Laurenz Rabl

Such a cool idea to screen for nascent chain interactors.

Stress adaptation of mitochondrial protein import by OMA1-mediated degradation of DNAJC15 Nature Structural & Molecular Biology, Published online: 27 February 2026; doi:10.1038/s41594-026-01756-0Kroczek et al show that degradation of DNAJC15 by OMA1 and AFG3L2 under stress limits mitochondrial protein import and OXPHOS biogenesis. Non-imported proteins lead to the induction of the unfolded protein responses from the endoplasmic reticulum.

New online: Stress adaptation of mitochondrial protein import by OMA1-mediated degradation of DNAJC15

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. 👇

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.

The ribosome synchronizes folding and assembly to promote oligomeric protein biogenesis Large oligomeric proteins constitute a major fraction of proteomes, but are difficult to refold in vitro, raising the question of how cells direct their biogenesis. Roeselová and Shivakumaraswamy et a...

Our latest cotranslational folding story is now published @cp-molcell.bsky.social. Really cool (I think) new ideas about how exactly the ribosome directs folding and assembly to make sure complicated proteins mature efficiently in cells.
www.cell.com/molecular-ce...

Intricate regulation of Src kinases via N-terminal modifications and specific degradation pathways. A novel degradation pathway involving the CUL4A-DDB1-DCAF10 E3 ligase found by Kremer et al. Tanja Bange lab @andrea-musacchio.bsky.social @ispt-proteinterm.bsky.social www.nature.com/articles/s41...

The protein complex NAC slows down the rate of protein synthesis right at the start. An international research team with significant involvement of #UniKonstanz biologists has now discovered what underlies this previously unknown function of NAC. Details: t1p.de/x7rm4

This has been an extraordinary collab, where I learned a lot and grew as a scientist. Thank you to everybody involved!

We find that NAC not only facilitates N-Terminal maturation (eg. iMet excision, Nt-acetylation) and SRP mediated targeting, but also chaperones cytosolic and mitochondrial proteins. Moreover, we find evidence for NACb tunnel Insertion and link it to translational pausing.

Extremely proud to see this published in Nature today. Spear-headed by Jae Ho Lee from Judith Frydmans group and with help from Marina Rodninas group we studied the determinants of NAC ribosome association using selective ribosome profiling.

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

Mechanism of cotranslational modification of histones H2A and H4 by MetAP1 and NatD NAC enables cotranslational N-terminal processing of histones H2A and H4 by recruiting MetAP1 and NatD at the ribosomal tunnel.

Last X-Mas, the ribosome gave you methionine,
but the very next day, MetAP took it away.
This year, to save histones from tears,
NatD gives you an acetyl group. ⭐️

Explore our latest paper with the Deuerling lab @uni-konstanz.de and Shu-ou Chan lab @caltech.edu!

www.science.org/doi/10.1126/...

Also very interesting that NatA has an inhibitor enforcing cotranslational mode, while other NATs do not.

Great paper explaining the fine details of NatA ribosome binding and how HYPK helps to optimize binding kinetics. Also explains why KO worms have a phenotype, something that I never fully understood. Still, I would be very interested to know why Nt-acetyation is restricted to cotranslational action?

How does the kinase ZAK sense ribosome collisions? Find out in our latest collaboration with the @greenlab.bsky.social @doubleshuang.bsky.social @Vienna Huso: 1/4
rdcu.be/eRmJl
#ribosome #cryoEM #LMU #JHMI

Structural basis of regulated N-glycosylation at the secretory translocon - Nature The structural mechanism of a natively isolated GRP94 folding intermediate tethered to a CCDC134-bound translocon is described, revealing how the nascent chain remodels the translocon to control N-glycosylation by OST.

Nature research paper: Structural basis of regulated N-glycosylation at the secretory translocon

go.nature.com/49vhkr5

Want to know how lipidation of some nascent chains takes place by NMT2-- Check our latest work on how NAC couples Protein Synthesis with Nascent Polypeptide Myristoylation on the Ribosome out today @embojournal.org‬: www.embopress.org/doi/full/10....

Very cool study! also nicely complementing the recent selective ribosome profiling study from the Shu-ou Shan lab. I am intriguied what might be the proposed inhibitory mechanism shielding proteins from cotranslational insertion.

Principles of cotranslational mitochondrial protein import Selective ribosome profiling reveals that nearly 20% of mitochondrial proteins in human cells are imported during translation on cytosolic ribosomes. Cotranslational import requires an N-terminal pres...

Emmanuel Levy @elevylab.bsky.social has joined BlueSky 🌟 with a fantastic Cell paper with Shu-ou Shan, showing the interactome of the TOM complex and how cotranslational mito import prioritizes large globular domains. Beautiful science!
Give him a warm welcome 🎉
link: www.cell.com/cell/fulltex...

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...

I want to thank all collaborators, especially Jae Ho Lee and Judith Frydman at Stanford University, as well Marina Rodnina at MPI Göttingen.

This story has been in the making for a long time, and I am so happy to see it online!

We find that NAC binds throughout translation, having various different functions. Depending on the substrate, NAC can act as a chaperone, guide N-terminal maturation and protein localisation, affect translation elongation and protect mitochondrial TMDs.

NAC controls nascent chain fate through tunnel sensing and chaperone action The nascent polypeptide-associated complex (NAC) is a conserved ribosome-bound factor with essential yet incompletely understood roles in protein biogenesis. Here, we show that NAC is a multifaceted r...

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

I am excited to share a big part of my thesis in preprint form, where we analysed the determinants of NAC-binding to translating ribosomes using selective ribosome profiling in C. elegans.

Last Friday I defended my PhD thesis. It was great day and I am so excited for what’s to come next!

NAC continues to deliver. What a fascinating protein!

News from the Lab!
Congrats to everybody involved!

The nascent polypeptide-associated complex (NAC) as regulatory hub on ribosomes The correct synthesis of new proteins is essential for maintaining a functional proteome and cell viability. This process is tightly regulated, with ribosomes and associated protein biogenesis factors...

doi.org/10.1515/hsz-...

I am super happy to share this review as my first post on Bluesky. After submitting my PhD thesis at the start of the year, my PI Elke Deuerling suggested to write this review with her, covering many of the findings of my thesis. I am excited to see it published today!