We are hiring a Research Associate to join our lab in Bristol School of Chemistry. The project will involve protein design and engineering to understand and control intracellular transport. Please share and get in touch if you are interested! jesscrosslab.org tinyurl.com/2aesevsu

Jess Cross Lab

Engineering Biology lab at the University of Bristol

jesscrosslab.org

Our latest review is out. We take a deep dive into the human mutations in microtubule motors that drive devastating neurodevelopmental and neurodegenerative diseases. Taking in motor protein biophysics, animal models of disease as well as patient phenotypes. onlinelibrary.wiley.com/doi/full/10....

🚨 New review article by Carrington and co-authors: Smooth muscle contractile cytoskeleton in health and disease doi.org/10.1007/s109... #smooth-muscle #disease #myoblue This article is part of the Smooth Muscle Cell Function in Health and Disease collection: link.springer.com/collections/...

Smooth muscle contractile cytoskeleton in health and disease - Journal of Muscle Research and Cell Motility

Smooth muscle cells are widespread in the human body, found in a range of tissues from the vasculature to the gut, airways, bladder and so on. They can be found as isolated cells or organised into syncytia (groups of cells). The organisation of the contractile cytoskeleton (smooth muscle actin and myosin filaments) is less well understood than that of striated (cardiac and skeletal) muscle. This review aims to explore what is known, the potential effects of mutations in smooth muscle actin, myosin and tropomyosin and how they lead to disease, and to highlight what we have still to learn about the smooth muscle contractile cytoskeleton.

doi.org

Using iPALM to determine protein organisation in cardiac muscle Z-discs www.biorxiv.org/content/10.6...

Cryo-EM reveals how cardiomyopathy therapeutic drugs modulate the myosin motors of the heart pubmed.ncbi.nlm.nih.gov/42054467/ #cryoEM

Phenomenally proud that this work is out in the wild now - excellent feeling having my qXL-MS of myosin conformational dynamics paired with @snmcmillan.bsky.social incredible cryo-EM work and analysis. A real team effort from @scarfflab.bsky.social www.science.org/doi/10.1126/...

Mavacamten inhibits myosin activity by stabilizing the myosin interacting-heads motif and stalling motor force generation

Mechanism of the myosin inhibitor mavacamten is revealed by cryo-EM and cross-linking studies.

science.org

New preprint! We asked a simple question: How do very different activating adaptors all activate dynein? Turns out: same architecture, wildly different implementations 🧵👇 doi.org/10.64898/202...

🚨 New review out in @jmrcm-springer.bsky.social 🧬 From the @michellepeckham.bsky.social lab, we summarise how smooth muscle myosin is regulated—covering autoinhibition, filament assembly, and structural insights into motor control and disease. 👉 rdcu.be/feUiX

Smooth muscle contractile cytoskeleton in health and disease - Journal of Muscle Research and Cell Motility

Smooth muscle cells are widespread in the human body, found in a range of tissues from the vasculature to the gut, airways, bladder and so on. They can be found as isolated cells or organised into syncytia (groups of cells). The organisation of the contractile cytoskeleton (smooth muscle actin and myosin filaments) is less well understood than that of striated (cardiac and skeletal) muscle. This review aims to explore what is known, the potential effects of mutations in smooth muscle actin, myosin and tropomyosin and how they lead to disease, and to highlight what we have still to learn about the smooth muscle contractile cytoskeleton.

doi.org

🚨 New paper alert 🧬 Our work from the @michellepeckham.bsky.social lab is now out in #ScienceAdvances. We present the #cryoEM structure of shutdown human non-muscle myosin 2A, showing how ionic interactions stabilise auto-inhibition and how mutations disrupt this state. 👉 tinyurl.com/4de8teyh

Two manuscripts from the lab to catch up upon exploring aspects kinesin-1 regulation. First, our examining the role of cargo-adaptor binding in controlling kinesin-1 conformational dynamics and association with MAP7 is now a VOR @elife.bsky.social elifesciences.org/articles/109...

Kinesin-1 conformational dynamics are controlled by a cargo-sensitive TPR switch

Cargo-adaptor binding to the KLC-TPR domains binding triggers structural rearrangements that relieve kinesin-1 autoinhibition, enabling MAP7 recruitment, through an allosteric mechanism that connects ...

elifesciences.org

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...)

The peer reviewed and updated version of this work is now online (although not quite the fully formatted version). We had an existential crisis about kinesin-1 regulation while developing this work, but we are super proud of everything we put into this project. www.cell.com/iscience/ful...

Kinesin-1 is highly flexible and adopts an open conformation in the absence of cargo

Kinesin-1 is an essential anterograde microtubule motor protein. The core kinesin motor is a homodimer of two heavy chains; N-terminal motor domains hydrolyse ATP and walk along microtubules, whilst a...

cell.com

Ali Twelvetrees @dozenoaks.bsky.social · 2y ago

Still have energy for science in the dark end of the year? Our new preprint is up. The tl;dr - we took a deep dive on kinesin-1 conformational dynamics and came up with a model that is basically “it’s really floppy”. Evie who led the work compared it to the air dancer gifs, and now I can’t unsee it.

Cryo-EM structure of shutdown human non-muscle myosin 2A www.biorxiv.org/content/10.1101/2025.10.15.682586v1 #cryoEM

Structure of the autoinhibited state of non-muscle myosin IIA - shows a different mechanism than seen for beta-cardiac myosin. www.biorxiv.org/content/10.1...

Cryo-EM structure of shutdown human non-muscle myosin 2A

Determining the high-resolution structure of the widely expressed non-muscle myosin 2A (NM2A), in its dephosphorylated shutdown state, is important in understanding its regulation and disease roles. I...

biorxiv.org

🚨 New paper alert! 🧬 Excited to share our latest preprint from the @michellepeckham.bsky.social lab 🎉 We reveal the structure of human non-muscle myosin 2A — showing how ionic interactions control auto-inhibition ⚡ and how disease mutations disrupt it 💪 👉 tinyurl.com/4fkxfv4e #cryoEM #myosin

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

Delighted to see Jon Machin's lovely OMP folding and assembly work on the front cover of JMB (doi: 10.1016/j.jmb.2025.169346) and in this Faraday Discussion article (doi: 10.1039/d4fd00180). Congratulations on your great work Jonathan!

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 😆

Swinging lever mechanism of myosin shown by time-resolved cryoEM www.nature.com/articles/s41... so glad to finally be able to share this with the community! @astburycentre.bsky.social @astbury-bsl.bsky.social @stemuench.bsky.social @snmcmillan.bsky.social @davidklebl.bsky.social

Swinging lever mechanism of myosin directly shown by time-resolved cryo-EM - Nature

A study using time-resolved cryogenic electron microscopy reveals the swinging lever mechanism of myosin, providing information on the molecular basis behind the production of force and movement by my...

nature.com

👋👋 Hi everyone! The Astbury Centre is now on Bluesky. Follow along for updates about exciting Astbury Centre science. For now, we have put together a starter pack of members of the Astbury Centre community.

We have a new 4-year postdoctoral position available working between our lab at the Woolfson lab at Schools of Biochemistry and Chemistry at Bristol. Applying protein design approaches to control intracellular transport. More info on link and flyer. Get in touch! www.bristol.ac.uk/jobs/find/de...

PhD studentship available! #AstburyCentre CryoEM & MD simulation to understand cardiac muscle function in health and disease Apply by 5th Jan www.findaphd.com/phds/project...

Unravelling the mechanisms of cardiac myosin function in health and disease through molecular dynamic simulation and electron microscopy at University of Leeds on FindAPhD.com

PhD Project - Unravelling the mechanisms of cardiac myosin function in health and disease through molecular dynamic simulation and electron microscopy at University of Leeds, listed on FindAPhD.com

findaphd.com