Marcin J. Suskiewicz
@msuskiewicz.bsky.social
1.6K followers 1.1K following 140 posts
Structural biologist and biochemist. CNRS researcher at CBM Orléans @cbm-upr4301.bsky.social. Interested in protein modifications & interactions. Also husband, dad of 2, friend, ☧. Personal website: msuskiewicz.github.io
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msuskiewicz.bsky.social
A part of our team at the recent EMBO SUMO conference in La Grande Motte/Montpellier
Reposted by Marcin J. Suskiewicz
lindorfflarsen.bsky.social
The proteasome-substrate-shuttle protein UBQLN2 contains—like other quality control system proteins—a long region devoid of lysine (a lysine desert)

Martin Grønbæk-Thygesen (from @rhp-lab.bsky.social) et al show that introducing K here causes ubiquitylation and degradation

doi.org/10.1101/2025...
Fig. 1 – UBQLN2 is a conserved lysine-depleted protein. (A) Sequence comparison of
UBQLN2 orthologs in the indicated species. Intrinsically disordered regions in human
UBQLN2 based on MobiDB are shown as a blue bar. The domain organization based on the
SMART database is marked. Lysine residues are marked as black squares. (B) ESM-2
predictions of all possible single amino acid substitutions of human UBQLN2 presented as a
heat map. The wild-type residues are marked in blue. ESM-2 scores close to zero (light
yellow colors) indicate that the amino acid substitution is compatible with the ESM-2
language model, whereas negative scores (dark orange colors) indicate that the variant is
incompatible with the ESM-2 model. The domain organization (based on SMART) is aligned
above the map. Note that substitutions to lysine or cysteine in general appear detrimental, in
particular downstream of the UBL domain. (C) The AlphaFold2 predicted structured of
human UBQLN2 (AF-Q9UHD9-F1) (left panel). The UBL domain is colored blue, and the
UBA domain is colored orange and the STI1 regions green. Zoom in on the UBL domain
(right panel) with the lysine residues highlighted as stick representations and colored based
on the relative accessible surface area (rASA, dark red exposed; grey, buried).
Reposted by Marcin J. Suskiewicz
madic.bsky.social
You can get MSAs directly from AlphaFold DB now (alphafold.ebi.ac.uk). I also missed the FoldSeek implementation, which lets you search for structurally similar proteins direktly.

This saves some clicking around. Neat!
Reposted by Marcin J. Suskiewicz
lindorfflarsen.bsky.social
A good day to remember John Gurdon’s school report from his biology master at Eton
Reposted by Marcin J. Suskiewicz
Reposted by Marcin J. Suskiewicz
michaelhendricks.bsky.social
"The work I was involved in had no obvious therapeutic benefit. It was purely of scientific interest. I hope the country will continue to support basic research even though it may have no obvious practical value."
- John Gurdon
katherine-brown.bsky.social
Very saddened to hear of John Gurdon’s passing. I’ve been lucky enough to interact with him at multiple points through my career - from undergrad lectures, through his position as former Chair of @biologists.bsky.social’s Board of Directors, and as an author at @dev-journal.bsky.social.
Nobel Laureate Professor Sir John Gurdon dies aged 92
It is with great sadness that the University shares the news of the death of Professor Sir John Gurdon, founder of the Gurdon Institute.
www.cam.ac.uk
msuskiewicz.bsky.social
Served on a PhD thesis jury today, for the 2nd time in my life. Greatly honoured, and enjoyed it a lot. It's a beautiful part of this job. Many other such parts (supervising interns, discussing with colleagues, doing experiments...).
Reposted by Marcin J. Suskiewicz
Reposted by Marcin J. Suskiewicz
jamesbriscoe.bsky.social
Very sad news, John Gurdon has died.

A developmental biologist's developmental biologist, Nobel prize winner

His work is the foundation of much of today's dev & stem cell bio.

An inspiration to many, including me. Always asking questions & wanting the answers

www.magd.cam.ac.uk/news/profess...
Professor Sir John Gurdon FRS (1933-2025) | Magdalene College
Magdalene College is deeply saddened to announce the death of Professor Sir John Gurdon FRS, who served as Master of the College from 1995 to 2002.
www.magd.cam.ac.uk
Reposted by Marcin J. Suskiewicz
pnas.org
For 25 years, the Chair of the @laskerfdn.bsky.social Jury has reflected on the intersection of science and art in an annual essay. This year, Joseph L. Goldstein explores “From simplicity to complexity: A path to innovation in science and art.” Read now: www.pnas.org/doi/10.1073/...
2025 Lasker Awards – “From simplicity to complexity: A path to innovation in science and art.” Read the essay in a PNAS Perspective. Portrait of Joseph L. Goldstein.
Reposted by Marcin J. Suskiewicz
embojournal.org
RNF114 and RNF166 exemplify a new E3 ligases family that recognizes #MARUbylation –hybrid ADP-ribose/ubiquitin modifications– and extends them with K11-linked polyubiquitin
@jnpruneda.bsky.social @michaelnadbio.bsky.social and colleagues
www.embopress.org/doi/full/10....
Reposted by Marcin J. Suskiewicz
andriigorelik.bsky.social
Out in @natcomms.nature.com: Cryo-EM structure of the pseudo-HAT-containing O-GlcNAcase!

Especially exciting since multiple companies are developing O-GlcNAcase inhibitors for Alzheimer's disease (tau is O-GlcNAcylated). Glad to have a small contribution in this story.
Congrats to all authors!
Multi-domain O-GlcNAcase structures reveal allosteric regulatory mechanisms - Nature Communications
This work reveals how a regulatory domain in O-GlcNAc hydrolase (OGA) shapes enzyme flexibility and activity, uncovering mechanisms that help maintain O-GlcNAc balance in cells.
www.nature.com
Reposted by Marcin J. Suskiewicz
Reposted by Marcin J. Suskiewicz
wpokrzywa.bsky.social
Preprint alert! 🚨
We reveal molecular switches that enable the nucleolus to reorganise into a proteostasis hub - coordinating protein quality control with ribosome biogenesis and cross-talk with other stress-responsive organelles.
A big tour de force by the team 💪
www.biorxiv.org/content/10.1...
CHIP, VCP, and Nucleolar Gatekeepers Remodel the Nucleolus into a Stress-Responsive Proteostasis Hub
The nucleolus, classically dedicated to ribosome biogenesis, also acts as a stress-responsive proteostasis hub. During heat shock, misfolded proteins accumulate in its granular component (GC), but whe...
www.biorxiv.org
Reposted by Marcin J. Suskiewicz
meiercredo.bsky.social
Check out our new preprint on an integrated pipeline combining in situ #cryo-ET with MALDI #MSImaging for single-cell identification and classification from previously analysed EM-grids.
Link: www.biorxiv.org/content/10.1...
Reposted by Marcin J. Suskiewicz
elisecutts.bsky.social
🚨 Astobio alert 🚨

@royalsocietypublishing.org recently put out a whole special issue on the origins of life edited by @ricardsole.bsky.social, Chris Kempes and Susan Stepney

I wondered why there were so many origin of life papers coming up in my Google Scholar alerts recently... 🧪
Philosophical Transactions of the Royal Society B: Biological Sciences: Vol 380, No 1936
royalsocietypublishing.org
Reposted by Marcin J. Suskiewicz
dijiang319.bsky.social
@science.org ⤵️challenges prevailing notion—repressor and activator act by distinct mechanisms: repressors block via steric hindrance/activators enable Pol II binding to promoter🧬

E. coli transcription factors regulate promoter activity by a universal, homeostatic mechanism | Science bit.ly/adv2064
Reposted by Marcin J. Suskiewicz
duxinlab.bsky.social
Excited to have contributed to this new @cp-molcell.bsky.social paper on how PARP1 auto-modification promotes faithful Okazaki fragment processing and limits replication fork speed.

A big congrats to Jonas for driving this work forward, great to see the results out!

👉 10.1016/j.molcel.2025.09.006
msuskiewicz.bsky.social
This looks super interesting! We work on self-assembly as well, but of larger protein domains with a natural propensity to undergo self-assembly into filaments and things like that. I will be curious to learn more about simpler biochemical systems that show such tendency.
Reposted by Marcin J. Suskiewicz