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Your search keyword '"M.J. Millan"' showing total 8 results
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8 results on '"M.J. Millan"'

3. The PINK1 kinase-driven ubiquitin ligase Parkin promotes mitochondrial protein import through the presequence pathway in living cells

Author

Zoi Erpapazoglou, M.J. Millan, C. Mannoury la Cour, D. Guedin, Olivier Nosjean, Alexis Brice, Jean A. Boutin, E. Hamon-Keromen, J. W. Harper, Maxime Jacoupy, F. Coge, Jean-Christophe Corvol, Clement A. Gautier, Olga Corti, Alban Ordureau, Institut du Cerveau = Paris Brain Institute (ICM), Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Institut National de la Santé et de la Recherche Médicale (INSERM)-CHU Pitié-Salpêtrière [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU)-Sorbonne Université (SU)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Sorbonne Université (SU), Harvard Medical School [Boston] (HMS), Institut de Recherches SERVIER (IRS), Service de Neurologie [CHU Pitié-Salpêtrière], IFR70-CHU Pitié-Salpêtrière [AP-HP], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU), Gestionnaire, Hal Sorbonne Université, Institut du Cerveau et de la Moëlle Epinière = Brain and Spine Institute (ICM), Institut National de la Santé et de la Recherche Médicale (INSERM)-CHU Pitié-Salpêtrière [AP-HP], Sorbonne Université (SU)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS), Sorbonne Université (SU)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP), Service de neurologie 1 [CHU Pitié-Salpétrière], Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-CHU Pitié-Salpêtrière [AP-HP], and Sorbonne Université (SU)-Assistance publique - Hôpitaux de Paris (AP-HP) (AP-HP)-Sorbonne Université (SU)

Subjects
Science, Ubiquitin-Protein Ligases, Parkinson's disease, [SDV]Life Sciences [q-bio], PINK1, Biosensing Techniques, Mitochondrion, Parkin, Article, Mitochondrial Proteins, 03 medical and health sciences, 0302 clinical medicine, Ubiquitin, Translocase, Humans, 030304 developmental biology, 0303 health sciences, Multidisciplinary, biology, HEK 293 cells, Ubiquitin ligase, Transport protein, Cell biology, Mitochondria, nervous system diseases, [SDV] Life Sciences [q-bio], Protein Transport, HEK293 Cells, Mechanisms of disease, biology.protein, Medicine, Protein Kinases, 030217 neurology & neurosurgery
Abstract

Most of over a thousand mitochondrial proteins are encoded by nuclear genes and must be imported from the cytosol. Little is known about the cytosolic events regulating mitochondrial protein import, partly due to the lack of appropriate tools for its assessment in living cells. We engineered an inducible biosensor for monitoring the main presequence-mediated import pathway with a quantitative, luminescence-based readout. This tool was used to explore the regulation of mitochondrial import by the PINK1 kinase-driven Parkin ubiquitin ligase, which is dysfunctional in autosomal recessive Parkinson’s disease. We show that mitochondrial import was stimulated by Parkin, but not by disease-causing Parkin variants. This effect was dependent on Parkin activation by PINK1 and accompanied by an increase in the abundance of K11 ubiquitin chains on mitochondria and by ubiquitylation of subunits of the translocase of outer mitochondrial membrane. Mitochondrial import efficiency was abnormally low in cells from patients with PINK1- and PARK2-linked Parkinson’s disease and was restored by phosphomimetic ubiquitin in cells with residual Parkin activity. Altogether, these findings uncover a role of ubiquitylation in mitochondrial import regulation and suggest that loss of this regulatory loop may underlie the pathophysiology of Parkinson’s disease, providing novel opportunities for therapeutic intervention.

Published
2019
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4. P.1.01 Time-dependent progression of tauopathy and disruption of synaptic proteins in the PS19 P301S transgenic mouse

Author

Catherine Liard, A. Gobert, Nathalie Dumas, F. Iop, M.J. Millan, Ross Jeggo, V. Pasteau, A. Francois, Rodolphe Billiras, G. Das Dores, Sylvie Girardon, and K. Lliopis

Subjects
Pharmacology, Genetically modified mouse, Psychiatry and Mental health, Neurology, medicine, Pharmacology (medical), Neurology (clinical), Tauopathy, Biology, medicine.disease, Biological Psychiatry, Cell biology
Published
2019
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7. Inactivation of the orphan G protein-coupled receptor Gpr88 in the dorsal striatum reverses the effects of dopamine depletion in a rat model of Parkinson’s disease

Author

Jonathan Pegon, Jacques Mallet, Rolando Meloni, Benjamin Galet, M. Ingallinesi, A. Do Thi, C. Mannoury la Cour, M.J. Millan, and N. Faucon Biguet

Subjects
Pharmacology, Dorsum, medicine.medical_specialty, Parkinson's disease, Chemistry, Rat model, Striatum, medicine.disease, Psychiatry and Mental health, Endocrinology, Neurology, Dopamine receptor D3, Dopamine, Dopamine receptor D2, Internal medicine, medicine, Pharmacology (medical), Neurology (clinical), Orphan G-Protein Coupled Receptor, Neuroscience, Biological Psychiatry, medicine.drug
Published
2017
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8. S.24.04 Cognitive deficits of schizophrenia and their control by the mTOR pathway

Author

Julie Meffre, M.J. Millan, Philippe Marin, C. Mannoury la Cour, David J. G. Watson, Kevin C. F. Fone, and J. Bockaert

Subjects
Pharmacology, business.industry, Schizophrenia (object-oriented programming), Cognition, Psychiatry and Mental health, Neurology, Medicine, Pharmacology (medical), Neurology (clinical), business, Control (linguistics), Neuroscience, Biological Psychiatry, PI3K/AKT/mTOR pathway
Published
2015
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