I am delighted to be among this years winners awards from the Biochemical Society! The Early Career Award recognises the work I did during my PhD and postdoc, and hopefully signals a bright start for my new lab within the @astbury-bsl.bsky.social at the University of Leeds 💫

The Biochemical Society 2027 Early Career Research Award presented to Dr Helen Foster from University of Leeds, UK, with award logo and photo.

Utilising in situ structural biology to uncover fundamental mechanisms of cytoskeletal regulation, we're excited to present Helen Foster with an Early Career Research Award in 2027! Helen's research on immune cell cytoskeletal remodeling could open new frontiers in molecular immunology.

Happy to share our latest work spearheaded by super talented PhD student Muyang Ren now out as a bioRxiv preprint.

'Motile ciliophagy promotes ciliary recycling under stress'

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

Check out our first lab preprint: A real team effort to understand the Plasmodium GAPM proteins, which form part of a essential bridge between the parasite's cytoskeleton and motility apparatus. Below is a sneak peek of some beautiful microscopy - light and electron! www.biorxiv.org/content/10.6...

🚨 Preprint alert!

We solved the structure of human NSUN2 bound to Asp tRNA, revealing how it installs m⁵C and recognizes RNAs
#CryoEM #RNABiology

A collab between Casañal & Gullerova labs, with @miclass.bsky.social and me working side by side as co-first authors

🔗 doi.org/10.64898/202...
(0/7🧵)

📢 First preprint from the Casañal Lab!

Excited to share our work on human NSUN2, done together with the brilliant @ecleroy.bsky.social.

Using #CryoEM, we capture the dramatic structural rearrangement of tRNA as it flips a cytidine into the NSUN2 catalytic pocket for m⁵C modification.

Take a look👇

Proud and excited to share our work with the community! Helen @helenfoster.bsky.social Foster et al. study how #cilia axonemes are built. 👀 Don't miss the gorgeous and insightful movies by @margotriggi.bsky.social, they really show our discoveries in full action!

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

Incredible new work on ciliary axoneme assembly spearheaded by @helenfoster.bsky.social (#NewPI) from the @gaiapigino.bsky.social. Like all good science, answers many questions & opens up many new ones!

Kudos to the entire team for this important advance in cilia biology. Lovely animation!

There was so much to unpack with this data, we teamed up with the marvellous @margotriggi.bsky.social to help explain what we think is going on. (Please also check out our model of central apparatus assembly here: www.biorxiv.org/content/10.6...)

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!

How do cells adapt morphology to function? In a 🔥 preprint by @zjmaggiexu.bsky.social , with @dudinlab.bsky.social and @amyweeks.bsky.social , we identify a self-organizing single-cell morphology circuit that optimizes the feeding trap structure of the suctorian P. collini. 🧵 tinyurl.com/4k8nv926

Happy to share the inaugural paper from the lab. We describe a molecular mechanism for the activation of outer dynein arm motors that power the vital motion of cilia.

Open access link below:
www.nature.com/articles/s41...

Here's a cool animated summary

I am excited to share our new preprint on the CAGE complex, a mysterious hollow protein complex that I first saw years ago while surveying Tetrahymena ciliary lysate www.biorxiv.org/content/10.1... #cilia #protistsonsky 🧬🧪

Excited to see this work published online at @cp-cell.bsky.social today!

www.cell.com/cell/fulltex...

Thrilled to see our study on how kinesin-2 motors are switched on and off published in @natsmb.nature.com ⚛️

➡️ www.nature.com/articles/s41...

Congrats to all authors from me and Anthony 🎉 @dunnschool.bsky.social Check out this animation made by talented PhD student @matthew-batisio.bsky.social 😆

Condensin II activation by M18BP1 Borsellini, Conti, Cutts, Harris, et al. identify an interaction between M18BP1 and condensin II that is essential for condensin II activity and chromatin localization. MCPH1 keeps the interphase geno...

Condensin II activation by M18BP1: Molecular Cell www.cell.com/molecular-ce...

Human Technopole - Electron Microscopy (EM) Specialist APPLICATION CLOSING DATE: July 9th 2025About the InstituteHuman Technopole (HT) is an interdisciplinary life science research institute, created and supported by the Italian government, with the aim o

🚨 We're Hiring! We're looking for a passionate and skilled EM Specialist to join our team! 📅 Application Deadline: July 9th, 2025 🔗 Learn more and apply here: careers.humantechnopole.it/o/electron-m...

A conserved mechanism for the retrieval of polyubiquitinated proteins from cilia The temporospatial distribution of proteins within cilia is regulated by intraflagellar transport (IFT), wherein molecular trains shuttle between the cell body and cilium. Defects in this process impair various signal-transduction pathways and cause ciliopathies. Although K63-linked ubiquitination appears to trigger protein export from cilia, the mechanisms coupling polyubiquitinated proteins to IFT remain unclear. Using a multidisciplinary approach, we demonstrate that a complex of CFAP36, a conserved ciliary protein of previously unknown function, and ARL3, a GTPase involved in ciliary import, binds polyubiquitinated proteins and links them to retrograde IFT trains. CFAP36 uses a coincidence detection mechanism to simultaneously bind two IFT subunits accessible only in retrograde trains. Depleting CFAP36 accumulates K63-linked ubiquitin in cilia and disrupts Hedgehog signaling, a pathway reliant on the retrieval of ubiquitinated receptors. These findings advance our understanding of ubiquitin-mediated protein transport and ciliary homeostasis, and demonstrate how structural changes in IFT trains achieve cargo selectivity. ### Competing Interest Statement The authors have declared no competing interest. Sara Elizabeth O'Brien Trust Postdoctoral Fellowship awarded through the Charles A. King Trust Postdoctoral Research Fellowship Program, , 8460873-01 Richard and Susan Smith Family Foundation, https://ror.org/05j95n956, National Institute of General Medical Sciences (NIGMS), , R01GM141109, R01GM143183

How do cells keep their cilia “clean” and functional? Our new study uncovers a conserved mechanism for retrieving polyubiquitinated proteins from #cilia – a process essential for cellular signaling and health. #cellbiology #ciliopathy #ubiquitin #IFT 🧵👇 1/n

Great to see our story on dynein & kinesin co-dependence published www.nature.com/articles/s41..., and absolutely chuffed that it's made the front cover (thanks NSMB!). A brilliant News & Views too by Steven Markus www.nature.com/articles/s41.... Collab between @carter-lab.bsky.social & Straube lab🔬

Excited to share our preprint on the molecular architecture of heterochromatin in human cells 🧬🔬w/ @jpkreysing.bsky.social, @johannesbetz.bsky.social,
@marinalusic.bsky.social, Turoňová lab, @hummerlab.bsky.social @becklab.bsky.social @mpibp.bsky.social

🔗 Preprint here tinyurl.com/3a74uanv

Credit: Margot Riggi (@margotriggi.bsky.social), Max-Planck Institute of Biochemistry (@mpibiochem.bsky.social)

Asgard archaea have actin - but what about microtubules? Where do they come from? 🧐 Our new paper www.cell.com/cell/fulltex... by @xujwet.bsky.social & @florianwollweber.bsky.social, in collaboration with the Schleper & Wieczorek labs, describes tiny Asgard microtubules! #TeamTomo #ArchaeaSky 1/6

Our MARCH Issue is now live! 🥳

Find the link to the full issue here:
🔗 go.nature.com/41gd09d

The cover is inspired by this great article on intraflagellar transport by @gaiapigino.bsky.social and @samlacey.bsky.social
👉 go.nature.com/41fEig5

#CellBio #cilia

“Join the Pigino Lab! We’re hiring a PhD student to explore primary cilia biology using advanced imaging, spatial ‘omics, and AI. Apply now at www.cilia-ai.eu and be part of the Cilia-AI Doctoral Network!”

Dynein-2 is tuned for the A-tubule of the ciliary doublet through tubulin tyrosination Eukaryotic cilia and flagella are thin structures present on the surface of cells, playing vital roles in signaling and cellular motion. Cilia structures rely on intraflagellar transport (IFT), which ...

We have posted our new #preprint regarding the track recognition mechanism of dynein-2 that works in #cilia on bioRxiv @biorxivpreprint.bsky.social!!
www.biorxiv.org/content/10.1...
1/8 🧵

DNAHX: a novel, non-motile dynein heavy chain subfamily, identified by cryo-EM endogenously Ciliogenesis and cilia motility rely on the coordinated actions of diverse dyneins, yet the complexity of these motor proteins in cilia has posed challenges for understanding their specific roles. Tra...

Excited to share our work on bioRxiv before my thesis defense! Together with my undergraduate mentee Diego, postdocs Wan and Jun, and my advisor Kai, we identified a novel dynein heavy chain subfamily, DNAHX, from sea urchin sperm axoneme.

Check out the details here: www.biorxiv.org/content/10.1...

👀 Looking for a PhD position but you are torn between cilia biology and computational AI research? 😜
The Cilia-AI Doctoral Network has you covered! Lots of fantastic projects throughout Europe, also @humantechnopole.bsky.social with us or @gaiapigino.bsky.social - apply now! ‼️
www.cilia-ai.eu

I am excited to share some of my PhD work on the motile cilia interactome revealed by XL/MS with @jbwallingford.bsky.social @edwardmarcotte.bsky.social Ophelia Papoulas, Chanjae Lee, David Taylor, and @builab.bsky.social www.cell.com/developmenta...

Our #CryoET paper on ciliary rootlet ultrastructure from mouse retina is now out in @elife.bsky.social! Have a peek with this video or dive deeper at bit.ly/3ZJzhgc. Big thanks to @carter-lab.bsky.social and #teamtomo.

#CryoET #CryoEM #Cilia #Rootlet #Centriole #Research #Science

This scheme shows the cargo adaptor FHF in the middle with arrows pointing to distinct microtubule and actin-based motors (dynein-dynactin, KIFC1, KIF1C and myosins V, IX and X as well as Tropomyosin 1). It also shows a link to Rab5 marked early endosomes. The hypothesis is that FHF coordinates multi motor binding at the early stages of endocytosis. The PhD project would address the hierarchy of motor binding and how these motors coordinate to allow the newly formed vesicle to transition from the actin to MT cytoskeletal network.

If you’re interested in how molecular motors coordinate to power intracellular trafficking events (e.g. endocytosis), I’ve got a PhD position available to study this at vibrant Bristol uni. In this project, we will capture highly dynamic events by #cryoEM, single molecule imaging & cell biology. 🔬❄️🧪

Thanks to @lisaheinke.bsky.social for guiding us through the process with lots of helpful feedback.