David Kuster
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rnadavid.bsky.social
David Kuster
@rnadavid.bsky.social
RNA & Metabolism. Ancient companions for Life. RNA as spatial organizer of the Cell. IDPs, biomolecular condensates and RNA fun @HymanLab. MBL Physiology '25. And birds.
ebird.org/profile/MjcyMDU0Nw
inaturalist.org/people/9261834
Reposted by David Kuster
Very happy to say that our work on how axonemes are generated is now available on bioRxiv: www.biorxiv.org/content/10.6... - if you’ve ever wondered how the incredibly beautiful, complex structures within motile #cilia are constructed then this is for you!
www.biorxiv.org
February 6, 2026 at 11:20 AM
Reposted by David Kuster
We are hiring!
Come work with us as a Laboratory Technician at IBEC in sunny Barcelona! We offer a one-year contract, with the possibility of extension for up to two additional years.
Please help spread the word! Feel free to contact me if you have any questions.
ibecbarcelona.eu/laboratory-t...
February 11, 2026 at 4:45 AM
Reposted by David Kuster
My student Aoi Otsuka ’s PhD work is now officially published @csf-jscb.bsky.social! 🔬 Single-nucleosome imaging uncovers biphasic local chromatin dynamics in an oncogene-inducible human carcinogenesis model (1–3 d: same, 5–7 d: ↑, back by week 4). Congrats! www.jstage.jst.go.jp/article/csf/...
February 10, 2026 at 1:19 PM
Reposted by David Kuster
Stages of biomolecular condensate formation in pro-β-carboxysome assembly

doi.org/10.1038/s414...
Stages of biomolecular condensate formation in pro-β-carboxysome assembly - Nature Plants
Carboxysomes are cyanobacterial CO2-concentrating compartments with a proteinaceous shell. The elucidation of the role of the shell adaptor protein ApN in stepwise β-carboxysome assembly will aid the ...
doi.org
February 10, 2026 at 10:35 AM
Reposted by David Kuster
#PhDPosition open — #RibosomeBiology & #Translation QC
📍 JGU Mainz, Germany
🗓️ Apply by 10 Mar 2026 (or until filled)
🔗 Full details + project options:
👉 ak-winz.pharmazie.uni-mainz.de/jobs/
Jobs/internships/theses | Winz Lab - AK Winz
ak-winz.pharmazie.uni-mainz.de
February 10, 2026 at 8:02 AM
Reposted by David Kuster
Join the #EMBL conference "Cellular mechanisms driven by phase separation" 🗓️ May 19-22! Register now for in-person at @embl.org Heidelberg or Virtual 👉 www.embl.org/about/info/c...

#EESPhaseSeparation
@events.embl.org
February 9, 2026 at 9:29 PM
Reposted by David Kuster
🧪🧬New preprint We present cryo-EM structures of reconstituted CTCF–nucleosome complexes, showing CTCF dimerization drives nucleosome oligomerization into defined higher-order assemblies. Disrupting CTCF–CTCF interfaces in mESCs reduces looping and impairs differentiation. tinyurl.com/CTCF-nucleos...
February 9, 2026 at 12:54 PM
Reposted by David Kuster
Monday mood: This Heron standing very still, hoping no one asks it to do anything today.

#MondayMotivation
February 2, 2026 at 8:00 AM
Reposted by David Kuster
After failing to find any Bean Geese around Whittle Dene this morning, delighted to catch up with two Tundra Beans on patch at Boulmer before dusk #NEbirding
February 8, 2026 at 6:07 PM
Reposted by David Kuster
I am excited to share a new review @cp-molcell.bsky.social written in collaboration with @tanjamittag.bsky.social , Mikayla Eppert, and Ambuja Navalkar where we review the current evidence for and against the role of density transitions in regulating transcription www.cell.com/molecular-ce...
February 6, 2026 at 9:20 PM
Reposted by David Kuster
I am thrilled to share our paper introducing RBPscan, a novel approach to profile RNA–protein interactions in living cells. Free access link at the end ⬇️ 🧵 1/
www.cell.com/molecular-ce...
RBPscan: A quantitative in vivo tool for profiling RNA-binding protein interactions
Kretov et al. introduce RBPscan, an RNA-editing-based platform that measures how RNA-binding proteins engage their targets in living cells. This approach quantifies the binding strength of protein-RNA...
www.cell.com
February 6, 2026 at 9:37 PM
Reposted by David Kuster
We've got two exciting chromatin talks coming up on Wednesday next week:

@epijenatics.bsky.social from @jbuenrostro.bsky.social's lab and @ambystoma22.bsky.social!

register and join us: us06web.zoom.us/webinar/regi...
February 6, 2026 at 2:58 PM
Reposted by David Kuster
This Friday (today), we’re pleased to welcome Melike Lakadamyali (@melikel.bsky.social) from @upenn.edu.

If you are interested in Super resolution microscopy, cytoplasmic and nuclear organization with a focus on biophysics, then do not miss Prof. Lakadamyali talk in our lecture hall at 13:00. 🤗
February 6, 2026 at 8:52 AM
Reposted by David Kuster
Tau phosphorylation impedes functionality of protective tau envelopes against microtubule-severing enzymes, providing a potential explanation for microtubule destabilization observed in neuropathology

www.nature.com/articles/s41...
Tau phosphorylation impedes functionality of protective tau envelopes - Nature Chemical Biology
Tau phosphorylation was found to hinder the formation and protective functionality of tau envelopes against microtubule-severing enzymes, providing a potential explanation for microtubule destabilizat...
www.nature.com
February 5, 2026 at 4:38 PM
Reposted by David Kuster
IDPSeminas is back again TOMORROW!

Talks from Lucia Strader (@luciastrader.bsky.social) and Heather Meyer! Sign up at idpseminars.com.

Talks start at 1 pm EST / 7 PM CET!! Come learn about transcriptional adaptation and IDRs as environmental sensors and accuators!
February 4, 2026 at 10:14 PM
Reposted by David Kuster
🧪 My lab has an opening for a postdoc position soon! Please share/get in touch!
February 3, 2026 at 2:00 PM
Reposted by David Kuster
Reposted by David Kuster
Put simply: high concentrations facilitate reactions because you get more molecular collisions. However, molecules don't move well (or collide) when they are stuck together:
journals.aps.org/pre/abstract...
Physical limits to acceleration of enzymatic reactions inside phase-separated compartments
We present a theoretical analysis of phase-separated compartments to facilitate enzymatic chemical reactions. While phase separation can facilitate reactions by increasing local concentration, it can ...
journals.aps.org
February 3, 2026 at 8:27 PM
Reposted by David Kuster
We welcome new research group leader Nagaraja Chappidi! He joins the @mpi-cbg.de to explore how cells regulate DNA replication and repair. www.mpi-cbg.de/news-outreac...
February 3, 2026 at 3:26 PM
Reposted by David Kuster
pdb101.rcsb.org/motm/314 histones outside of the eukaryotic domain are the 'molecule of the month'! nice!
PDB101: Molecule of the Month: Histones Across the Tree of Life
Uncovering the evolutionary diversity of histones
pdb101.rcsb.org
February 3, 2026 at 7:14 AM
Reposted by David Kuster
🚀 Just published: New1 shields mRNAs from no-go decay — by preventing ribosome crashes at specific codons.
What’s new?
New1 (eEF3 homolog) stops ribosomes from stalling at C-terminal AAA/AGG/CGU codons. No New1 = collisions + Hel2 recruitment + Cue2-mediated no-go decay.
February 1, 2026 at 9:49 PM
This is my favorite biochemical counter-example by the John Gross lab, where rates are enhanced in the condensed phase - but critically due to an altered enzyme conformation:

www.nature.com/articles/s41...
Biomolecular condensates amplify mRNA decapping by biasing enzyme conformation - Nature Chemical Biology
Alterations in the interactions driving phase separation of the mRNA decapping complex led to conformational rearrangements in its active site, providing a mechanism to control whether substrate mRNA ...
www.nature.com
February 2, 2026 at 4:46 PM
That's likely what has happened in many cases - that retardation/inhibition was interpreted as 'negative, unpublishable result', which is a bit unfortunate since it could just as well have been biologically meaningful.
February 2, 2026 at 4:27 PM
Also fits well with the cumulative intuition, or experience, from biochemical experiments and the 'publication gap' (with few notable exceptions, i.e. altered enzyme conformation in the condensed phase) for rate-enhancing condensates in the literature.
February 2, 2026 at 3:53 PM
Reposted by David Kuster
Does targeting enzymes and substrates in a condensate lead to rate enhancement? No. Here, we investigate how the condensate environment can inhibit an enzyme reaction.

Spoiler: Mass-transport limitations. We find a strong correlation between diffusion and reaction rates.

doi.org/10.64898/202...
February 2, 2026 at 2:25 PM