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X-WR-CALNAME:Institut Jacques Monod
X-ORIGINAL-URL:https://www.ijm.fr
X-WR-CALDESC:Évènements pour Institut Jacques Monod
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DTSTART;TZID=Europe/Paris:20260612T110000
DTEND;TZID=Europe/Paris:20260612T120000
DTSTAMP:20260612T185749
CREATED:20260602T094657Z
LAST-MODIFIED:20260602T094657Z
UID:33288-1781262000-1781265600@www.ijm.fr
SUMMARY:Séminaire de l'Institut Jacques Monod - Laurent Blanchoin & Manuel Théry
DESCRIPTION:Invité par l’équipe Romet-Lemonne/Jégou\, Manuel Théry (Directeur de Recherche CEA\, Cytomorpholab\, ESPCI/IPGG\, Paris) et Laurent Blanchoin (Directeur de Recherche CNRS\, Cytomorpholab\, IRIG/LPCV\, Grenoble) présenteront un séminaire de l’Institut Jacques Monod sur le thème : \nThe self-renewing cell: how actin networks are built\, sized\, and dismantled \nRésumé : \nThe actin cytoskeleton continuously assembles and disassembles its filaments\, a process of self-renewal essential for cell shape\, movement\, and response to the environment. Yet how the cell coordinates this renewal across multiple coexisting actin structures\, and what sets the rate at which individual networks turn over\, remains poorly understood. Using a minimal reconstituted system with either unlimited or limited monomer availability\, we show that when monomers are scarce\, competition between distinct actin architectures profoundly disrupts turnover: as competition increases\, the turnover rate of individual networks decreases. Actin turnover is therefore not an intrinsic property of individual networks but an emergent outcome dictated by the competitive balance between coexisting architectures. We then show that this principle operates in living cells: when cells increase their spreading area\, the expanding cytoskeleton monopolizes available monomers\, forcing a slowing of turnover at the whole-cell scale. Together\, these results establish competition between actin structures as a fundamental determinant of turnover\, revealing how the global cytoskeletal state collectively shapes the dynamic properties of each individual network
URL:https://www.ijm.fr/event/seminaire-de-linstitut-jacques-monod-laurent-blanchoin-manuel-thery/
LOCATION:Institut Jacques Monod Salle François Jacob\, 15 rue Hélène Brion\, Paris\, 75013\, France
ATTACH;FMTTYPE=image/jpeg:https://www.ijm.fr/wp-content/uploads/2026/06/Bandeau-web-seminar-Laurent-Blanchoin-Manuel-Thery-scaled.jpg
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BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260612T140000
DTEND;TZID=Europe/Paris:20260612T170000
DTSTAMP:20260612T185749
CREATED:20260522T145207Z
LAST-MODIFIED:20260522T145207Z
UID:33260-1781272800-1781283600@www.ijm.fr
SUMMARY:Soutenance HDR - Hugo Wioland
DESCRIPTION:Hugo Wioland (équipe Romet-Lemonne/Jégou) va défendre son Habilitation à Diriger des recherche : \nActin biochemical and mechanical diversity \nLe jury sera composé de : \n\nNicolas Joly\, Président\nLaurent Blanchoin\, Rapporteur\nPeter Bieling\, Rapporteur\nAurélie Bertin\, Examinatrice\nPatricia Bassereau\, Examinatrice
URL:https://www.ijm.fr/event/soutenance-hdr-hugo-wioland/
LOCATION:Institut Jacques Monod Salle François Jacob\, 15 rue Hélène Brion\, Paris\, 75013\, France
ATTACH;FMTTYPE=image/jpeg:https://www.ijm.fr/wp-content/uploads/2026/05/HDR-bandeau-Hugo-Wioland-scaled.jpg
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BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260617T093000
DTEND;TZID=Europe/Paris:20260617T110000
DTSTAMP:20260612T185749
CREATED:20260605T115913Z
LAST-MODIFIED:20260605T115913Z
UID:33346-1781688600-1781694000@www.ijm.fr
SUMMARY:Cytoskeleton club
DESCRIPTION:La prochaine réunion du cytoskeleton club aura lieu mercredi 17 juin. \n\nLucas PRADEAU-PHELUT (PhD student\, S. Etienne-Manneville’s group\, Institut Pasteur) présentera « Synemin–MARK2 interaction: a key regulator of cytoskeletal crosstalk during glioblastoma cell adhesion\, migration\, and invasion. »\nBhagyanath Suresh (Ph Student\, M. Thery’s group\, IPGG) présentera « From morphogenesis to space partitioning »
URL:https://www.ijm.fr/event/cytoskeleton-club-16/
LOCATION:Institut Jacques Monod Salle François Jacob\, 15 rue Hélène Brion\, Paris\, 75013\, France
ATTACH;FMTTYPE=image/jpeg:https://www.ijm.fr/wp-content/uploads/2026/06/20260617-bandeau-scaled.jpg
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DTSTART;TZID=Europe/Paris:20260623T140000
DTEND;TZID=Europe/Paris:20260623T170000
DTSTAMP:20260612T185749
CREATED:20260603T143401Z
LAST-MODIFIED:20260603T143556Z
UID:33313-1782223200-1782234000@www.ijm.fr
SUMMARY:Soutenance de thèse - Aurélie Masson
DESCRIPTION:Aurélie Masson (équipe Prioleau) va défendre sa thèse : \nCartographie des sites fragiles communs potentiels dans les précurseurs neuronaux et étude de leur impact sur le développement du cortex cérébral \nLe jury sera composé de : \nPatricia KANNOUCHE\, DR\, Université Paris-Saclay\, Rapportrice.\nPhilippe PASERO\, DR\, Université de Montpellier\, Rapporteur.\nSara BIZZOTTO\, CR\, Université Paris Cité\, Examinatrice.\nStéphane KOUNDRIOUKOFF\, PU\, Université d’Orléans\, Examinateur.\nJean-Charles CADORET\, PU\, Université Paris Cité\, Examinateur.\nMarie-Noëlle PRIOLEAU\, DR\, Université Paris Cité\, Directrice de thèse.
URL:https://www.ijm.fr/event/soutenance-de-these-aurelie-masson/
LOCATION:Amphithéâtre Alan Turing – Bâtiment Sophie Germain\, 8 place Aurélie Nemours\, Paris\, 75013\, France
ATTACH;FMTTYPE=image/jpeg:https://www.ijm.fr/wp-content/uploads/2026/06/These-bandeau-Aurelie-Masson.jpg
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BEGIN:VEVENT
DTSTART;TZID=Europe/Paris:20260626T114500
DTEND;TZID=Europe/Paris:20260626T130000
DTSTAMP:20260612T185749
CREATED:20260522T145834Z
LAST-MODIFIED:20260522T150044Z
UID:33267-1782474300-1782478800@www.ijm.fr
SUMMARY:Séminaire de l'Institut Jacques Monod - Christian Schlieker
DESCRIPTION:Invité par l’équipe Palancade\, Christian Schlieker (Department of Molecular Biophysics and Biochemistry\, Yale University\, USA) présentera un séminaire de l’Institut Jacques Monod sur le thème : \nBiomolecular Condensates at the Nuclear Envelope: From Mechanism to Therapeutic Modulation \nChristian started his scientific training as an undergraduate at the University of Bonn in Germany\, with a research stay at the University of New South Wales in Sydney\, Australia. He then earned his Ph.D. in the laboratory of Dr. Bernd Bukau at the Center for Molecular Biology (ZMBH) of Heidelberg University\, where he used biochemical and biophysical approaches to uncover how Clp/HSP100 AAA+ ATPases counteract proteotoxic stress. \nChristian continued his training as an EMBO postdoctoral fellow with Dr. Hidde Ploegh at Harvard Medical School and the Whitehead Institute/MIT\, where he explored the ubiquitin–proteasome system and discovered a novel role for a ubiquitin-like modifier in RNA biology. \nChristian joined the Department of Molecular Biophysics and Biochemistry at Yale University in 2009\, where he is currently Professor and Director of Undergraduate Studies\, with a secondary appointment in the Department of Cell Biology. He is a recipient of the NIH Director’s New Innovator Award and has served on the scientific advisory board of the Dystonia Medical Research Foundation and reviewed for the NIH\, the Department of Defense\, the German Excellence Initiative\, ANR and the European Research Council\, among others. At Yale\, he has chaired the Committee on Majors for Yale College and currently serves on the Advisory Board of the Yale Center for Molecular Discovery. Starting in July 2026\, he will chair the Department of Molecular Biophysics and Biochemistry. \nBrief synopsis \nWe explore how cells build and safeguard two the nuclear envelope and the endoplasmic reticulum. Our work focuses on how disruptions in membrane organization and phase separation drive the formation of aberrant condensates that are increasingly implicated in neurological disease. To tackle these questions\, we develop and apply new tools that allow us to probe and modulate these processes across scales\, from the dynamics of individual proteins and condensates to genome-wide functional screens. By integrating cell biology\, biochemistry\, and computational approaches with patient-derived and animal model systems\, we aim to uncover fundamental principles of cellular organization and translate these discoveries into novel therapeutic strategies for movement disorders and related conditions. \nWe recently developed a high-content platform and computational pipeline to screen modulators of nuclear condensates across chemical and genetic space. This effort identified novel players in nuclear condensates formation\, along with small molecules that modualte proteotoxic condensates. Application of the platform in a genome-wide CRISPR knockout screen revealed strong enrichment of candidate genes linked to primary microcephaly and related neurodevelopmental disorders\, pointing to condensate dysregulation as a shared molecular axis across disease. \nA complementary line of work asks how the nuclear pore complex itself contributes to protein quality control. Co-translational folding allows nascent proteins to begin folding as they are synthesized\, reducing the risk of aggregation and avoiding energy-intensive unfolding steps. We propose that karyopherins and flexible FG-nucleoporins not only safeguard the nuclear permeability barrier but also generate a supportive environment — a “folding phase” — that promotes correct folding of proteins entering the nucleus. This perspective offers new insight into how disruptions in nuclear transport and protein quality control may contribute to neurological disease. Together\, these efforts may inform biotechnological advances in protein stability and targeted therapeutics for diseases of disrupted folding. \nSelected publications \n\nProphet SM\, Rampello AJ\, Niescier RF\, Gentile JE\, Mallik S\, Koleske AJ\, Schlieker C: Atypical nuclear envelope condensates linked to neurological disorders reveal nucleoporin-directed chaperone activities. Nat Cell Biol 2022\, 24:1630–1641.\nPoch D\, Mukherjee C\, Mallik S\, Todorow V\, Kuiper EFE\, Dhingra N\, Surovtseva YV\, Schlieker C: Integrative Chemical Genetics Platform Identifies Condensate Modulators Linked to Neurological Disorders. bioRxiv 2025\, doi:10.1101/2025.06.07.658469.\nRampello AJ\, Laudermilch E\, Vishnoi N\, Prophet SM\, Shao L\, Zhao C\, Lusk CP\, Schlieker C: Torsin ATPase deficiency leads to defects in nuclear pore biogenesis and sequestration of MLF2. J Cell Biol 2020\, 219:e201910185.\nMallik S\, Poch D\, Burick S\, Schlieker C: Protein folding and quality control during nuclear transport. Curr Opin Cell Biol 2024\, 90:102407.
URL:https://www.ijm.fr/event/seminaire-de-linstitut-jacques-monod-christian-schlieker/
LOCATION:Institut Jacques Monod Salle François Jacob\, 15 rue Hélène Brion\, Paris\, 75013\, France
ATTACH;FMTTYPE=image/jpeg:https://www.ijm.fr/wp-content/uploads/2026/05/Bandeau-web-seminar-Christian-Schlieker-scaled.jpg
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