Morgane Le Bras

ORCID: 0000-0003-4317-5591
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Research Areas
  • Retinoids in leukemia and cellular processes
  • Neuroblastoma Research and Treatments
  • Mitochondrial Function and Pathology
  • RNA Interference and Gene Delivery
  • Cell death mechanisms and regulation
  • Cancer, Hypoxia, and Metabolism
  • RNA Research and Splicing
  • RNA modifications and cancer
  • Advanced biosensing and bioanalysis techniques
  • Cancer-related Molecular Pathways
  • Acute Myeloid Leukemia Research
  • Parasites and Host Interactions
  • RNA and protein synthesis mechanisms
  • ATP Synthase and ATPases Research
  • Ubiquitin and proteasome pathways
  • Lung Cancer Research Studies
  • MicroRNA in disease regulation
  • Neuroendocrine Tumor Research Advances
  • CRISPR and Genetic Engineering
  • Antioxidant Activity and Oxidative Stress
  • Herpesvirus Infections and Treatments
  • Cancer-related gene regulation
  • Ocular Oncology and Treatments
  • Infectious Encephalopathies and Encephalitis
  • Autophagy in Disease and Therapy

Inserm
2014-2024

Université Paris Cité
2011-2023

Hôpital Saint-Louis
2009-2022

Centre de Recherche en Cancérologie de Toulouse
2016-2022

Université Toulouse III - Paul Sabatier
2016-2022

Institut de recherche Saint-Louis
2020-2022

HIPI - Immunologie humaine, physiopathologie et immunithérapie
2022

Centre d'Investigation Clinique de Nantes
2014-2021

Centre National de la Recherche Scientifique
2007-2017

Délégation Paris 7
2011-2017

Abstract RNA G-quadruplexes (RG4s) are four-stranded structures known to control mRNA translation of cancer relevant genes. RG4 formation is pervasive in vitro but not cellulo, indicating the existence poorly characterized molecular machinery that remodels RG4s and maintains them unfolded. Here, we performed a quantitative proteomic screen identify cytosolic proteins interact with canonical its folded unfolded conformation. Our results identified hnRNP H/F as important components cytoplasmic...

10.1038/s41467-020-16168-x article EN cc-by Nature Communications 2020-05-27

Promyelocytic leukemia (PML) nuclear bodies (NBs) recruit partner proteins, including p53 and its regulators, thereby controlling their abundance or function. Investigating arsenic sensitivity of acute promyelocytic leukemia, we proposed that PML oxidation promotes NB biogenesis. However, physiological links between oxidative stress response in vivo remain unexplored. Here, identify as a reactive oxygen species (ROS) sensor. Pml-/- cells accumulate ROS, whereas expression decreases ROS...

10.1084/jem.20160301 article EN cc-by-nc-sa The Journal of Experimental Medicine 2017-09-20

Multiple endocrine neoplasia syndrome type 1 (MEN1), which is secondary to mutation of the MEN1 gene, a rare autosomal-dominant disease that predisposes carriers tumors. Although genotype-phenotype studies have so far failed identify any statistical correlations, some families harbor recurrent tumor patterns. The function MENIN unclear, but has been described through discovery its interacting partners. Mutations in domains functional partners shown directly alter regulation abilities. We...

10.1093/hmg/ddt039 article EN Human Molecular Genetics 2013-01-31

Significance Promyelocytic leukemia protein (PML) nuclear bodies (NBs) are subnuclear domains proposed to facilitate posttranslational modifications. Among NB partners, proteins p53 and most of the regulators. Overexpression a single PML splice variant, IV, triggers p53-driven senescence. We demonstrate an interaction between IV C terminus ARF tumor suppressor. This is required promote SUMOylation subsequent stabilization. These results unexpectedly bridge three key suppressors stress role...

10.1073/pnas.1507540112 article EN Proceedings of the National Academy of Sciences 2015-11-02

Abstract Mitochondrial membrane permeabilization (MMP) is a rate-limiting step of apoptosis, including in anticancer chemotherapy. Adenine nucleotide translocase (ANT) mediates the exchange ADP and ATP on inner mitochondrial healthy cells. In addition, ANT can cooperate with Bax to form lethal pore during apoptosis. Humans possess four distinct isoforms, encoded by genes, whose transcription depends cell type, developmental stage, proliferation, hormone status. Here, we show that ANT2 gene...

10.1158/0008-5472.can-05-4407 article EN Cancer Research 2006-09-15

Replication of human cytomegalovirus (CMV) requires the expression viral mitochondria–localized inhibitor apoptosis (vMIA). vMIA inhibits by recruiting Bax to mitochondria, resulting in its neutralization. We show that decreases cell size, reduces actin polymerization, and induces rounding. As compared with vMIA-expressing CMV, vMIA-deficient which replicates fibroblasts expressing adenoviral suppressor E1B19K, less cytopathic effects. These effects can be separated from death–inhibitory...

10.1083/jcb.200604069 article EN The Journal of Cell Biology 2006-09-18

Inhibitors of HIV protease have been shown to antiapoptotic effects in vitro, yet whether these are seen vivo remains controversial. In this study, we evaluated the impact inhibitor (PI) nelfinavir, boosted with ritonavir, models nonviral disease associated excessive apoptosis. mice Fas-induced fatal hepatitis, Staphylococcal enterotoxin B-induced shock, and middle cerebral artery occlusion-induced stroke, demonstrate that PIs significantly reduce apoptosis improve histology, function,...

10.1172/jci22954 article EN Journal of Clinical Investigation 2005-06-04

The promyelocytic leukemia (PML) tumour suppressor is the organiser of PML nuclear bodies, which are domains precise functions still disputed. We show that upon several types stress, endogenous proteins form nucleolar caps and eventually engulf components. Only two specific splice variants (PML-I PML-IV) efficiently targeted to nucleolus abundant PML-I isoform required for targeting this organelle. identified a domain within evolutionarily conserved C-terminus PML-I. This contains predicted...

10.1242/jcs.007492 article EN Journal of Cell Science 2007-09-15

Despite the clinical success of blocking inhibitory immune checkpoint receptors such as programmed cell death-1 (PD-1) in cancer, mechanisms controlling expression these have not been fully elucidated. Here, we identify a post-transcriptional mechanism regulating PD-1 T cells. Upon activation, PDCD1 mRNA and ribonucleoprotein complexes coalesce into stress granules that require microtubules kinesin 1 molecular motor to proceed translation. Hence, is highly sensitive microtubule or granule...

10.1016/j.celrep.2018.12.014 article EN cc-by-nc-nd Cell Reports 2019-01-01

Since its discovery, 25 years ago, promyelocytic leukemia (PML) has been an enigma. Implicated in the oncogenic PML/RARA fusion, forming elusive intranuclear domains, triggering cell death or senescence, controlled by and perhaps controlling SUMOylation… there are multiple PML-related issues. Here we review reciprocal interactions between PML, SUMOylation, notably context of cellular transformation.

10.3389/fonc.2013.00171 article EN cc-by Frontiers in Oncology 2013-01-01

The mutagenic properties of ionizing radiation are well known, but the presence specific mutations in human radiation-induced tumours is not established. We have studied a series 36 secondary sarcomas arising irradiation field primary tumour following radiotherapy. allelic status and TP53 gene were investigated. mutation pattern was compared with data from sporadic recorded IARC somatic database. A high proportion (58%) exhibited inactivating for one allele TP53, systematically associated...

10.1093/carcin/bgi356 article EN Carcinogenesis 2006-02-20

MEN1, which is secondary to the mutation of MEN1 gene, a rare autosomal-dominant disease that predisposes carriers endocrine tumors. Most studies demonstrated absence direct genotype-phenotype correlations. The existence higher risk death in Groupe d'étude des Tumeurs Endocrines-cohort associated with JunD interacting domain suggests heterogeneity across families expressivity. This study aims assess modifying genetic factors by estimating intrafamilial correlations and heritability six main...

10.1530/eje-15-0691 article EN European Journal of Endocrinology 2015-09-22

// Anne Cammas 1, 2, * , Magali Lacroix-Triki 3, Sandra Pierredon 3 Morgane Le Bras 2 Jason S. Iacovoni Marie-Paule Teulade-Fichou 4, 5 Gilles Favre Henri Roché Thomas Filleron Stefania Millevoi Stéphan Vagner 6, 7, 8 1 INSERM UMR 1037, Centre de Recherches en Cancérologie Toulouse, France Université Toulouse III Paul Sabatier, Institut Claudius Regaud, 4 Curie, PSL Research University, CNRS 176, Orsay, 3348, 6 Paris Sud, Paris-Saclay, 7 Equipe Labellisée...

10.18632/oncotarget.7589 article EN Oncotarget 2016-02-22
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