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Guest speakersCIC bioGUNE, Bizkaia, Spain
Rosa Barrio obtained her BSc in Biology from the Autonomous University of Madrid (UAM) and her PhD in Sciences from the same University. She joined the laboratory of Prof. FC Kafatos at Harvard University (Cambridge, USA), IMBB (Greece), and EMBL (Germany) to study SALL transcription factors, which mutations contribute to hereditary human diseases such as Townes-Brocks Syndrome (TBS) and Okihiro Syndrome (OS). In 2004, Dr. Barrio joined CIC bioGUNE as a Group Leader, leading the Ubiquitin-likes And Development Lab. Her laboratory is focused on understanding protein homeostasis regulation, especially focusing on the Ubiquitin-like (UbL) family. The group develops technologies like BioUbL, SUMO-ID, and BioE3 to identify UbL modified proteins, their interactors, and E3 ligase targets. The interests of the laboratory include the study of how disruptions in protein homeostasis contribute to rare diseases like TBS and other.
Ludwig Maximilians University, München, Germany
After hypothesis-driven research on chaperones and aggregation-prone proteins in the group of Ulrich Hartl at the Max-Planck-Institute of Biochemistry as PhD student and explorative screening on autophagy in the Harper lab at Harvard Medical School in Boston as post-doc, Christian sought to combine these two approaches when he started his own group in 2010 in the Institute of Biochemistry II (IBC2) at the Goethe University in Frankfurt. After setting up proteomics and high-content imaging platforms at the IBC2, he focused on exploring the cellular components that drive or regulate autophagy and that are subject to autophagosomal degradation. Within this framework, the ubiquitin system gained particular attention. In 2016, Christian returned to Munich and neurodegeneration by joining the Munich Cluster of Systems Neurology (SyNergy) at the Ludwig-Maximilians-University (LMU) as professor for Systems Biology of Neurodegenerative Diseases.
Institute of Pharmacology and Structural Biology (IPBS), Toulouse, France.
Marie-Pierre Bousquet was trained as a biochemical engineer at the National Institute of Applied Sciences (INSA, France). After spending two years working as an engineer at Zeneca bio-products in the UK, she joined the academic research for a PhD. In her PhD and postdoc trainings, she has designed, produced, purified, and used enzymes for biocatalysis in non conventional media to synthetize sugar derivatives for cosmetic and food applications. In 2002, she joined the ProteoToul Research group at the Pharmacology and Structural Biology Institute (CNRS UMR 5089, France) as an associate-professor and started to develop MS-based tools to explore the structure-function relationship of the main proteolytic degradation machinery of the cell – the proteasome. The purpose of her research project is to carry out a comprehensive study of the proteasome complexes structural, dynamics and functional diversity in eukaryotic cells and in different physiological and pathological settings. Given the heterogeneity of proteasome complexes, such an undertaking requires analytical methods capable of coping with such diversity. She mainly uses proteomic and structural strategies based on mass spectrometry, including Affinity-Purification coupled to Mass Spectrometry (AP-MS), targeted proteomics, and structural mass spectrometry. In particular, her group has developed integrated strategies, using in-vivo cross-linking, affinity purification and quantitative bottom-up and top-down proteomics, to measure the quantities and the dynamics of several proteasome subtypes in patient samples. The ultime goal would be to better understand proteasome regulation and provide useful information for the development of therapies targeting particular proteasome subtypes that would prevent inhibition of signaling pathways and undesirable side effects. Her bibliography and the reputation she has acquired in the proteasome field has enabled her to set up numerous collaborations, and she was granted with successive competitive fundings from French ministerial or associative programs, which today enables her to carry out her research projects independently. Marie-Pierre Bousquet was appointed a full professorship in Biochemistry at the Sciences University in Toulouse in 2022 and manages an international Master Program on Biomolecular Sciences, Mechanisms and Therapeutic Targets in Toulouse university.
Institute of Chemical Biology, National Hellenic Research Foundation, Athens, Greece She graduated from the Department of Biology of the National and Kapodistrian University of Athens (NKUA) in Greece. She obtained her PhD in Biochemistry and Molecular Biology from NKUA while she was a visiting fellow at the Universities Paris 7 in France and Bristol in UK. She conducted her post-doctoral studies at the National Hellenic Research Foundation (NHRF) in Athens. During her post-doctoral studies, she was trained in the use of Caenorhabditis elegans at the Foundation of Research and Technology-Hellas, Institute of Molecular Biology and Biotechnology (FORTH-IMBB) in Greece. She became Research Assistant Professor at NHRF in 2009, Research Associate Professor in 2013 and Research Director in 2022. She is a national and international patent holder that resulted in the development of novel anti-ageing products that act as proteasome activators (EP2246037A2, two relative product series in the national/ international market). She also holds a PCT (EP3761950A1) on bioinspired proteasome activators with anti-ageing activity. She focuses on the genetic and environmental factors that govern ageing, longevity and age-related diseases with emphasis on proteasome regulation. She is seeking for compounds that may act as proteasome activators and thus may serve as anti-ageing agents. She is equally interested in identifying compounds than can decelerate protein aggregation and thus the progression of proteinopathies with emphasis on Alzheimer’s disease using C. elegans, human cells of neuronal origin and murine primary neurons. Based on the latter activity, she holds a national patent. She is an elected meeting officer for the Society of Free Radical Research-Europe (SFRR-E), responsible for the organization of the SFRR-E Summer Schools that are often co-organized with FEBS and IUBMB. She serves as an editor in Free Radical Biology and Medicine (Elsevier) since November 2023.
University of Liverpool, United Kingdom. Michael Clague obtained a PhD in biological chemistry from University of Essex. For post-doctoral work he moved to NIH, Bethesda USA to study the biophysics of membrane fusion. An EMBO long term fellowship allowed him to move to EMBL, Heidelberg, to study cell biology (membrane trafficking) for the first time. He was then appointed to a faculty position at Liverpool, where he is currently Professor of Molecular and Cellular Physiology. Early work at Liverpool focused on the role of phosphoinositide metabolism along the endocytic pathway. He was drawn into the ubiquitin field through studies of the MET receptor trafficking itinerary and has since developed a specific interest in the family of deubiquitylases. Working together with Sylvie Urbé, he investigates these enzymes in pathways germane to cancer and neurodegeneration. Contributions span foundational biology to development and characterisation of tool compound inhibitors. Work on USP30 has helped establish it as an actionable target for Parkinson’s Disease and led to a broader interest in mitophagy and pexophagy pathways.
Harvard Medical School, Boston, United States of America Dr. Finley graduated from Harvard College in 1980 and received his PhD from MIT in 1984, having worked with Alex Varshavsky and in collaboration with Aaron Ciechanover. His thesis work showed that the ubiquitin pathway is essential in mammals and is the major pathway for selective protein degradation. This work also linked ubiquitination to cell cycle control and the stress response. He continued at MIT for his post-doctoral work and developed yeast as a model system for the study of ubiquitination. He was appointed in 1988 to the faculty of Harvard Medical School, where he remains today, studying proteasome biochemistry, mechanisms of proteostasis, and remodeling of the proteome by the UPS in differentiating cells.
Danish Cancer Institute, University of Copenhagen, Danemark Lisa Frankel has a long-standing interest in molecular and cellular cancer biology, with the aim of understanding how basic errors in the control of cellular homeostasis pathways can lead to the development of disease. Born and raised in Toronto, Canada, Lisa performed her studies at the University of Copenhagen and at McGill University, Montreal. After her PhD and postdoc at the BRIC institute, University of Copenhagen, Lisa was awarded with a starting grant from the Lundbeck Foundation, allowing the establishment of her independent group at the Danish Cancer Institute (DCI) in 2019. The current work of the group focuses on the interplay between RNA biology, ubiquitin signaling and autophagy and the impact of this in disease including cancer and neurodegeneration.
Technion-Institute of Technology, Haifa, Israel Michael Glickman is dean of the faculty of Biology (Technion - Israel Institute of Technology). Michael Glickman's group has a long-standing interest in understanding how ubiquitin and ubiquitin-like signals are recognized at the proteasome. On proteasome structure and function, we have obtained structural snapshots of 26S Proteasome Reveal Tetraubiquitin-Induced Conformations and found that 26S undergoes dramatic conformational changes upon binding to tetraubiquitin, yet displays low ability to process these chains, thereby explaining why tetraubiquitin serves as an efficient targeting signal for proteasome. In parallel, we are investigating signature activities of 20S proteasome including its ability to degrade globular domains and its biological role under hypoxia. Since most proteolytic processes are ubiquitin-dependent, we posited that interference with ubiquitin signaling has the potential to contribute to onset of Alzheimer’s disease (AD). Therefore, we have adapted a system to grow pluripotent stem cells, differentiate them into neuronal progenitors and into neurons and we are now skilled in growing 3-D neuronal cultures and measuring amyloid plaques and neurofibrillary tangles and are studying the links between ubiquitin-dependent turnover in neurons to progression of Alzheimer hallmarks. Since mis-regulated mitochondria have also been linked to AD, and Ubiquitination is an efficient mechanism to enforce rapid changes of protein levels in response to stimuli and even direct entire mitochondria to autophagy (mitophagy), we have directed a large part of our efforts to evaluate how ubiquitination of mitochondrial proteins adapts mitochondria morphology and physiology. We have exposed a number of links between the ubiquitin-proteasome system and the mitochondria. Components of the proteasome associate with the mitochondria. Mutants in proteasome subunits display unique mitochondrial phenotypes.
UiT The Artic University of Norway, Tromso, Norway
Terje Johansen has all his academic education from UiT The Arctic University of Norway and obtained his Dr. scient. degree (equivalent to PhD) in 1988. From 1991 onwards Terje has been Professor and PI leading his own research group at the Department of Medical Biology, Faculty of Health Sciences at UiT. His research topics has spanned from transcriptional regulation, cell signaling to selective autophagy. In 2005 Terje and his group published their discovery of the first selective autophagy receptor p62/SQSTM1 and how it could recognize ubiquitinated cargo for degradation by autophagy. This was followed up by showing that the ATG8 family of ubiquitin-like proteins acted to connect p62, by binding to its LC3-interacting region (LIR) motif, with the forming autophagosome. In essence, this deciphered the major steps in selective autophagy from cargo recognition to inclusion in autophagosomes. Together with the groups of Ivan Dikic and Masaki Komatsu, Terje and his group also discovered NBR1 as a selective autophagy receptor and has gone on to show that NBR1 is the archetypal autophagy receptor also found in plants that appeared first in the evolution of eukaryotes. A major focus for studies in Terje’s lab for the last 20 years has been on various forms of selective autophagy involving autophagy receptors and ATG8 family proteins including the selective autophagic degradation of protein aggregates (aggrephagy), mitochondria (mitophagy), peroxisomes (pexophagy), endoplasmic reticulum (ER-phagy) and Golgi apparatus (Golgiphagy). Another related focus has been on the roles of ATG8 family proteins as membrane scaffolds for other proteins, like FYCO1 involved in transport of autophagosomes and late endosomes, and components of the basal autophagy apparatus like ULK1/2, ATG13, ATG14L, Beclin1 and ATG4 proteins. A recent interest is in the nuclear roles of ATG8 family proteins.
Harvard Medical School, Boston, United States of America John Hanna is an Associate Professor at Harvard Medical School. He obtained his undergraduate degree at Stanford in 2001 and his PhD (2006) and MD (2009) degrees at Harvard. During his thesis work in the lab of Daniel Finley, John focused on regulation of the proteasome by the associated deubiquitinating enzyme Ubp6/Usp14. Since starting his own lab in 2013, John has focused on three aspects of proteasome biology. The first is the complicated chaperone-mediated pathway by which the proteasome’s core particle is assembled. This area of study has major implications for an emerging family of human diseases known as proteasomopathies. The second is the regulation of proteasome activity by endogenous inhibitors, including PI31. This work has in turn led to efforts to develop novel proteasome inhibitors using a rational, structure-guided approach based on PI31’s evolutionarily optimized mechanism. Third, John’s lab has been interested in the cellular stress response mediated by Rpn4/Nrf1 that senses and controls proteasome abundance in response to proteotoxicity. John is also a practicing physician and lives in Boston with his wife and daughter.
Max Planck Institute for Multidisciplinary Sciences, Göttingen, Germany
2004-2008 Ph.D. Biochemistry with Iain D. Campbell and Martin Nobel at the University of Oxford, UK 2009 -2013 Postdoctoral fellowship with John Kuriyan at the University of California, Berkeley, CA/USA 2014-2020 Emmy Noether Group Leader at the University of Wuerzburg, Germany since 2021 Independent Group Leader at the Max Planck Institute for Multidisciplinary Sciences, Goettingen, Germany Sonja Lorenz’ lab explores fundamental principles of specificity in the ubiquitin system with a particular focus on HECT-type ubiquitin ligases. The lab combines high-resolution structural tools, including cryo-EM and crystallography, with biochemical and cell biological approaches. Sonja was named an EMBO Young Investigator in 2018.
Research Center Borstel/Leibniz Lung Center, Borstel, Germany Silke Meiners was trained as a biochemist and molecular biologist at the universities of Bonn (Germany), Norwich (GB), and Berlin, where she got her PhD degree. She worked as a Postdoc and assistant professor at the Charité in Berlin where she habilitated on the application of proteasome inhibitors in cardiovascular disease in 2008. In 2010, Silke Meiners joined the Comprehensive Pneumology Center at the Helmholtz Center Munich (Germany) as a research group leader and started to work on the proteasome in lung health and disease. Since September 2021, Silke Meiners is heading a research group dedicated to immunoproteasome research at the Research Center Borstel/Leibniz Lung Center. She also holds a Leibniz Chair for Immunoproteasome Research at the University of Kiel (Germany). Silke Meiners is an active fellow of the European Respiratory Society where she is the current ERS Research Seminar and Conference Director organizing the annual Lung Science Conferences and Research Seminars. She is also co-chair of the DZL-Academy, that supports early career scientists within the German Center for Lung Research (DZL).
University of Tokyo, Tokyo, Japan Shigeo Murata is a professor at the Graduate School of Pharmaceutical Sciences at the University of Tokyo. He earned his M.D. in 1994 and, after two years of residency training in internal medicine, obtained his Ph.D. in 2000 from the University of Tokyo. He later joined the laboratory of Keiji Tanaka at the Tokyo Metropolitan Institute of Medical Science as a postdoctoral researcher. In 2007, he was appointed as a professor at the University of Tokyo. Shigeo’s research is dedicated to understanding the regulation of the proteasome. His significant contributions include studies on the chaperone-dependent ubiquitin ligase CHIP, the proteasome activator PA28, and the assembly mechanism of the proteasome. He has also been credited with the discovery of the thymus-specific proteasome, which is crucial for thymic positive selection, the identification of DDI2 as the Nrf1 processing enzyme, and the discovery of nuclear proteasome condensates that uniquely form in senescent cells.
University of California, Berkeley, United States of America Michael Rape is a pioneer in uncovering fundamental mechanisms of cellular regulation by ubiquitylation. Michael’s work revealed new ubiquitin chain types, essential ubiquitylation enzymes and substrates, as well as mechanisms of ubiquitylation that are essential for human development and disease. His work led to the first prospective development of a molecular glues targeting E3 ligases, thus helping to opening up the ubiquitin system for drug discovery. Michael received his PhD at the Max-Planck Institute of Biochemistry, where he discovered the function of the ubiquitin-dependent chaperone, the segregase CDC48/p97. His work was recognized with the Otto-Hahn Medal. Michael then joined Marc Kirschner’s lab at Harvard Medical School, where he uncovered principles of ordered protein degradation during cell division and revealed pathways underlying cancer cell resistance to the chemotherapeutic paclitaxel. In late 2006, Michael joined the Department of Molecular and Cell Biology at the University of California at Berkeley, where he is currently the Dr. K. Peter Hirth Chair of Cancer Biology and a Professor of Cell and Developmental Biology. Michael is also an Investigator of the Howard Hughes Medical Institute. His work has been recognized with a Vilcek Prize for Creative Promise, a National Blavatnik Award, and an NIH Director’s New Innovator Award.
Francis Crick Institute, London, United Kingdom
Katrin Rittinger is a senior group leader at the Francis Crick Institute in London. She did a PhD at the Max Planck Institute for Medical Research in Heidelberg, followed by a short postdoc at the MPI for Molecular Physiology in Dortmund, Germany. She then obtained EMBO Long-term and Marie Curie Fellowships to join the MRC-NIMR in London for a second postdoc, working on the structural characterisation of 14-3-3/ligand complexes and the regulation of Rho family GTPases. In 2000 she established her own research group studying protein assemblies that regulate signalling processes using biochemical and structural approaches. Her current work is focussed on the role of ubiquitination in the regulation of immune and inflammatory signalling pathways, with an emphasis on the function and mechanism of E3 ubiquitin ligases.
Head of the Department of Biomedical Sciences at the University of Padova, Italy. Marco Sandri is Full Professor of Pathology and Head of the Department of Biomedical Sciences at University of Padova. He received his M.D. degree and the residency in Clinical Pathology at the University of Padova. He carried out postdoctoral work in Alfred L Goldberg lab at Harvard Medical School, Boston. In 2005 and 2010 he was awarded by the prestigious Dulbecco Telethon career award prize and established his lab at Venetian Institute of Molecular Medicine in Padova. Marco Sandri has also an honorary position as Adjunct Professor at McGill University, Montreal, Canada from 2011. He got the prestigious ERC consolidator grant, he has been panel member of ERC consolidator program and is now a reviewer for the European Commission (ERC). In 2021, 2022, 2023 he got the award “Highly Cited Researcher”, which recognizes the true pioneers in their fields over the last decade, demonstrated by the production of multiple highly-cited papers that rank in the top 1% by citations for field and year in the Web of Science™. He is particularly interested in understanding the signaling pathways that control muscle mass with a focus on the role of the ubiquitin-proteasome and autophagy-lysosome systems. He was the first to show a transcriptional-dependent regulation of autophagy and protein breakdown. His research has provided insights into mechanisms of regulation of these proteolytic systems and to metabolic adaptations to physical activity. His work has been obtained more than 39.000 citations (Scopus) and he has an h-index of 83. For his contribution to the regulation of protein breakdown, Marco Sandri was invited to give lectures in outstanding research centers, among them the Harvard Medical School in Boston, the Imperial College of London, the Institut Pasteur in Paris, the Oxford University, the Medical Research Council in Cambridge, the McGill University in Montreal, the University of Pennsylvania of Philadelphia, and many others.
The Norwegian Radium Hospital, Montebello, N-0379 Oslo, Norway Professor Anne Simonsen leads the Autophagy research group at the Inst for Cancer Research, Oslo University Hospital, and is the co-director of the Centre of Excellence CanCell (Centre for Cancer Cell Reprogramming) at the University of Oslo, Norway. She received her PhD in 1996 and during her postdoc, she identified the FYVE domain as a specific PtdIns(3)P binding domain and EEA1 as a PtdIns(3)P and RAB5 effector protein important for endosome fusion. She started her laboratory at the University of Oslo in 2009 where she became a full professor in 2011. The main objective of the Simonsen laboratory is to unravel the molecular mechanisms involved in selective types of autophagy and their role in normal health and disease. Specific focus areas include characterization of the role of hypoxia-induced mitophagy in cancer development and protein aggregate clearance in neurodegenerative disease. Her lab also has a continued interest in ALFY and other BEACH-domain containing proteins. They have used both mammalian cell lines, various in vitro approaches and zebrafish for their discoveries. She has authored more than 120 papers and has an H-index of 63. She is a member of the Norwegian Academy of Sciences and elected member of EMBO.
Department of Cell and Chemical Biology of the Leiden University Medical Center, Leiden, The Netherlands Alfred Vertegaal received his Ph.D. from the Leiden University in 2001. Subsequently, he joined the laboratory of Prof. Angus Lamond at the Wellcome Trust Biocentre in Dundee, U.K., where he initiated a project to study signal transduction by Small Ubiquitin-like Modifiers (SUMOs) using a proteomic approach. An independent research line on SUMO signaling was started in 2004 in the Department of Molecular Cell Biology at the Leiden University Medical Center.
McGill University, Montreal, Canada Simon Wing, MD, FRCPC is the Leader of the Metabolic Disorders and Complications Program at the Research Institute of the McGill University Health Centre. He is Professor of Medicine at McGill University and staff endocrinologist at the McGill University Health Centre. His research interests are on the roles of ubiquitination in spermatogenesis and muscle wasting. He will present recent findings on the roles and targeting of a deubiquitinating enzyme in metabolic disorders. |
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