A5029133670- Glycosylation and Glycoproteins Research
- RNA and protein synthesis mechanisms
- Cellular transport and secretion
- Carbohydrate Chemistry and Synthesis
- HIV Research and Treatment
- HIV/AIDS drug development and treatment
- RNA modifications and cancer
- Invertebrate Immune Response Mechanisms
- Ubiquitin and proteasome pathways
- Enzyme Production and Characterization
- Galectins and Cancer Biology
- Endoplasmic Reticulum Stress and Disease
- Mitochondrial Function and Pathology
- Autophagy in Disease and Therapy
- Supramolecular Self-Assembly in Materials
- Protein Structure and Dynamics
- ATP Synthase and ATPases Research
- Lipid Membrane Structure and Behavior
- Cancer, Hypoxia, and Metabolism
University of Copenhagen
2021-2023
CEA Paris-Saclay
2016-2020
Centre National de la Recherche Scientifique
2016-2020
Université Paris-Saclay
2016-2020
Commissariat à l'Énergie Atomique et aux Énergies Alternatives
2016-2020
Université Paris-Sud
2020
University of Oulu
2018-2020
Institut de Biologie Intégrative de la Cellule
2016-2018
Laboratoire d'Enzymologie et Biochimie Structurales
2016
Branching and processing of N-glycans in the medial-Golgi rely both on transport donor UDP-N-acetylglucosamine (UDP-GlcNAc) to Golgi lumen by SLC35A3 nucleotide sugar transporter (NST) as well addition GlcNAc residue terminal mannoses nascent several linkage-specific N-acetyl-glucosaminyltransferases (MGAT1-MGAT5). Previous data indicate that MGATs NSTs form higher order assemblies membranes. Here, we investigate their specific mutual interactions using high-throughput FRET- BiFC-based...
Abstract Introduction In epithelial cancers, truncated O-glycans, such as the Thomson-nouveau antigen (Tn) and its sialylated form (STn), are upregulated on cell surface associated with poor prognosis immunological escape. Recent studies have shown that these carbohydrate epitopes facilitate cancer development can be targeted therapeutically; however, mechanism underpinning their expression remains unclear. Methods To identify genes directly influencing of cancer-associated we conducted an...
Glycosylation, a common modification of cellular proteins and lipids, is often altered in diseases pathophysiological states such as hypoxia, yet the underlying molecular causes remain poorly understood. By utilizing lectin microarray glycan profiling, Golgi pH redox screens, we show here that hypoxia inhibits terminal sialylation N- O-linked glycans HIF- independent manner by lowering oxidative potential. This state change was accompanied loss two surface-exposed disulfide bonds catalytic...
The upstream stimulatory factor 2 (USF2) is a transcription implicated in several cellular processes and among them, tumor development seems to stand out. However, the data with respect role of USF2 are conflicting suggesting that it acts either as promoter or suppressor. Here we show absence promotes proliferation migration. Thereby, reveal previously unknown function mitochondrial homeostasis. Mechanistically, demonstrate deficiency survival by inducing mitophagy ROS-sensitive manner...
Most glycosyltransferases, including B4GalT1 (EC 2.4.1.38), are known to assemble into enzyme homomers and functionally relevant heteromers in vivo. However, it remains unclear why how these enzymes interact at the molecular/atomic level. Here, we solved crystal structure of wild-type human homodimer. We also show that exists a dynamic equilibrium between monomer dimer, since purified reappears as mixture both obtained forms dimer assemblies same crystallization conditions. These two...
Human cytoplasmic lysyl-tRNA synthetase (LysRS) is associated within a multi-aminoacyl-tRNA complex (MSC). Within this complex, the p38 component scaffold protein that binds catalytic domain of LysRS via its N-terminal region. In addition to translational function when MSC, also recruited in nontranslational roles after dissociation from MSC. The balance between MSC-associated and MSC-dissociated states essential regulate functions cellular homeostasis. With aim understanding rules govern...
An important step in human immunodeficiency virus type 1 (HIV-1) replication is the packaging of tRNA3Lys from host cell, which plays role primer RNA process initiation reverse transcription. The viral GagPol polyprotein precursor, and mitochondrial lysyl-tRNA synthetase (mLysRS) have been proposed to be involved process. More specifically, catalytic domain mLysRS supposed interact with transframe (TF or p6*) integrase (IN) domains Pol region polyprotein. In this work, we report a...
Replication of human immunodeficiency virus type 1 (HIV-1) requires the packaging tRNALys,3 from host cell into new viral particles. The GagPol polyprotein precursor associates with mitochondrial lysyl-tRNA synthetase (mLysRS) in a complex tRNALys, an essential step to initiate reverse transcription virions. C-terminal integrase moiety is for its association mLysRS. We show that integrases HIV-1 and HIV-2 bind mLysRS same efficiency. In this work, we have undertaken probe three-dimensional...