Seminars & Events

This is an in-person talk only with no online option.

External attendees please arrive 10 minutes early to sign in at LMB Reception

Cellular reprogramming by the simultaneous expression of OCT4, SOX2, KLF4 and MYC (OSKM) is a fascinating process known to erase many aspects of molecular aging, particularly those related to transcriptional regulation and epigenetics. Despite its profound therapeutic potential for restoring health and fitness to diseased or aged tissues, significant translational challenges remain. This seminar will present an update on our research into the in vivo cellular and tissue-level changes induced by OSKM expression. Finally, I will explore the hypothesis that the mechanisms underlying cellular reprogramming are fundamentally interconnected with innate tissue regeneration.

External attendees, if you wish to attend, please contact Jan Löwe: jyl@mrclmb.ac.uk

Abstract: Spiroplasma is a unique helical bacterium without a cell wall. The cytoskeletal proteins of Spiroplasma, including 5 paralogs of the bacterial actin MreB and fibril, a cytoskeletal protein of novel fold, help it to achieve its unique shape. The cytoskeletal ribbon formed also function as its motility machinery. The current understanding in the field for bacterial shape determination and division is based on studies carried out on cell walled bacteria, in which the peptidoglycan synthesis machinery plays an important role along with the cytoskeleton. Understanding the action of the bacterial cytoskeletal proteins MreB and FtsZ in Spiroplasma will help in unravelling the fundamental mechanism of cytoskeletal function in shape and division in the absence of peptidoglycan synthesis. Our insights on shape determination and kink-based motility of Spiroplasma based on in vitro reconstitution of the protein complexes on liposomes will be presented.

External attendees, if you would like to attend, please contact Lori Passmore: passmore@mrc-lmb.cam.ac.uk

Abstract: Cell signaling orchestrates cellular development and physiology. Yet, how cells process information at the molecular level to make decisions adapted to their surroundings and internal state remains poorly understood. Many signals are physically processed through multivalent protein–protein interactions mediated by modular peptide-binding domains. Domains’ promiscuity facilitates pathway crosstalk, while their unique interaction affinities and protein contexts ensure signal specificity. The development of methods to quantify domain binding affinity across the proteome, however, has been stymied by the large diversity of modular domains in Metazoa combined with their weak and transient interaction biophysics and sensitivity to subtle sequence variation. In my talk, I will describe how I overcome these challenges by developing a biophysically-informed machine learning method for predicting domain binding affinity directly from amino acid sequence. Applying my method proteome-wide yields fundamental insights into signaling biophysics and enables the construction of molecularly-mechanistic protein interaction networks that display emergent signaling functions. These quantitative molecular models, thus, provide a foundation to decode the biophysical logic of cell signaling so that we can quantitatively predict, mechanistically explain, and engineer new cellular behaviors.

https://mrc-lmb-cam-ac-uk.zoom.us/j/93380539076?pwd=Zgm76hrbs70yPVlSJ0YEHyhRKaMVKS.1

External attendees please arrive 10 minutes early to sign in at LMB Reception

Messenger RNA levels are controlled by a balance between transcription and mRNA decay. Viral infection offsets this balance, often dramatically, leading to widespread changes to the cellular RNA pool. What signals trigger such global changes in mRNA transcription, and how do cells appropriately tune transcriptional responses to pathogenic stress? We investigate these questions by probing gene regulatory responses to viral infection. I will discuss how virus-activated cytoplasmic mRNA decay leads to extensive repression of mRNA transcription via redistribution of RNA-binding proteins. However, cellular stress response genes must retain their ability to be transcriptionally activated. We find a surprising role for RNA polymerase III, which is strongly activated by DNA virus infection, in tuning transcription at these coding gene loci. Thus, infection can significantly alter the activity of RNA polymerases II and III, thereby reconfiguring the gene expression landscape.

External attendees, if you wish to attend in person please contact Felix Randow randow@mrclmb.ac.uk or Leo James@mrclmb.ac.uk

External attendees, if you would like to attend in person please contact Max Behzadi: mbehzadi@mrc-lmb.cam.ac.uk

External attendees, if you wish to attend in person please contact Leo James: lcj@mrclmb.ac.uk

Abstract to follow

2-3 July 2026

See website for further information https://www3.mrc-lmb.cam.ac.uk/sites/gsasymposium/

2-3 July 2026

See website for further information https://www3.mrc-lmb.cam.ac.uk/sites/gsasymposium/

https://mrc-lmb-cam-ac-uk.zoom.us/j/94514662338?pwd=QFmpzVDjmvrrMmV476z2wynx6r2aoA.1

Register here: https://www.enterprise.cam.ac.uk/events/new-technologies-and-building-successful-biotechnology-companies-to-treat-disease/#harvey-lodish‑register

Celebrating his return to Cambridge and the MRC Laboratory of Molecular Biology (LMB), we are delighted to welcome Professor Harvey Lodish, Professor of Biology and Biological Engineering at MIT, who undertook his postdoctoral research at the LMB with Drs Sydney Brenner and Francis Crick, for a special lecture and discussion.

The event will explore how fundamental scientific discovery can be translated into real‑world benefit and the role universities play in supporting that journey with integrity, responsibility, and long‑term vision.

Professor Lodish will share insights from his academic career and his experience founding and advising biotechnology companies, including perspectives on mentorship, ethics, and the relationship between research excellence and enterprise. The lecture will be followed by a panel discussion, Q&A, and networking over lunch.

This unique opportunity is open to academics, postdoctoral researchers, and staff from across the Biomedical Campus, including the LMB, Clinical Schools, Milner Therapeutics Institute, and partner organisations

Schedule for the day:
10.00 – Arrival & coffee
10.30 – Welcome
10.45 – Special Lecture with Professor Harvey Lodish: New Technologies and Building Successful Biotechnology Companies to Treat Disease: A Personal History
11.45 – Panel & Q&A
12.30 – Lunch
13.30 – Event close

External attendees, if you would like to attend in person please contact Max Behzadi: mbehzadi@mrc-lmb.cam.ac.uk

This will be a joint seminar, please see both abstracts below.

Delphine’s Abstract:
Two-pore domain potassium channels regulate neuronal excitability through hyperpolarizing leak currents and play important roles in sensory physiology. Among them, THIK1 and THIK2 remain poorly characterized despite their strong enrichment in nociceptive dorsal root ganglion (DRG) neurons. In this seminar, we will present a multidisciplinary study combining molecular analyses, electrophysiology, and behavioral approaches to investigate the contribution of THIK channels to sensory neuron excitability and pain processing under physiological and inflammatory conditions. THIK1 and THIK2 expression patterns were characterized in mouse DRG, while whole-cell recordings and behavioral analyses were used to explore the consequences of THIK deletion on neuronal function and nociceptive responses. Our findings reveal an unexpected role for THIK channels in the regulation of sensory neuron activity and thermal pain sensitivity, highlighting these poorly understood K2P channels as potential new players in inflammatory pain mechanisms and possible therapeutic targets for chronic pain disorders.

Franck’s Abstract:
Despite being the first channel in the K2P family to be cloned, TWIK1 remains largely mysterious in terms of its physiological role. We have shown that its sensitivity to extracellular pH is accompanied by a change in its ionic selectivity, thereby reinforcing questions about its function. At neutral physiological pH, TWIK1 is, like most potassium channels, selective for K+ ions. However, when exposed to a pH below 6—as occurs in the recycling endosomes it transits during intracellular trafficking—the channel undergoes conformational changes. These changes alter the structure of its selectivity filter, rendering TWIK1 permeable to Na+ ions. We have identified the molecular determinants responsible for this pH sensitivity and proposed a model describing the sequence of molecular events occurring around the selectivity filter during the gradual acidification of the extracellular environment. Research into the physiological role of this dynamic selectivity suggests that, in certain functional contexts, TWIK1’s preference for potassium ions may not be absolute, nor even indispensable.

An informal one day meeting organised by MRC LMB, MRC LMS and Imperial College London examining the application of cutting edge biophysical techniques in complex biological settings. Bringing together scientists in both academia and industry for stimulating talks and discussions how these new and emerging technologies may be able to address challenging questions in the future.

For more information see https://www3.mrc-lmb.cam.ac.uk/sites/nextgen/

External attendees, if you wish to attend in person please contact Tanmay Bharat: tbharat@mrc-lmb.cam.ac.uk

Abstract to follow

External attendees, if you would like to attend in person please contact David Favara: dfavara@mrc-lmb.cam.ac.uk

Adhesion GPCRs are among the most intriguing unresolved problems in receptor biology. The key challenge for their understanding is to decipher their input-output relationship. Their unusual architecture and sensitivity to mechanical and adhesive inputs raise a central question: how are extracellular cues converted into defined signalling outputs? Unlike classical GPCRs, they do not merely bind soluble ligands but instead sense and interpret mechanical stimuli through an elaborate molecular architecture built around the GAIN domain and a cryptic intramolecular agonist. I will present recent work that brings this problem into quantitative focus through through a combination of biophysical measurements and method development: tools for acute, time-controlled receptor activation, strategies for engineered ligand engagement, and force-resolved assays that capture GAIN-domain unfolding, receptor dissociation and mechanochemical signalling. Together, these approaches reveal how adhesion GPCRs convert mechanical and adhesive information into distinct downstream responses. This emerging framework recasts adhesion GPCRs as measurable signalling machines and opens a route towards understanding their roles in neural development, tissue organisation, immunity and cancer with molecular precision.

Abstract: TBC

https://mrc-lmb-cam-ac-uk.zoom.us/j/94514662338?pwd=QFmpzVDjmvrrMmV476z2wynx6r2aoA.1