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Ben Goult

@bengoult.bsky.social
896 followers 776 following 133 posts

Talin as a memory molecule #MeshCODE. Talin shock absorbing materials #TSAM. Professor of Mechanistic Cell Biology at University of Liverpool Dad, Husband. Hobbies: Mechanobiology, talin, looking at the sky

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Reposted by Ben Goult
Junzhe @junzhe28.bsky.social · 09/09/2026
Excited to share that Saket Bagde @saketbagde.bsky.social and I @junzhe28.bsky.social are chairing the 2027 Fibronectin, Integrins & Related Molecules GRS in Ventura, CA, 6-7 Feb 2027! Theme: The 4D Matrisome: Integrating Architecture & Dynamics from Morphogenesis to Disease. Applications are OPEN!
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myosinactncrazy.bsky.social @myosinactncrazy.bsky.social · 02/09/2026
CCT8 associates with the MYO10 motor domain and regulates filopodia and breast cancer cell invasion journals.biologists.com/jcs/article/...
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Jon Humphries @jdhl18.bsky.social · 15/08/2026
Fantastic to see this paper out from @martinhumphries.bsky.social and collaborators Well done Mahak 👏
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Jon Humphries @jdhl18.bsky.social · 15/08/2026
FERMT3 alternative splicing enhances kindlin-3 membrane recruitment for neutrophil adhesion during stress myelopoiesis ashpublications.org/blood/articl...
ashpublications.org
FERMT3 alternative splicing enhances kindlin-3 membrane recruitment for neutrophil adhesion during stress myelopoiesis
Key Points. A four–residue IPRR insertion enhances kindlin-3 membrane recruitment and promotes β2 integrin activationFERMT3 alternative splicing dynamicall
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Mark Peifer (He, him) @peiferlabunc.bsky.social · 18/06/2026
The array of organs in the animal body differ dramatically in their architecture, but cell-cell adhesion mediated by cadherins is a common principle. Our lab usually focuses on epithelia but cadherins are also active in migrating mesenchymal cells like these migrating testis myoblasts 1/n 🧪
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Ben Goult @bengoult.bsky.social · 10/08/2026
The longer kindlin-3 isoform had previously been considered non-functional. Instead, we find that it is selectively upregulated during haematopoietic stress, suggesting that alternative splicing tunes integrin activation when the demand for neutrophils is high. Great collaboration with the Wen Lab
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Ben Goult @bengoult.bsky.social · 10/08/2026
New paper out today in Blood In this work led by Serena Lee, we show that alternative splicing of FERMT3 creates a kindlin-3 isoform with enhanced membrane recruitment, leading to stronger β2 integrin activation and neutrophil adhesion during stress myelopoiesis. DOI: doi.org/10.1182/bloo...
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Ben Goult @bengoult.bsky.social · 10/07/2026
New preprint! 🎉 We discovered an unexpected way that the postsynaptic scaffold protein Densin-180 binds SHANK proteins. Instead of using a conventional C-terminal PDZ-binding motif, Densin-180 uses an internal PDZ-binding motif that engages the canonical SHANK3 PDZ domain. 🧵1/8
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Ankita Jha @ankita13jha.bsky.social · 07/07/2026
Excited to share our new paper, now published in Nature Cell Biology! 🎉 We asked a fundamental question in cell biology: How do cells maintain polarity while migrating? Especially how do cancer cells navigate confined spaces? www.nature.com/articles/s41556-026-01981-1
nature.com
CD44 restricts EGFR mobility to polarize cytoskeletal signalling modules driving bleb-based migration - Nature Cell Biology
Jha et al. show that the transmembrane protein CD44 restricts EGFR mobility to maintain an EGFR–PI3K–Rac gradient during bleb-based cell migration.
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Ben Goult @bengoult.bsky.social · 10/07/2026
Congratulations to Yasumi Otani, Vignesh Srinivasan, Töller, Till Kallem and Neil Ball for their excellent work. Great collaboration with Kreienkamp and @saarikangaslab.bsky.social labs 8/8 www.biorxiv.org/content/10.6...
biorxiv.org
An internal PDZ-binding motif in Densin-180 promotes activity-dependent SHANK scaffold remodelling
SHANK proteins form core postsynaptic density (PSD) scaffolds that organise synaptic signalling complexes through multiple protein-protein interaction domains, including PDZ domains that typically rec...
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Ben Goult @bengoult.bsky.social · 10/07/2026
SHANK proteins and Densin-180 are both linked to autism spectrum disorders and other neurodevelopmental conditions, so understanding how they assemble synapses may help explain how disease-associated mutations disrupt neuronal function. 7/8
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Ben Goult @bengoult.bsky.social · 10/07/2026
This project started with a conversation during a PhD viva last year. Hans-Jürgen Kreienkamp and I were discussing our recent discovery that CDKL5 binds SHANK when he mentioned that his lab had identified a region of Densin-180 that also bound SHANK. That conversation became this project. 6/8
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Ben Goult @bengoult.bsky.social · 10/07/2026
Densin-180 does not bind a new surface on SHANK. Its internal motif directly competes with the canonical C-terminal CDKL5 ligand for the same PDZ groove. Even more strikingly, it binds SHANK1-3 but not PSD-95, showing that internal PDZ recognition is highly selective. 5/8
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Ben Goult @bengoult.bsky.social · 10/07/2026
We used the structure to design mutations that disrupt the Densin-180-SHANK interaction, then showed in neurons that this impairs activity-dependent SHANK scaffold assembly and dendritic spine plasticity. That is always my favourite part: connecting biochemistry with cell biology. 4/8
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Ben Goult @bengoult.bsky.social · 10/07/2026
One of my favourite things about this project is how visual the data are. The crystal structure gives beautifully defined electron density for the Densin-180 peptide within the SHANK3 PDZ groove. It's always satisfying when the structure tells such a clear story. 3/8
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Ben Goult @bengoult.bsky.social · 10/07/2026
www.biorxiv.org/content/10.6... 2/8
biorxiv.org
An internal PDZ-binding motif in Densin-180 promotes activity-dependent SHANK scaffold remodelling
SHANK proteins form core postsynaptic density (PSD) scaffolds that organise synaptic signalling complexes through multiple protein-protein interaction domains, including PDZ domains that typically rec...
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Ben Goult @bengoult.bsky.social · 10/07/2026
New preprint! 🎉 We discovered an unexpected way that the postsynaptic scaffold protein Densin-180 binds SHANK proteins. Instead of using a conventional C-terminal PDZ-binding motif, Densin-180 uses an internal PDZ-binding motif that engages the canonical SHANK3 PDZ domain. 🧵1/8
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Ben Goult @bengoult.bsky.social · 27/06/2026
✉️ Emails you love to receive. ✉️ Got email with this image on Thursday night, 2 Å diffraction from our new protein complex, with beautiful electron density defining the peptide interface. Huge credit to Till Kallem for getting these crystals. Hopefully we'll be sharing the full story very soon.
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Karin Pfisterer @pfistererkarin.bsky.social · 22/06/2026
🚨We are recruiting a Postdoc🚨 We are seeking a highly motivated Postdoctoral Researcher for our newly funded Horizon Europe Mission Cancer Melanoma Project! 🎯Apply, if you are interested in extracellular matrix-cancer cell interactions, tissue mechanics, advanced fluorescence imaging in 2D and 3D!
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Reposted by Ben Goult
Henry De Belly @henrydebelly.bsky.social · 10/06/2026
Very excited to be sharing our new paper, just out in Nature Cell Biology! The big question we investigate: How do migrating cells put their front 🔴 and back 🔵 in the right place?
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Ben Goult @bengoult.bsky.social · 11/06/2026
All expression constructs for the KANK1-4 ankyrin repeat domains and pathogenic variants used in this study are now available from @addgene.bsky.social. We hope they prove useful to others working on KANK biology, adhesions and microtubule regulation. www.addgene.org/browse/artic...
addgene.org
Addgene: The KN domain of KANK proteins contains separable talin-binding and intramolecular interaction modules
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Ben Goult @bengoult.bsky.social · 10/06/2026
Our current thinking is that either additional cellular/mechanical cues regulate this interaction, or that much of the KANK visible in cultured cells is already active. Either way, there is clearly more biology here to uncover.
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Ben Goult @bengoult.bsky.social · 10/06/2026
One aspect of the project that surprised us was the contrast between the biochemistry and the cell biology. The interaction was robust, conserved across the KANK family and easy to detect biochemically. Yet it was remarkably difficult to find a clear cellular consequence of disrupting it.
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Ben Goult @bengoult.bsky.social · 10/06/2026
New preprint We identify a conserved intramolecular interaction in KANK proteins. We show that the KANK KN domain contains separable functional modules: the LD motif mediates talin binding, while residues 60-68 mediate interaction with the KANK ankyrin repeat domain doi.org/10.64898/202...
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Ben Goult @bengoult.bsky.social · 01/06/2026
1/ Our new crystal structure is now available in the PDB (9SR0). It is the structure of the widely used A50I vinculin mutant bound to talin. Which is slightly awkward, because A50I is supposed to be a talin-binding-null mutant. rcsb.org/structure/9SR0
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Ben Goult @bengoult.bsky.social · 02/06/2026
All the constructs for working with new improved talin-binding-null mutant of vinculin are now on @addgene.bsky.social www.addgene.org/browse/artic...
addgene.org
Addgene: Talin controls the spatial distribution of vinculin tension in focal adhesions
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Ben Goult @bengoult.bsky.social · 01/06/2026
Sometimes the most interesting result comes from the control experiment. PDB: 9SR0 Preprint link www.biorxiv.org/content/10.6...
biorxiv.org
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Ben Goult @bengoult.bsky.social · 01/06/2026
3/ That observation sent us down a much bigger rabbit hole. We eventually showed that force can unfold talin rod domains and expose vinculin-binding sites that A50I can still bind, leading us to develop a new talin-binding-null mutant and revisit vinculin mechanotransduction.
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Ben Goult @bengoult.bsky.social · 01/06/2026
2/ The structure itself looks remarkably similar to wildtype. The surprise came from the biochemistry. A50I disrupts binding to some talin vinculin-binding sites, but retains essentially wildtype affinity for others.
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Ben Goult @bengoult.bsky.social · 01/06/2026
1/ Our new crystal structure is now available in the PDB (9SR0). It is the structure of the widely used A50I vinculin mutant bound to talin. Which is slightly awkward, because A50I is supposed to be a talin-binding-null mutant. rcsb.org/structure/9SR0
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Reposted by Ben Goult
Ben Goult @bengoult.bsky.social · 12/05/2026
1/ Our new preprint is out today.🎉 It started from a surprising control experiment while studying how talin binds vinculin. We were using the widely adopted A50I vinculin mutant to disrupt talin binding — but unexpectedly, it still bound talin. www.biorxiv.org/content/10.6...
Graphical Abstract showing how A50I still binds talin, how the new mutant abolishes binding and how this mutant allows us to show that vinculin tension gradient are lost when talin-vinculin interactions are abolished.
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Ben Goult @bengoult.bsky.social · 12/05/2026
Mine too, and that conference sounds great lol. Was such a surprise when the control bound tighter than the experiment, we had to go back and repeat it multiple times to sanity check it.
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Ben Goult @bengoult.bsky.social · 12/05/2026
💯
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Ben Goult @bengoult.bsky.social · 12/05/2026
Excellent collaboration led by Till Kallem, with the Hoffman, Hytonen, and Yan labs.
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Ben Goult @bengoult.bsky.social · 12/05/2026
However, what is lost is the spatial organisation of vinculin tension across adhesions. These findings suggest that talin does not simply recruit or load vinculin, but instead helps organise how mechanical forces are distributed within adhesion complexes.
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Ben Goult @bengoult.bsky.social · 12/05/2026
So we made a new vinculin mutant (I12K/A50I) that abolishes talin binding, even under mechanical force. This mutant is poorly recruited to adhesions, but surprisingly, the vinculin that does localise to adhesions is still able to experience mechanical load in the absence of direct talin binding.
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Ben Goult @bengoult.bsky.social · 12/05/2026
Vinculin is a central component of cellular force transmission, linking integrins to the actin cytoskeleton through interactions with talin. Because A50I has been widely used as a “talin-binding-null” mutant, we wanted to ask. What actually happens when talin binding is fully abolished?
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Ben Goult @bengoult.bsky.social · 12/05/2026
1/ Our new preprint is out today.🎉 It started from a surprising control experiment while studying how talin binds vinculin. We were using the widely adopted A50I vinculin mutant to disrupt talin binding — but unexpectedly, it still bound talin. www.biorxiv.org/content/10.6...
Graphical Abstract showing how A50I still binds talin, how the new mutant abolishes binding and how this mutant allows us to show that vinculin tension gradient are lost when talin-vinculin interactions are abolished.
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Reposted by Ben Goult
Johanna Ivaska @johannaivaska.bsky.social · 20/02/2026
What music should we play to our cells? This was the start of an amazing journey from @ivaskalab.bsky.social at @turkubioscience.bsky.social with Jasmin Kaivola and collaborators @sarawickstrom.bsky.social and others to explore larynx cancer mechanosensitivity! www.nature.com/articles/s41...
nature.com
Restoring the tumour mechanophenotype of vocal fold cancer reverts its malignant properties - Nature Materials
Vocal fold cancer tumours lose some of their malignant traits when mechanically stimulated by physiological stretch or vibrations, mimicking the opening and closing of vocal folds and phonation.
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Ben Goult @bengoult.bsky.social · 16/02/2026
Incredibly bright 🌈
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Guillaume Jacquemet @guijacquemet.bsky.social · 11/02/2026
Delighted to share our latest preprint "Filopodia-mediated trans-endocytosis" www.biorxiv.org/content/10.6... Work driven by many people including Hanna, Marcela, Sujan, Marie-Catherine, Anna and Monika. Fantastic collaboration with Johanna Englund, Emilia Peuhu, and Eija Jokitalo
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Jon Humphries @jdhl18.bsky.social · 08/02/2026
A TRPV4-dependent calcium signaling axis regulates lamellipodial actin architecture to promote cell migration: Current Biology www.cell.com/current-biol...
cell.com
A TRPV4-dependent calcium signaling axis regulates lamellipodial actin architecture to promote cell migration
Iu et al. uncover a Ca2+ signaling pathway promoting cell migration by facilitating actin assembly in protrusions. Ca2+ influx through TRPV4 channel activates RhoA in lamellipodia via CaMKII and TEM4,...
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Reposted by Ben Goult
Martin Humphries @martinhumphries.bsky.social · 30/01/2026
My personal obituary for Richard Hynes now live on the Manchester Cell-Matrix Centre website. www.manchester-matrix.org/news/profess...
manchester-matrix.org
Professor Richard O. Hynes PhD FRS (1944-2026) - Manchester Centre for Cell-Matrix Research
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Sarah Keary @lilkbot.bsky.social · 25/01/2026
Last night @museeorsay.bsky.social we saw fluorescence images of cells or protein filaments seemingly grow along the internal structures of the ceiling of the main hallway. It was mesmerising I loved it Science is Art! More of this please! Congratulations @manuelthery.bsky.social very cool 🤩🤓
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Guillaume Jacquemet @guijacquemet.bsky.social · 21/01/2026
🚨 We are hiring TWO postdocs to join the Cell Migration Lab (cellmig.org) 🇫🇮 as part of the new Centre of Excellence in Immune–Endothelial Interfaces (IMMENs). Join us to decode immune regulation & develop next-gen imaging tools! 🧪🔬 Details in thread 🧵👇 #ScienceSky #Postdoc #AcademicJobs Please RT🫶
cellmig.org
CELL MIGRATION LAB
We study cell migration in health and disease
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Ben Goult @bengoult.bsky.social · 20/01/2026
It provides a summary of our ongoing research to understand the binary switches built into the synaptic scaffold protein talin, and how these switch patterns change when synapses are stimulated.
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Ben Goult @bengoult.bsky.social · 20/01/2026
Check out our new Talin Infographic! The poster summarises why we think there is a binary code in animals. Great artwork made by Josh Hawley @golgigraphics.bsky.social
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Ben Goult @bengoult.bsky.social · 14/01/2026
Excited to share our new preprint! and the surprising finding that the second integrin-binding site (IBS2) does not bind integrin. IBS2 can be better explained as talin-talin interactions mediated via a cryptic talin-binding site in R11. We also show a new role for vinculin as a mechano-chaperone
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Ben Goult @bengoult.bsky.social · 14/01/2026
When R11 unfolds it exposes a cryptic Aggregation Prone Region, which we call APR1. This motif mediates talin-talin oligomerisation. Excitingly vinculin binding resolves these talin oligomers revealing that vinculin acts as a mechano-chaperone to maintain mechanotransduction through talin.
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Ben Goult @bengoult.bsky.social · 14/01/2026
Great collaboration with Vesa Hytonen and Jie Yan's teams and led by Neil Ball in my lab @liverpooluni.bsky.social
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