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22 results on '"Nuebel, Esther"'

1. UCP2 regulates energy metabolism and differentiation potential of human pluripotent stem cells

Author

Zhang, Jin, Khvorostov, Ivan, Hong, Jason S, Oktay, Yavuz, Vergnes, Laurent, Nuebel, Esther, Wahjudi, Paulin N, Setoguchi, Kiyoko, Wang, Geng, Do, Anna, Jung, Hea-Jin, McCaffery, J Michael, Kurland, Irwin J, Reue, Karen, Lee, Wai-Nang P, Koehler, Carla M, and Teitell, Michael A

Subjects
Biological Sciences, Biomedical and Clinical Sciences, Information and Computing Sciences, Medical and Health Sciences, Developmental Biology, Biological sciences, Biomedical and clinical sciences
Abstract

[Image: see text]

Published
2016

8. Protective mitochondrial fission induced by stress-responsive protein GJA1-20k

Author

Shimura, Daisuke, Nuebel, Esther, Baum, Rachel, Valdez, Steven E., Xiao, Shaohua, Warren, Junco S., Palatinus, Joseph A., Hong, TingTing, Rutter, Jared, Shaw, Robin M., Shimura, Daisuke, Nuebel, Esther, Baum, Rachel, Valdez, Steven E., Xiao, Shaohua, Warren, Junco S., Palatinus, Joseph A., Hong, TingTing, Rutter, Jared, and Shaw, Robin M.

Abstract

The Connexin43 gap junction gene GJA1 has one coding exon, but its mRNA undergoes internal translation to generate N-terminal truncated isoforms of Connexin43 with the predominant isoform being only 20 kDa in size (GJA1-20k). Endogenous GJA1-20k protein is not membrane bound and has been found to increase in response to ischemic stress, localize to mitochondria, and mimic ischemic preconditioning protection in the heart. However, it is not known how GJA1-20k benefits mitochondria to provide this protection. Here, using human cells and mice, we identify that GJA1-20k polymerizes actin around mitochondria which induces focal constriction sites. Mitochondrial fission events occur within about 45 s of GJA1-20k recruitment of actin. Interestingly, GJA1-20k mediated fission is independent of canonical Dynamin-Related Protein 1 (DRP1). We find that GJA1-20k-induced smaller mitochondria have decreased reactive oxygen species (ROS) generation and, in hearts, provide potent protection against ischemia-reperfusion injury. The results indicate that stress responsive internally translated GJA1-20k stabilizes polymerized actin filaments to stimulate non-canonical mitochondrial fission which limits ischemic-reperfusion induced myocardial infarction.

Published
2021

11. Msp1/ATAD1 restores mitochondrial function in Zellweger Spectrum Disease

Author

Nuebel, Esther, primary, Morgan, Jeffrey T, additional, Fogarty, Sarah, additional, Winter, Jacob M, additional, Lettlova, Sandra, additional, Berg, Jordan A, additional, Chen, Yu-Chan, additional, Kidwell, Chelsea U, additional, Maschek, J. Alan, additional, Clowers, Katie J, additional, Argyriou, Catherine, additional, Chen, Lingxiao, additional, Wittig, Ilka, additional, Cox, James E, additional, Roh-Johnson, Minna, additional, Braverman, Nancy, additional, Steinberg, Steven J, additional, Gygi, Steven P, additional, and Rutter, Jared, additional

Published
2020
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16. UCP 2 regulates energy metabolism and differentiation potential of human pluripotent stem cells

Author

Zhang, Jin, primary, Khvorostov, Ivan, additional, Hong, Jason S, additional, Oktay, Yavuz, additional, Vergnes, Laurent, additional, Nuebel, Esther, additional, Wahjudi, Paulin N, additional, Setoguchi, Kiyoko, additional, Wang, Geng, additional, Do, Anna, additional, Jung, Hea‐Jin, additional, McCaffery, J Michael, additional, Kurland, Irwin J, additional, Reue, Karen, additional, Lee, Wai‐Nang P, additional, Koehler, Carla M, additional, and Teitell, Michael A, additional

Published
2016
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18. Interaction between AIF and CHCHD4 Regulates Respiratory Chain Biogenesis

Author

Hangen, Emilie, primary, Féraud, Olivier, additional, Lachkar, Sylvie, additional, Mou, Haiwei, additional, Doti, Nunzianna, additional, Fimia, Gian Maria, additional, Lam, Ngoc-vy, additional, Zhu, Changlian, additional, Godin, Isabelle, additional, Muller, Kevin, additional, Chatzi, Afroditi, additional, Nuebel, Esther, additional, Ciccosanti, Fabiola, additional, Flamant, Stéphane, additional, Bénit, Paule, additional, Perfettini, Jean-Luc, additional, Sauvat, Allan, additional, Bennaceur-Griscelli, Annelise, additional, Ser-Le Roux, Karine, additional, Gonin, Patrick, additional, Tokatlidis, Kostas, additional, Rustin, Pierre, additional, Piacentini, Mauro, additional, Ruvo, Menotti, additional, Blomgren, Klas, additional, Kroemer, Guido, additional, and Modjtahedi, Nazanine, additional

Published
2015
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21. Orphan proteins of unknown function in the mitochondrial intermembrane space proteome: New pathways and metabolic cross-talk

Author

Nuebel, Esther, Manganas, Phanee, and Tokatlidis, Konstantinos

Subjects
Intermembrane space, Redox signalling, Metabolism, Mitochondrial proteome, Cell Biology, Molecular Biology, Protein import, Mitochondria
Abstract

The mitochondrial intermembrane space (IMS) is involved in protein transport, lipid homeostasis and metal ion exchange, while further acting in signalling pathways such as apoptosis. Regulation of these processes involves protein modifications, as well as stress-induced import or release of proteins and other signalling molecules. Even though the IMS is the smallest sub-compartment of mitochondria, its redox state seems to be tightly regulated. However, the way in which this compartment participates in the cross-talk between the multiple organelles and the cytosol is far from understood. Here we focus on newly identified IMS proteins that may represent future challenges in mitochondrial research. We present an overview of the import pathways, the recently discovered new components of the IMS proteome and how these relate to key aspects of cell signalling and progress made in stem cell and cancer research.

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22. Interaction between AIF and CHCHD4 Regulates Respiratory Chain Biogenesis

Author

Olivier Feraud, Fabiola Ciccosanti, Stephane Flamant, Annelise Bennaceur-Griscelli, Isabelle Godin, Kevin Müller, Karine Ser-Le Roux, Changlian Zhu, Kostas Tokatlidis, Gian Maria Fimia, Esther Nuebel, Menotti Ruvo, Jean-Luc Perfettini, Mauro Piacentini, Emilie Hangen, Haiwei Mou, Allan Sauvat, Patrick Gonin, Paule Bénit, Nunzianna Doti, Pierre Rustin, Ngoc vy Lam, Klas Blomgren, Afroditi Chatzi, Sylvie Lachkar, Guido Kroemer, Nazanine Modjtahedi, Hangen, Emilie, Féraud, Olivier, Lachkar, Sylvie, Mou, Haiwei, Doti, Nunzianna, Fimia, Gian Maria, Lam, Ngoc Vy, Zhu, Changlian, Godin, Isabelle, Muller, Kevin, Chatzi, Afroditi, Nuebel, Esther, Ciccosanti, Fabiola, Flamant, Stéphane, Bénit, Paule, Perfettini, Jean Luc, Sauvat, Allan, Bennaceur Griscelli, Annelise, Ser Le Roux, Karine, Gonin, Patrick, Tokatlidis, Kosta, Rustin, Pierre, Piacentini, Mauro, Ruvo, Menotti, Blomgren, Kla, Kroemer, Guido, Modjtahedi, Nazanine, Institut Gustave Roussy (IGR), Apoptose, cancer et immunité (Equipe labellisée Ligue contre le cancer - CRC - Inserm U1138), Institut Gustave Roussy (IGR)-Centre de Recherche des Cordeliers (CRC (UMR_S_1138 / U1138)), École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Université de Paris (UP)-École pratique des hautes études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-Université de Paris (UP), Centre de Recherche des Cordeliers (CRC (UMR_S_1138 / U1138)), Hématopoïèse normale et pathologique (U1170 Inserm), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Sud - Paris 11 (UP11)-Institut Gustave Roussy (IGR), École Pratique des Hautes Études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Université Paris Diderot - Paris 7 (UPD7)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-École Pratique des Hautes Études (EPHE), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Université Paris Diderot - Paris 7 (UPD7)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU), Institut interdisciplinaire d'anthropologie du contemporain (IIAC), École des hautes études en sciences sociales (EHESS)-Centre National de la Recherche Scientifique (CNRS), The Third Affiliated Hospital of Zhengzhou University, Zhengzhou University, Hematopoïese et cellules souches normales et pathologiques (U790), Université Paris-Sud - Paris 11 (UP11)-Institut Gustave Roussy (IGR)-Institut National de la Santé et de la Recherche Médicale (INSERM), National Institute for Infectious Diseases, Université Pierre et Marie Curie - Paris 6 - UFR de Médecine Pierre et Marie Curie (UPMC), Université Pierre et Marie Curie - Paris 6 (UPMC), Physiopathologie, conséquences fonctionnelles et neuroprotection des atteintes du cerveau en développement, Université Paris Diderot - Paris 7 (UPD7)-IFR2-Institut National de la Santé et de la Recherche Médicale (INSERM), Apoptose, cancer et immunité (U848), Hôpital Paul Brousse, Université Paris-Sud - Paris 11 (UP11)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Hôpital Paul Brousse, Institute of Molecular Biology and Biotechnology (IMBB), Foundation for Research and Technology - Hellas (FORTH), Handicaps génétiques de l'enfant (Inserm U393), Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM), CNR – Istituto di Biostrutture e Bioimmagini, Karolinska University Hospital [Stockholm], Radiothérapie moléculaire (UMR 1030), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Université Paris Diderot - Paris 7 (UPD7)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-École pratique des hautes études (EPHE), Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut Gustave Roussy (IGR)-Université Paris-Sud - Paris 11 (UP11), École pratique des hautes études (EPHE)-Université Paris Diderot - Paris 7 (UPD7)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU)-École pratique des hautes études (EPHE)-Université Paris Diderot - Paris 7 (UPD7)-Université Paris Descartes - Paris 5 (UPD5)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Sorbonne Université (SU), and Université Paris-Sud - Paris 11 (UP11)-Assistance publique - Hôpitaux de Paris (AP-HP) (APHP)-Hôpital Paul Brousse

Subjects
Time Factors, Mitochondrial intermembrane space, [SDV]Life Sciences [q-bio], Respiratory chain, Mitochondrial Membrane Transport Proteins, Mice, AIF, Mitochondrial Precursor Protein Import Complex Proteins, Respiratory function, ComputingMilieux_MISCELLANEOUS, Mice, Knockout, Tumor, Electron Transport Chain Complex Protein, apoptosis, Apoptosis Inducing Factor, Cell biology, Mitochondria, mitochondria, Protein Transport, Embryo, RNA Interference, biological phenomena, cell phenomena, and immunity, Amino Acid Sequence, Animals, Cell Line, Tumor, Electron Transport, Electron Transport Chain Complex Proteins, Embryo, Mammalian, Embryonic Development, Humans, Immunoblotting, Molecular Sequence Data, Protein Binding, Human, Programmed cell death, CHCHD4, amino acid sequence, animals, apoptosis inducing factor, cell line, tumor, electron transport, electron transport chain complex proteins, embryo, Settore BIO/06, AIFM1, Knockout, Biology, Cell Line, Downregulation and upregulation, Embryonic morphogenesis, cardiovascular diseases, Molecular Biology, Animal, Mammalian, Cell Biology, Mitochondrial Membrane Transport Protein, [SDV.BDD.EO]Life Sciences [q-bio]/Development Biology/Embryology and Organogenesis, Biogenesis
Abstract

Apoptosis-inducing factor (AIF) is a mitochondrial flavoprotein that, beyond its apoptotic function, is required for the normal expression of major respiratory chain complexes. Here we identified an AIF-interacting protein, CHCHD4, which is the central component of a redox-sensitive mitochondrial intermembrane space import machinery. Depletion or hypomorphic mutation of AIF caused a downregulation of CHCHD4 protein by diminishing its mitochondrial import. CHCHD4 depletion sufficed to induce a respiratory defect that mimicked that observed in AIF-deficient cells. CHCHD4 levels could be restored in AIF-deficient cells by enforcing its AIF-independent mitochondrial localization. This modified CHCHD4 protein reestablished respiratory function in AIF-deficient cells and enabled AIF-deficient embryoid bodies to undergo cavitation, a process of programmed cell death required for embryonic morphogenesis. These findings explain how AIF contributes to the biogenesis of respiratory chain complexes, and they establish an unexpected link between the vital function of AIF and the propensity of cells to undergo apoptosis.

Published
2015
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