Haselbach Lab

Congrats Leo!

#pictureofthemonth: March shows a “Cross-section” of the endoplasmic reticulum, a kind of membrane-labyrinth, using cryo-electron microscopy.

More: www.biochem.mpg.de/plitzko

March – Calendar of @mpiforbi.bsky.social and @mpibiochem.bsky.social

📸 Illustration by Jürgen Plitzko & Sven Klumpe

Job opening for Research Group Leader in Structural Studies at MRC Laboratory of Molecular Biology, focusing on macromolecular structures.

Are you a structural biologist pushing the boundaries of molecular science with an ambitious research programme?
Join our Structural Studies Division as a tenure-track Group Leader, with core funding, world-leading facilities & enthusiastic colleagues.
Apply by 16 MAR
www.nature.com/naturecareer...

SAVE THE DATE: Ubiquitin & Friends Symposium 2026 on April 29-30 or even better, sign up now: lnkd.in/eEQmaCYT
It takes place at Van Swieten Hall, 1090 Vienna & is organized by the SFB Targeted Protein Degradation (incl. numerous research groups at Vienna BioCenter)
@sfb-tpd-vienna.bsky.social

We‘re looking for a motivated Master student to join our team!

Do you want to optogenetically control metabolic activity to see how metabolism affects patterning and morphogenesis? 💡🧫🧬🔬

Then please apply!
#optogenetics #metabolism #devbio #hESCs

Please RT. Thank you!🙏

Please spread the word: the Structural Studies Division @mrclmb.bsky.social is looking for a new tenure-track, independent group leader with an exciting plan in any area of Structural (Molecular & Cell) biology, in discovery biology and/or methods development. 🥳

mrc.tal.net/vx/mobile-0/...

Our paper is out in @natcomms.nature.com! APOBEC3s drive mutagenesis in cancer. We uncover a novel pathway keeping them in check. The key is APOBEC3 binding of cellular RNAs, which simultaneously controls their nuclear localization and shields them from degradation.

Read it here: rdcu.be/e4qaa

This work was spearheaded by @hannabrunner.bsky.social and was again a great collaboration with @johanneszuber.bsky.social. It features a saturation mutagenesis screen, a cryo structure of the import complex and in-vitro reconstitution of the process

In the nucleus the importins are released and Akirin2 is degraded by the proteasome itself.

It shows how the proteasome is bound by Akirin2 in the cytoplasm. This then recruits the importin IPO9 and further Akirin2 dimers. All Akirin2 protomers will then bind canonical importins, leading to clustering of importins on the proteasome surface enableing the transition through he nuclear pore.

This is a video summarizing our recent paper (www.nature.com/articles/s41...)

youtu.be/eNY2CRlYTRo

The video shows how how the proteasome binds Akirin2 dimers in the cytoplasm. These recruit the importin IPO9 as well as the further Akirin2 dimers. Each Akirin2 dimer will also bind canonical importins leading to importin clustering. This in turn enables the passage through the nuclear pore

Nuclear transport of the proteasome!

And a new paper from the lab. A follow up to a previous study in which we elucidate the mechanism of the nuclear transport. Read the full story: www.nature.com/articles/s41...

A near-complete map of human cytosolic degrons and their relevance for disease

We measured degron potency of >200,000 30-residue tiles from >5,000 human proteins, and trained a model to predict degrons from sequence

Led by @vvouts.bsky.social in @rhp-lab.bsky.social

doi.org/10.1126/scia...

Great story from our neighbours at the university of Vienna. We are that we could contribute to this.

Please share!
My group at @zmbp-tuebingen.bsky.social is offering a post-doctoral position (4 years). We look for a structural biologist with experience in Cryo-EM/Cryo-ET to investigate the mechanisms of host invasion by pathogenic fungi. Deadline February 28th!
uni-tuebingen.de/universitaet...

Thank you Ahmad

Check out our new paper in @natcomms.nature.com .com where we used #cryoEM together with biochemical and mutational analyses investigated the cotranslational protein folding by Ssb in yeast.

Publication: doi.org/10.1038/s41467-025-67685-6

Check below for the cryoEM centric feed. 👇

Formation & function of #MembranelessOrganelles! #CryoET structures of #proteasome storage granules inside cells!
Read our paper @cp-cell.bsky.social!

❕Publication: doi.org/10.1016/j.ce...
❕Press Release: www.biochem.mpg.de/en/pressroom

@uoftmedicine.bsky.social
@erc.europa.eu #UPSmeetMet

New work from our Haselbach lab with collaborators captures ribosomes 𝘮𝘪𝘥-𝘣𝘶𝘪𝘭𝘥 and reveals a flexible, modular strategy behind their assembly, rather than a strict assembly line.
Published in _Nucleic Acids Research _👉 https://doi.org/10.1093/nar/gkag036

🔬 Ribosomes are hands down one of the most intricate molecular machines we know. Huge (for a cellular scale at least) complexes made of long RNAs (rRNAs) and proteins … a lot of different proteins.

1/6

(❗️Sound on!)

@narjournal.bsky.social

Thank you

A comprehensive view on r-protein binding and rRNA domain structuring during early eukaryotic ribosome formation Abstract. Formation of the eukaryotic ribosomal subunits follows a strict regime to assemble ribosomal proteins (r-protein) with ribosomal RNAs (rRNA) whil

And the 4th paper in this week contribution from our lab tells about ribosome biogenesis in yeast. A follow-up story from our wonderful collaborators in Graz - the Bergler Lab. Structural work was again done by the amazing @lgrundmann.bsky.social: academic.oup.com/nar/article/...

Excited to share our new paper! We developed a method to visualize proteasomal degradation at the single–molecule level in live cells, enabling us to dissect distinct modes of substrate engagement, probe co-factor dependence, and study proteasome–ribosome collisions.
www.biorxiv.org/content/10.6...

I am very happy that I could advice in this great story. Seeing single proteasomes degrade in cells is opens so many interesting possibilities. Check the preprint.

And another paper with contribution from us. Here Sascha Amann solved the structure of the BORC complex. Due to its shape it is extremely challenging for cryo EM analysis but still he cracked it. Read the full story spearheaded by the Huber lab in Innsbruck: www.pnas.org/doi/10.1073/...

🔬 Postdoc position – Infection Biology & Cryo-ET (Zurich) 🇨🇭
We are looking for a motivated Postdoc to join our interdisciplinary team.
📩 Interested? Check out the job advert:
www.imm.uzh.ch/dam/jcr:cb17...

👉 More info on the lab: www.weiss-laboratory.com
Please share with interested colleagues!

Have a look at our new structure of co translational folding in yeast. This is collaborative work initialized by the Rospert lab from the @uni-freiburg.de. Structural work has been done by the amazing @lgrundmann.bsky.social Stay tuned for the next ribosome paper from him, following very soon.

You want to give details whether this is an available tool or something you wrote? ;)