Really proud to see this. Huge congratulations to @helenfoster.bsky.social on the Biochemical Society Early Career Award, well deserved!!

Beautiful new study from @dyneinassembly.bsky.social lab on cilia recycling.

It’s done!! Molecular architecture of the ciliary base in mammalian multiciliated cells! A study 13 years in the making 👴, thanks to collab with @stearnslab.bsky.social + @centriolelab.bsky.social & visionary work by @computingcaitie.bsky.social, who integrated native #cryoET with #XLMS & #UExM 🧪🧶🧬🔬

Our latest @biorxivpreprint.bsky.social: "Prion-like transmission of human tau strains in the mouse brain" 🥳

With Michel Goedert and Masato Hasegawa.

www.biorxiv.org/content/10.6...

Postdoctoral Scientist | PNAC | Dr Ana Tufegdzic Vidakovic | LMB 2142 - Cambridge, Cambridgeshire (GB) job with MRC Laboratory of Molecular Biology (LMB) | 12857096 Postdoctoral Scientist Salary £42,694 per annum pro rata Fixed term for 3 years MRC Laboratory of Molecular Biology, Cambridge, UK Applications are...

We are looking for a postdoc to join us on the quest for understanding RNA Pol II destruction machines! If you are curious why more than 80% of Pol II are removed from genes, check out the post below:

www.nature.com/naturecareer...

On this 1st April I'm happy to release a technical report from our startup MirageBio, describing a new protein structure model with state-of-the-art performance.

jgreener64.github.io/posts/techni...

Check out this new work from @ckylau.bsky.social and @ritatewari.bsky.social labs on proteins that bridge Plasmodium cytoskeleton and it's motility apparatus. Congrats to all authors!!

Huge congratulations to @vcmentowski.bsky.social on winning the Bayer Pharmaceuticals PhD Award at this year’s Mosbach Symposium!! Really great to see her work being recognised.

Depictions of the structure of CDK11-cyclin L-SAP30BP. Four cryo-EM densities are shown at the top, two molecules models at the bottom. CDK11 is green, cyclin L is purple, and SAP30BP is yellow.

Have a look at our latest results on #CDK regulation, just posted as a pre-print! This study was spearheaded by PhD student Amy McGeoch. Amy has determined the #cryoEM structure of the CDK11-cyclin L-SAP30B complex, an important regulator of #spliceosome activation.
www.biorxiv.org/content/10.6...

Proud to share the yeast telomerase structure, led by the talented @hongmiaohu.bsky.social in collaboration with the Wellinger and Chartrand labs. Discovered 37 years ago and took us nearly 7 years but totally worth the wait 😍.
www.science.org/doi/10.1126/...
www.youtube.com/watch?v=gFE4...

Also do check out a related manuscript that came out last week. www.nature.com/articles/s41...

Overall, these structural insights reveal how cytoplasmic lattices are assembled and suggest hypotheses for their function. Much remains to be explored.

We also find an equally abundant state where the cavity contains a central FBXW-SKP1 complex but no ubiqutin density. This is explained by the ubiqutin binding pockets on the protein PADI6 opening up which would make the ubiquitin binding unfavourable and make it available for ubiqutin transfer.

Our structure raises another possibility that these structures are directly involved with ubiquitination as they have the components one would need for ubiquitin transfer. Eg: The proteins within the repeat unit core are arranged to form a cavity that contains E2-E3 ligases charged with ubiquitin. 🤯

What are these proteins doing here? One possibility is that CPLs could be storing them for use during development consistent with previous proposals that CPLs act as protein storage sites. If true, when would they be released and used is not clear.

So what’s in this core? Proteins involved in ubiquitination and tubulin. We find multiple F-box protein–SKP1 complexes and an interesting assembly made of the E2-ubiqutin-conjugating enzyme UBE2D, E3 ligase UHRF1, NLRP14 and, guess what, an alpha-beta tubulin.

A striking finding is that proteins shown by prior genetic studies to be non-essential are involved in filament formation. This suggests that the functionally important part of cytoplasmic lattices is not the filament itself, but the core of each repeat unit.

Our structure reveals the architecture of cytoplasmic lattices and shows how the different proteins are arranged into a huge ~4.5MDa repeat unit, how they form filaments and how these filaments connect to each other to form lattices.

Cytoplasmic lattices are enigmatic structures required for mammalian development that occupy large portions of the cytoplasm in oocyte and early embryos. We took an in situ cryo-ET approach to understand what they are made of and what their function might be.

Excited to share our work on the structure and function of cytoplasmic lattices within mouse embryos. A collaborative effort with @niakanlab.bsky.social and work led by @kashishsingh.bsky.social and @inaharasimov.bsky.social . It is now out on BioRxiv: www.biorxiv.org/content/10.6...

#journalclub! We had a look at axonal lysosomes in a preprint from Walker et al. (2026). The authors show that as v-ATPase-positive lysosomes mature, the mRAVE-dependent recruitment of V1 onto V0 is associated with a change in motile behaviour, from bidirectional to retrograde-only. Very cool!

Very interesting work! Otherwise we wouldn't bring it up :)) — and it is especially cool for us to see what dynein proteins are up to outside of their roles in dynein-dynactin motor complexes

TANGO: Analysis and curation of particles in cryo-electron tomography - Nature Communications Cryo-electron tomography visualizes molecules inside cells, but it lacks flexible tools to study their spatial organization. The authors present TANGO, a framework that utilizes neighborhoods of parti...

Today in #journalclub we learned that it takes two to TANGO: particle lists and spatial analysis! 💃🕺 Check out this new open-source Python package that lets you get more information from your cryo-ET data.
www.nature.com/articles/s41...

In our last week's #journalclub, we looked at how the dynein light chain LC8 stablises the disordered domain of KANK1, transforming it into a rigid, hinged rod that can span the cortex–microtubule gap and recruit kinesin-4 to cortical microtubule plus ends.

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

Everybody presents a paper that's either relevant to transport or simply very interesting. We mostly review new papers. Each person gives a 2-slide 5 min presentation.

The new isoNet2 looks amazing! We are excited to try it out! #journalclub www.biorxiv.org/content/10.6...

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.

Today in #JournalClub we discussed a new preprint that uses in situ cryo-ET and molecular dynamics simulations to study biomolecular condensate formation. Very beautiful data and interesting insights. Check it out!
www.biorxiv.org/content/10.6...

Beautiful images from @christlet.bsky.social labelling tubulin in neurons #journalclub
www.biorxiv.org/content/10.6...