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BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260303T140000
DTEND;TZID=Europe/Paris:20260303T140000
DTSTAMP:20260404T115923
CREATED:20260227T153207Z
LAST-MODIFIED:20260227T153207Z
UID:10000089-1772546400-1772546400@sfp-alpes.fr
SUMMARY:Marco MACCARINI (chercheur UGA)
DESCRIPTION:Exploring the Nanostructure of Biomimetic Membranes\nRésumé : \nModel lipid membranes are simplified yet powerful systems that mimic key features of biological plasma membranes—the essential envelopes that define and protect living cells. Their controlled simplicity makes them ideal for precise experimental techniques\, enabling us to explore their interactions with novel nanoengineered materials. \nWhen combined with biological components like proteins\, these membranes not only deepen our understanding of fundamental biological processes but also serve as building blocks for advanced nanoengineered materials with tailored technological applications. \nIn this seminar\, I will present examples from my research\, where laboratory techniques\, large-scale facility analyses\, and computational methods converge to provide in-depth characterization and mechanistic insights into membrane behavior. These findings hold significant potential for advancements in health\, biotechnology\, and fundamental biology. \nShort Bio/CV\nAs  a CNRS Chargé de Recherche\, I’ve recently joined the LMGP to continue my research journey in this scientific new environment. My academic path has taken me across borders—starting with a Physics degree in Italy\, followed by a PhD in Polymer Physics in England\, and postdoctoral experiences in Germany and Canada. Along the way\, I’ve had the privilege of working at world-class facilities like the Institut Laue Langevin\, where I deepened my expertise in large-scale scientific infrastructure. I now continue this work at LMGP\, where my research focuses on the intersection of physics\, materials science\, and biomimetic systems. \nContact : deborah.verger@grenoble-inp.fr
URL:https://sfp-alpes.fr/event/marco-maccarini-chercheur-uga/
LOCATION:LMGP – salle des séminaires\, Grenoble INP -Phelma 3 parvis Louis Néel\, Grenoble\, 38054\, France
CATEGORIES:Séminaire
ORGANIZER;CN="LMGP":MAILTO:deborah.verger@grenoble-inp.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260305T113000
DTEND;TZID=Europe/Paris:20260305T123000
DTSTAMP:20260404T115923
CREATED:20260227T134443Z
LAST-MODIFIED:20260227T134815Z
UID:10000084-1772710200-1772713800@sfp-alpes.fr
SUMMARY:Viviana RICON MONTES & Andreas OFFENHÄUSSER (Forschungszentrum Jülich\, Allemagne)
DESCRIPTION:Devices that interact with the brain: from nanostructured to flexible electrodes\nRésumé : \nNeural electrodes are the core components of neuroelectronic devices\, enabling the recording and simulation of neural activity. Our research focuses on two primary areas : (1) the design and\ncharacterization of the neuron-electrode interface\, and (2) the development of flexible neural interfaces for both in vivo and in vitro applications. Microelectrode arrays (MEAs) are commonly used to bridge the interface between neurons and electronic systems. However\, current MEAs face limita7ons in signal fidelity\, precision of neural modulation\, and long-term biocompatibility. To address these challenges\, we are developing nanomaterial-based MEAs that offer enhanced physical and chemical properties\, leading to improved cell-electrode coupling. Specifically\, we have engineered a hybrid structure combining vertical nanostraws with nanocavities\, enabling stable\, non-invasive\, and long-term recording at sub-threshold resolution. \nImplantable neural prosthetic devices provide direct access to local neural circuits and are critical components of brain-machine interfaces. While current clinical-grade devices—typically based on silicon or noble metals—have driven significant advances\, they oPen fail to sustain reliable neural communication over extended periods. Our goal is to create next-generation neurotechnologies that integrate seamlessly with biological tissue\, supporting multimodal neural interrogation through electrical\, optical\, or chemical means. We are actively exploring novel device architectures\, materials\, and implantation strategies\, alongside rigorous performance evaluation\, with the ultimate aim of enabling both acute and chronic in vivo applications. Our approach combines thin-film technology and surface micromachining processes with additive manufacturing techniques\, including two-photon lithography. These are integrated with self-\naligned\, template-assisted electrodeposition processes\, kirigami-inspired designs with matched-die forming\, novel bonding methods\, and the modular stacking of two-dimensional neural probes with key-lock systems. These technologies support versatile applications\, ranging from investigating seizure-like activity in in vitro epilepsy models to advancing visual prosthesis that enable bidirectional communication along the visual pathway. \nContact : clement.hebert@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/viviana-ricon-montes-andreas-offenhausser-forschungszentrum-julich-allemagne/
LOCATION:GIN – Amphi Serge Kampf\, Grenoble Institut des Neurosciences (GIN) Bât. Edmond J. Safra\, Chemin Fortune Ferrini CHU\, La Tronche\, 38700\, France
CATEGORIES:Séminaire
ORGANIZER;CN="GIN":MAILTO:yves.goldberg@univ-grenoble-alpes.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260306T140000
DTEND;TZID=Europe/Paris:20260306T150000
DTSTAMP:20260404T115923
CREATED:20260305T145615Z
LAST-MODIFIED:20260305T145620Z
UID:10000093-1772805600-1772809200@sfp-alpes.fr
SUMMARY:Carlo PIFFERI (Centre de Biophysique Moléculaire\, Orléans)
DESCRIPTION:Exploiting disulfide-rich peptides as protein epitope mimics : development of a generalizable conjugation approach for immunogen preparation\nRésumé : \nGeneration of specific antibodies against peptides by immunization requires their covalent conjugation to protein carriers to override their inherently weak immunogenicity. The vast majority of bioconjugation approaches to achieve peptide-protein constructs rely on thiol-maleimide chemistry1 and capitalize on a wide array of commercial maleimide-functionalized protein carriers. Disulfide-rich peptides2 (DRPs) possess a rigid\, constrained structure that makes them ideal for designing synthetic mimics of protein regions/domains. For bioconjugation purposes\, the introduction of a single spare thiol moiety into a linear peptide antigen is straightforward\, while DRPs’ disulfide bonds are prone to intramolecular thiophilic attack by the reactive thiolate. This unintended reactivity competes with the desired Michael addition to the maleimide moiety\, ultimately disrupting the native disulfide bridging framework. As a result\, DRP’s tertiary structure will be altered\, affording an immunogen that is a poor mimic of the native target. Although a few studies have explored the late-stage introduction of thiol-containing cross-linkers onto DRP antigens for their conjugation onto protein carriers\,3\,4 the stability of DRP’s disulfide pattern in the presence of an extra thiol has never been examined. To address this\, we systematically evaluated the influence of different spacers in “DRP-spacer-thiol” constructs\, under thiol-maleimide reaction conditions.5 Our results highlight how both linker length and flexibility are key to maintain DRP disulfides unaltered\, providing a general approach to achieve DRP bioconjugation by thiol-maleimide chemistry. We have applied our approach to a small DRP predicted to closely mimic a surface-accessible epitope of the full LINGO-1 protein\, and obtained a very specific antibody response upon immunization: the resulting polyclonal IgG was able to selectively bind the full-length protein in a cellular context\, with stringent selectivity across its four homologs. \nReferences : \n1. M. Góngora-Benítez\, J. Tulla-Puche & F. Albericio\, Chem. Rev. 2014\, 114\, 901–926.\n2. K. Renault\, J. W. Fredy\, P.-Y. Renard & C. Sabot\, Bioconjug. Chem. 2018\, 29\, 2497–2513.\n3. H. Katayama & M. Mita\, Bioorganic Med. Chem. 2016\, 24\, 3596–3602.\n4. H. Katayama\, R. Mizuno & M. Mita\, Biosci. Biotechnol. Biochem. 2019\, 83\, 1791–1799.\n5. L. Azzoug et al.\, ChemRxiv 2025\, DOI:10.26434/chemrxiv-2025-krjcm \n_ \nContact : david.goyard@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/carlo-pifferi-centre-de-biophysique-moleculaire-orleans/
LOCATION:DCM – Salle C209\, DCM - Bât Chimie Recherche 301 rue de la Chimie\, St Martin d'Hères\, 38400\, France
CATEGORIES:Séminaire
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260312T130000
DTEND;TZID=Europe/Paris:20260312T140000
DTSTAMP:20260404T115923
CREATED:20260213T093616Z
LAST-MODIFIED:20260226T095902Z
UID:10000066-1773320400-1773324000@sfp-alpes.fr
SUMMARY:Stéphane GUINDON (LIRMM - Montpellier)
DESCRIPTION:Recent advances in phylogeography\nContact : lucie.lamothe@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/stephane-guindon-lirmm-montpellier/
LOCATION:IMAG – Salle de Réunion\, 150 place du Torrent\, St Martin d’Hères\, 38400\, France
CATEGORIES:Séminaire
ORGANIZER;CN="TIMC - IMAG":MAILTO:lucie.lamothe@univ-grenoble-alpes.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260312T183000
DTEND;TZID=Europe/Paris:20260312T223000
DTSTAMP:20260404T115923
CREATED:20260130T145238Z
LAST-MODIFIED:20260130T153923Z
UID:10000048-1773340200-1773354600@sfp-alpes.fr
SUMMARY:Hugues Nury (Irig / IBS)
DESCRIPTION:« Soirée du vivant » : récepteurs neuronaux : comment les poisons trouvent leur cible\nCette « S​​oirée du vivant »\, d’un format inédit\, proposera présentation interactive\, quiz participatifs\, échanges libres\, le tout autour de tapas végétales\, pour un moment convivial et grand public.\n​\nHugues Nury\, chercheur CNRS à l’Institut de biologie structurale de Grenoble\, nous plongera dans l’univers fascinant des venins de serpents\, alcaloïdes végétaux et autres insecticides modernes\, qui exercent leurs effets en ciblant des récepteurs neuronaux spécifiques. Il apportera d’abord des connaissances générales pour répondre à des questions essentielles telles : pourquoi certaines substances sont-elles mortelles à des doses infimes tandis que d’autres restent inoffensives ? Comment un récepteur neuronal reconnaît-il son « poison » ?​​​​\n​\n​Il présentera ensuite le projet ANR Pesti Penta qu’il coordonne\, et qui vise à comprendre les mécanismes moléculaires d’action des insecticides sur les récepteurs neuronaux d’insectes. Cette recherche combine biologie structurale\, dynamique moléculaire et électrophysiologie afin d’explorer les interactions entre différentes molécules et leurs cibles biologiques.\nÀ terme\, l’objectif de ces travaux fondamentaux est de contribuer au développement d’insecticides plus efficaces et plus ciblés. \nEn savoir plus : https://www.cea.fr/drf/irig/Pages/Animation-scientifique/seminaires/2026_Nury.aspx
URL:https://sfp-alpes.fr/event/hugues-nury-irig-ibs/
LOCATION:La Casemate\, 2 Place Saint-Laurent\, Grenoble\, 38000\, France
CATEGORIES:Conférence
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260313T110000
DTEND;TZID=Europe/Paris:20260313T120000
DTSTAMP:20260404T115923
CREATED:20260227T095412Z
LAST-MODIFIED:20260227T095425Z
UID:10000078-1773399600-1773403200@sfp-alpes.fr
SUMMARY:Peter DAHLBERG (Stanford University\, USA)
DESCRIPTION:Fluorescence-guided cryogenic FIB milling and their application to the study of the NLRP3 inflammasome\nRésumé : \nNumerous critical events in cell biology depend on rare ( 1 copy per cell) and small (<500 nm in diameter) structures. Observation of these processes at high resolution using cryogenic electron tomography (CryoET) presents challenges\, as the structures must first be precisely targeted within thin sections through focused ion beam milling. In this presentation\, I will introduce my group’s work on a tri-coincident system that integrates light\, ion\, and electron microscopy at a single focal point. This approach enables real-time monitoring of the milling process and makes two different modes of guidance possible that require no addition of fluorescent fiducials or image registration and whose accuracy far exceeds the optical diffraction limit. I will discuss both guidance modes in detail and then describe their application to the study of the in situ structure of the NLRP3 inflammasome. Despite its central role in innate immunity as a master regulator responsible for proinflammatory cytokine maturation and cell death\, its in situ structure has remained elusive due to challenges in capturing the small singular punctum it forms per cell in thin sections compatible with CryoET — precisely the kind of target the tri-coincident system was developed for. Using our guidance approach\, our cryo-tomograms revealed that the NLRP3 inflammasome forms a dense condensate within and around the microtubule-organizing center. At a later stage after activation\, we saw further growth of the condensate\, and the cells underwent pyroptosis with widespread mitochondrial damage and autophagy. Our study revealed new insights into NLRP3 structure and other organelle alterations during inflammation. \nContact : ibs.seminaires@ibs.fr
URL:https://sfp-alpes.fr/event/peter-dahlberg-stanford-university-usa/
LOCATION:IBS – Salle des séminaires\, IBS 71 avenue des Martyrs\, Grenoble\, 38042\, France
CATEGORIES:Séminaire
ORGANIZER;CN="IBS":MAILTO:ibs.seminaires@ibs
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260316T110000
DTEND;TZID=Europe/Paris:20260316T120000
DTSTAMP:20260404T115923
CREATED:20260312T153257Z
LAST-MODIFIED:20260312T153303Z
UID:10000100-1773658800-1773662400@sfp-alpes.fr
SUMMARY:Martha MERROW (LMU Munich\, Germany)
DESCRIPTION:A circadian clock in Bacillus subtilis\nRésumé : \nThe circadian clock is a molecular machine that is present in each one of our cells\, directing diverse processes in a cell(developmentally)-specific manner. The natural state of the clock is ‘entrainment’\, namely through synchronization with zeitgeber signals (such as the light/dark cycle) in the environment. Once moved to constant conditions\, a free running rhythm of approximately 24h can be observed\, demonstrating the endogenous nature of the clock. One can understand how the clock relates to our lives by noting the timing of the sleep wake cycle: this is determined by the interaction of the biological (circadian) oscillator and the external zeitgeber cycle. Disrupting the clock in humans and mice leads to increased cancers\, metabolic disease and decreased cognitive performance\, likely through misexpression of key regulators. The circadian clock is an essential aspect of biology and its function can be regarded as a biophysical phenomenon. \nCircadian clocks have been described in all kingdoms of life except for the Eubacteria – until very recently. I will discuss the circadian clock in the model prokaryote\, Bacillus subtilis. We observe rhythms in gene expression\, in colony morphology on agar\, and in metabolism and in planktonic cultures. The circadian transcriptome shows pervasive regulation of gene expression by the biological clock\, even more extensively than sigma factors. The clock is thus a major regulatory phenomenon in this bacterium. Our work begs the questions ‘what is the same as clocks in higher organisms?’ and ‘what is different?’. \nContact : irina.mihalcescu@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/martha-merrow-lmu-munich-germany/
LOCATION:LiPhy\, Salle de Conférence\, 140 rue de la Physique\, St Martin d'Hères\, 38400
CATEGORIES:Séminaire
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260317T140000
DTEND;TZID=Europe/Paris:20260317T150000
DTSTAMP:20260404T115923
CREATED:20260227T144116Z
LAST-MODIFIED:20260227T144239Z
UID:10000085-1773756000-1773759600@sfp-alpes.fr
SUMMARY:Montserrat SOLER-LÓPEZ (Macromolecular X-ray Crystallography\, Imaging and Scattering Group\, ESRF)
DESCRIPTION:Mitochondrial Bioenergetics in Alzheimer’s Disease : Insights from the European Synchrotron\nRésumé : \n\nAlzheimer’s disease (AD) is a devastating neurodegenerative disorder increasingly linked to defects in mitochondrial bioenergetics. At the European Synchrotron Radiation Facility (ESRF)\, we investigate the structural and functional mechanisms that underlie mitochondrial dysfunction in AD\, with a focus on respiratory complex I\, a central player in cellular energy production [1\,2]. \nUsing an integrative biology approach\, we combine macromolecular crystallography\, cryo-electron microscopy\, X-ray imaging\, and spectroscopy to analyse the architecture and regulation of mitochondrial complex I and its assembly factors (MCIA proteins) across spatial and temporal scales. Our structural and functional studies reveal novel regulatory mechanisms of energy metabolism\, including phosphorylation-dependent modulation at the interface of respiration and fatty acid oxidation. Importantly\, we demonstrate that AD-related amyloid oligomers disrupt these regulatory processes within neuronal mitochondria\, thereby contributing to oxidative stress and impaired bioenergetics in AD [3\,4]. Recent synchrotron-based imaging\, including X-ray fluorescence and nano-tomography\, has further provided first insights into the ultrastructure of mitochondrial assemblies in situ. \nCollectively\, these findings highlight how the ESRF’s interdisciplinary\, state-of-the-art methodologies enable breakthroughs in deciphering the molecular basis of neurodegeneration\, offering new perspectives for diagnostic markers and therapeutic strategies targeting mitochondrial dysfunction in Alzheimer’s disease. \n[1] Giachin et al. Dynamics of Human Mitochondrial Complex I Assembly: Implications for Neurodegenerative Diseases. Front. Mol. Biosci. 2016\, 3:43 \n[2] McGregor & Soler-Lopez. Structural basis of bioenergetic protein complexes in Alzheimer’s disease pathogenesis. Cur Opin Struct Biol. 2023\, 80:102573 \n[3] Giachin et al. Assembly of The Mitochondrial Complex I Assembly Complex Suggests a Regulatory Role for Deflavination. Angew. Chem. Int. Ed. 2021\, 60(9):4689 \n[4] McGregor et al. The assembly of the Mitochondrial Complex I Assembly complex uncovers a redox pathway coordination. Nat Commun. 2023\, 14(1):8248 \nContact : deborah.verger@grenoble-inp.fr
URL:https://sfp-alpes.fr/event/montserrat-soler-lopez-5macromolecular-x-ray-crystallography-imaging-and-scattering-group-esrf/
LOCATION:LMGP – salle des séminaires\, Grenoble INP -Phelma 3 parvis Louis Néel\, Grenoble\, 38054\, France
CATEGORIES:Séminaire
ORGANIZER;CN="LMGP":MAILTO:deborah.verger@grenoble-inp.fr
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260319T140000
DTEND;TZID=Europe/Paris:20260319T150000
DTSTAMP:20260404T115923
CREATED:20260305T151014Z
LAST-MODIFIED:20260305T151747Z
UID:10000094-1773928800-1773932400@sfp-alpes.fr
SUMMARY:Matthieu RAYNAL (Sorbonne Université\, CNRS\, Institut Parisien de Chimie Moléculaire (IPCM))
DESCRIPTION:Supramolecular helical catalysts : chirality induction and beyond\nRésumé : \nHelices are commonly formed by symmetry breaking operating during the bottom-up assembly of small molecules or monomers and their sense of rotation can be controlled by various methods. Important progress has been made in controlling the chiral and structural properties of supramolecular discrete assemblies and polymers.[1] Benzene-1\,3\,5- tricarboxamide[2] (BTA) are ubiquitous synthons for the preparation of hydrogen-bonded helices but it remains to be demonstrated how a given macroscopic property\, notably related to chirality (e.g. chiroptical\, magnetic\, catalytic)\, can be affected by tuning the structure of these supramolecular polymers or copolymers. We demonstrated that the supramolecular chirality of BTA assemblies can be transferred to intrinsically achiral metal centres (Rh\, Cu) located at their periphery.[3] How the selectivity of a catalytic reaction of reference can be affected by the nature of the monomers\, the presence of metal centres\, and the addition of achiral additives will be particularly discussed.[4] Not only a fine tuning of the chirality of the supramolecular assemblies but also a proper control of their dynamicity is key to address important challenges. We recently disclose the possibility to select one major (70%-79%) amongst four possible stereoisomers of an amino alcohol by applying the supramolecular helical catalyst in either concomitant (with no inversion of catalyst handedness) or sequential (with inversion of catalyst handedness) hydrosilylation and hydroamination reactions [5]. \nReferences : \n[1] Yashima E. et al. Chem. Rev.\, 2016\, 116\, 13752.\n[2] Cantekin S. et al. Chem. Soc. Rev.\, 2012\, 41\, 6125.\n[3] Desmarchelier A. et al. J. Am. Chem. Soc.\, 2016\, 138\, 4908.\n[4] (a) Li Y. et al. J. Am. Chem Soc.\, 2020\, 142\, 5676. (b) Martínez-Aguirre M. A. et al. Angew. Chem. Int. Ed.\, 2021\, 60\, 4183. (c) Hammoud A. et al. Chem. Eur. J.\, 2023\, e202300189. (d) Kong H. et al. ChemistryEurope\, 2023\, 1\, e202300027.\n[5] Chen\, R. et al. Nature Commun.\, 2024\, 15\, 4116 \n_ \nContact : adrien.quintard@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/matthieu-raynal-sorbonne-universite-cnrs-institut-parisien-de-chimie-moleculaire-ipcm/
LOCATION:DCM – Salle C209\, DCM - Bât Chimie Recherche 301 rue de la Chimie\, St Martin d'Hères\, 38400\, France
CATEGORIES:Séminaire
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260320T110000
DTEND;TZID=Europe/Paris:20260320T120000
DTSTAMP:20260404T115923
CREATED:20260227T100104Z
LAST-MODIFIED:20260313T171306Z
UID:10000079-1774004400-1774008000@sfp-alpes.fr
SUMMARY:Chrystel GENOUD (EPFL\, Lausane\, Suisse)
DESCRIPTION:Understanding tissue by volumeEM – some examples from an EM platform\nSéminaire dans le cadre de la Journée Microscopie Electronique \nRésumé : \nUnderstanding the complex architecture of cells and tissues requires imaging technologies that can bridge the gap between ultrastructural details and large-volume context in room temperature and cryo-EM. Volume electron microscopy (volume EM) addresses this need by enabling 3D imaging of biological samples at nanometer resolution over tens to hundreds of microns. In this presentation\, I will provide an overview of volume EM techniques available on our platform based on examples and how we combine it with correlative light and electron microscopy.I will also show how we are adressing the targeting of small structures in lare tissue in cryo-ET by using the serial lift-out method and cryo-CLEM. The example of targeting the Casparian strip in the root of Arabidopsis thaliana will be developed. \nContact : ibs.seminaires@ibs
URL:https://sfp-alpes.fr/event/chrystel-genoud-epfl-lausane-suisse/
LOCATION:IBS – Salle des séminaires\, IBS 71 avenue des Martyrs\, Grenoble\, 38042\, France
CATEGORIES:Séminaire
ORGANIZER;CN="IBS":MAILTO:ibs.seminaires@ibs
END:VEVENT
BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260323T110000
DTEND;TZID=Europe/Paris:20260323T120000
DTSTAMP:20260404T115923
CREATED:20260320T094540Z
LAST-MODIFIED:20260320T094546Z
UID:10000101-1774263600-1774267200@sfp-alpes.fr
SUMMARY:Chloé ROFFAY (IMP Vienna\, Austria)
DESCRIPTION:Uncovering the forces driving the fate and shape of the extraembryonic amnion during human gastrulation\nRésumé : \nExtraembryonic tissues provide key molecular signals and mechanical support to the growing embryo. For instance\, the extraembryonic amnion\, which forms a fluid-filled sac surrounding the embryo\, was recently shown to trigger germ layer specification during gastrulation\, by secreting BMP ligands. Despite the key roles of extraembryonic tissues in embryo development\, little is still known regarding their molecular and biophysical programs\, particularly in human. Using a 2D stem cell-based model of human gastrulation\, termed gastruloid discs\, we found that amnion cells undergo a sharp columnar-to-squamous transition concomitantly with fate specification. Via biophysical modelling\, direct force measurements\, pharmacological and genetic perturbations\, we showed that this morphogenetic transition is amnion-intrinsic and it is driven by active wetting\, i.e. a transition from tensile to adhesion-dominated cellular states. Molecularly\, active wetting is implemented via a rewiring of cytoskeleton composition\, from actomyosin to keratin-based cytoskeletal networks\, akin to a bistable toggle-switch in gene regulatory networks. Strikingly\, blocking shape changes at the colony edge results both in defective cellular states in the amnion and impaired gastruloid disc morphogenesis within the embryonic compartment. Together\, our findings establish that a cytoskeletal toggle switch couples fate specification to tissue architecture in the human amnion and suggest an unexpectedly active mechanical role for extraembryonic tissues in shaping the embryo proper. \nContact : thomas.boudou@univ-grenoble-alpes.fr
URL:https://sfp-alpes.fr/event/chloe-roffay-imp-vienna-austria/
LOCATION:LiPhy – Salle de conférence\, LiPhy 140 avenue de la Physique\, St Martin d'Hères\, 38402\, France
CATEGORIES:Séminaire
END:VEVENT
END:VCALENDAR