb/article/... 📕 From The Year In Cell Biology: rupress.org/jcb/collecti... #CellBio2025

Just published! We share an open-source workflow to measure membrane thickness from tomograms, including a tutorial with 3D visualizations. We analyze thickness variations across organelles and reflect on where to define a membrane boundary. @becklab.bsky.social #teamtomo rupress.org/jcb/article/...

Glushkova, Böhm, & Beck @maxplanck.de develop a publicly available computational method to measure the thickness of biological membranes in cryo-electron tomograms. Analysis of algae & human cells reveals systematic membrane thickness variations within & across organelles rupress.org/jcb/article/...

This was a fun new collaboration using selective ribosome profiling to understand how the subunit composition of the ER translocon is tailored by the nascent chain. Congratulations to everyone involved! www.nature.com/articles/s41...

Our first lab paper is out! We identify and solve the first structure of the SND3 translocon involved in fungal membrane protein insertion. Congratulations @tzujingyang.bsky.social, and our colleagues @saumyakm.bsky.social, @hummerlab.bsky.social and Julian Langer. Read more ⬇️ and ➡️ rdcu.be/eNgIO

We discovered how an engineered ribosome arrest peptide (eRAP) acts as a built-in “pause button” to precisely control protein synthesis. eRAP merges two natural stalling systems to stop the ribosome at just the right time — shaping how nascent proteins begin to fold. academic.oup.com/nar/article/...

Excited to share our Nature Communications paper 🎉 rdcu.be/eK7wG
We uncovered by cryoEM how the human proteasome recognizes branched K11/K48 ubiquitin chains through a new K11-binding site in the RPN2 subunit, revealing how the proteasome precisely identifies targets for rapid turnover. #cryoEM

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...