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3. A white paper from the FEBS Education and Training Conference: challenges, opportunities, and action plans for transforming molecular life sciences education.

Author

Villo, Ly, Sincic, Nino, Mello, Luciane V., Costa, Manuel Joao, Picard, Didier, Malatesta, Francesco, Dumic, Jerka, and Sagin, Ferhan G.

Subjects
EDUCATION conferences, LIFE science education, TECHNOLOGICAL innovations, SCIENCE conferences, DIGITAL technology
Abstract

The inaugural FEBS Education and Training Conference (ETC) was held in Türkiye, in 2024. This first‐ever Molecular Life Sciences Education Conference in Europe was organized by the FEBS Education and Training Committee and it was a groundbreaking event that brought together educators and scientists to explore how to enhance education and training in molecular life sciences. The conference explored a wide range of critical themes, for example—digital revolution, active learning and student engagement, multidisciplinary teaching and learning, transitions and inclusivity in education, students' self‐assessment, and self‐regulated learning. The discussions and presentations underscored the pressing need for transformation in how academics and researchers approach teaching and learning. Such shift is driven by rapid technological advancements, societal shifts, and the evolving demands of the scientific landscape. This document synthesizes key insights, discussions, and recommendations from the conference and proposes actionable strategies for all stakeholders in the field—institutions, educators and students—to address current challenges in education and training in molecular life sciences. [ABSTRACT FROM AUTHOR]

Published
2025
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8. Dynamic Imaging of LDH Inhibition in Tumors Reveals Rapid In Vivo Metabolic Rewiring and Vulnerability to Combination Therapy

Author

Oshima, Nobu, Ishida, Ryo, Kishimoto, Shun, Beebe, Kristin, Brender, Jeffrey R., Yamamoto, Kazutoshi, Urban, Daniel, Rai, Ganesha, Johnson, Michelle S., Benavides, Gloria, Squadrito, Giuseppe L., Crooks, Dan, Jackson, Joseph, Joshi, Abhinav, Mott, Bryan T., Shrimp, Jonathan H., Moses, Michael A., Lee, Min-Jung, Yuno, Akira, Lee, Tobie D., Hu, Xin, Anderson, Tamara, Kusewitt, Donna, Hathaway, Helen H., Jadhav, Ajit, Picard, Didier, Trepel, Jane B., Mitchell, James B., Stott, Gordon M., Moore, William, Simeonov, Anton, Sklar, Larry A., Norenberg, Jeffrey P., Linehan, W. Marston, Maloney, David J., Dang, Chi V., Waterson, Alex G., Hall, Matthew, Darley-Usmar, Victor M., Krishna, Murali C., and Neckers, Leonard M.

Published
2020
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17. Proteomic Analyses of the G Protein-Coupled Estrogen Receptor GPER1 Reveal Constitutive Links to Endoplasmic Reticulum, Glycosylation, Trafficking, and Calcium Signaling.

Author

Ahmadian Elmi, Maryam, Motamed, Nasrin, and Picard, Didier

Subjects
ESTROGEN receptors, G protein coupled receptors, ENDOPLASMIC reticulum, PROTEOMICS, CALCIUM, GLYCOSYLATION, IMMUNOPRECIPITATION
Abstract

The G protein-coupled estrogen receptor 1 (GPER1) has been proposed to mediate rapid responses to the steroid hormone estrogen. However, despite a strong interest in its potential role in cancer, whether it is indeed activated by estrogen and how this works remain controversial. To provide new tools to address these questions, we set out to determine the interactome of exogenously expressed GPER1. The combination of two orthogonal methods, namely APEX2-mediated proximity labeling and immunoprecipitation followed by mass spectrometry, gave us high-confidence results for 73 novel potential GPER1 interactors. We found that this GPER1 interactome is not affected by estrogen, a result that mirrors the constitutive activity of GPER1 in a functional assay with a Rac1 sensor. We specifically validated several hits highlighted by a gene ontology analysis. We demonstrate that CLPTM1 interacts with GPER1 and that PRKCSH and GANAB, the regulatory and catalytic subunits of α-glucosidase II, respectively, associate with CLPTM1 and potentially indirectly with GPER1. An imbalance in CLPTM1 levels induces nuclear association of GPER1, as does the overexpression of PRKCSH. Moreover, we show that the Ca2+ sensor STIM1 interacts with GPER1 and that upon STIM1 overexpression and depletion of Ca2+ stores, GPER1 becomes more nuclear. Thus, these new GPER1 interactors establish interesting connections with membrane protein maturation, trafficking, and calcium signaling. [ABSTRACT FROM AUTHOR]

Published
2023
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19. Molecular chaperone TRAP1 regulates a metabolic switch between mitochondrial respiration and aerobic glycolysis

Author

Yoshida, Soichiro, Tsutsumi, Shinji, Muhlebach, Guillaume, Sourbier, Carole, Lee, Min-Jung, Lee, Sunmin, Vartholomaiou, Evangelia, Tatokoro, Manabu, Beebe, Kristin, Miyajima, Naoto, Mohney, Robert P., Chen, Yang, Hasumi, Hisashi, Xu, Wanping, Fukushima, Hiroshi, Nakamura, Ken, Koga, Fumitaka, Kihara, Kazunori, Trepel, Jane, Picard, Didier, and Neckers, Leonard

Published
2013

20. Metformin reverses TRAP1 mutation-associated alterations in mitochondrial function in Parkinsonʼs disease

Author

Fitzgerald, Julia C., Zimprich, Alexander, Carvajal Berrio, Daniel A., Schindler, Kevin M., Maurer, Brigitte, Schulte, Claudia, Bus, Christine, Hauser, Anne-Kathrin, Kübler, Manuela, Lewin, Rahel, Bobbili, Dheeraj Reddy, Schwarz, Lisa M., Vartholomaiou, Evangelia, Brockmann, Kathrin, Wüst, Richard, Madlung, Johannes, Nordheim, Alfred, Riess, Olaf, Martins, Miguel L., Glaab, Enrico, May, Patrick, Schenke-Layland, Katja, Picard, Didier, Sharma, Manu, Gasser, Thomas, and Krüger, Rejko

Published
2017
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33. H90-10 single-chain antibody recognizes Hsp90beta by immunoprecipitation and Western blotting

Author

Abboud, Ernest, Bernasconi, Lilia, and Picard, Didier

Subjects
biology, Chemistry, Immunoprecipitation, Immunoblotting, Hsp90, Endogeny, General Medicine, Single chain, Molecular biology, law.invention, Blot, law, ddc:570, Molecular chaperone, biology.protein, Recombinant DNA, Antibody, Beta (finance)
Abstract

The recombinant antibody H90-10 detects the endogenous human heat-shock protein 90 beta (Hsp90β) by immunoprecipitation (IP) and Western blotting.

Published
2021
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34. Cytosolic Hsp90 Isoform-Specific Functions and Clinical Significance.

Author

Maiti, Samarpan and Picard, Didier

Subjects
*HEAT shock proteins, *MOLECULAR chaperones, *PHYSIOLOGICAL stress
Abstract

The heat shock protein 90 (Hsp90) is a molecular chaperone and a key regulator of proteostasis under both physiological and stress conditions. In mammals, there are two cytosolic Hsp90 isoforms: Hsp90α and Hsp90β. These two isoforms are 85% identical and encoded by two different genes. Hsp90β is constitutively expressed and essential for early mouse development, while Hsp90α is stress-inducible and not necessary for survivability. These two isoforms are known to have largely overlapping functions and to interact with a large fraction of the proteome. To what extent there are isoform-specific functions at the protein level has only relatively recently begun to emerge. There are studies indicating that one isoform is more involved in the functionality of a specific tissue or cell type. Moreover, in many diseases, functionally altered cells appear to be more dependent on one particular isoform. This leaves space for designing therapeutic strategies in an isoform-specific way, which may overcome the unfavorable outcome of pan-Hsp90 inhibition encountered in previous clinical trials. For this to succeed, isoform-specific functions must be understood in more detail. In this review, we summarize the available information on isoform-specific functions of mammalian Hsp90 and connect it to possible clinical applications. [ABSTRACT FROM AUTHOR]

Published
2022
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39. Réduire les pertes d'azote dans l'élevage

Author

Picard Didier

Subjects
Agriculture (General), S1-972, Plant culture, SB1-1110
Abstract

Le livre « Réduire les pertes d’azote dans l’élevage » s’attache à identifier les moyens de lutter efficacement contre les risques de pollution de l’environnement par les composés azotés réactifs dus à cette production. Les formes d’azote réactif sont décrites, leurs sources identifiées, leurs flux mesurés. Les moyens de réduire ces flux et les politiques à conduire pour y parvenir sont analysés.

Published
2016
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42. The Mitochondrial HSP90 Paralog TRAP1: Structural Dynamics, Interactome, Role in Metabolic Regulation, and Inhibitors.

Author

Joshi, Abhinav, Ito, Takeshi, Picard, Didier, and Neckers, Len

Subjects
METABOLIC regulation, HEAT shock proteins, STRUCTURAL dynamics, MITOCHONDRIA, MOLECULAR chaperones, GLYCOLYSIS, HOMEOSTASIS, CYTOPROTECTION
Abstract

The HSP90 paralog TRAP1 was discovered more than 20 years ago; yet, a detailed understanding of the function of this mitochondrial molecular chaperone remains elusive. The dispensable nature of TRAP1 in vitro and in vivo further complicates an understanding of its role in mitochondrial biology. TRAP1 is more homologous to the bacterial HSP90, HtpG, than to eukaryotic HSP90. Lacking co-chaperones, the unique structural features of TRAP1 likely regulate its temperature-sensitive ATPase activity and shed light on the alternative mechanisms driving the chaperone's nucleotide-dependent cycle in a defined environment whose physiological temperature approaches 50 °C. TRAP1 appears to be an important bioregulator of mitochondrial respiration, mediating the balance between oxidative phosphorylation and glycolysis, while at the same time promoting mitochondrial homeostasis and displaying cytoprotective activity. Inactivation/loss of TRAP1 has been observed in several neurodegenerative diseases while TRAP1 expression is reported to be elevated in multiple cancers and, as with HSP90, evidence of addiction to TRAP1 has been observed. In this review, we summarize what is currently known about this unique HSP90 paralog and why a better understanding of TRAP1 structure, function, and regulation is likely to enhance our understanding of the mechanistic basis of mitochondrial homeostasis. [ABSTRACT FROM AUTHOR]

Published
2022
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