Gwénaël Rabut

ORCID: 0000-0003-2658-2769
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About
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Research Areas
  • Ubiquitin and proteasome pathways
  • Nuclear Structure and Function
  • RNA Research and Splicing
  • Bioinformatics and Genomic Networks
  • Protein Degradation and Inhibitors
  • RNA regulation and disease
  • Autophagy in Disease and Therapy
  • Fungal and yeast genetics research
  • Biomedical Text Mining and Ontologies
  • DNA Repair Mechanisms
  • Peptidase Inhibition and Analysis
  • Advanced Fluorescence Microscopy Techniques
  • HIV Research and Treatment
  • Immune Cell Function and Interaction
  • Genomics and Chromatin Dynamics
  • Receptor Mechanisms and Signaling
  • HIV/AIDS drug development and treatment
  • Advanced Proteomics Techniques and Applications
  • Computational Drug Discovery Methods
  • Cell Image Analysis Techniques
  • 14-3-3 protein interactions
  • Semantic Web and Ontologies
  • Neurobiology and Insect Physiology Research
  • Pharmacological Effects and Assays
  • T-cell and B-cell Immunology

Institut de génétique et de développement de Rennes
2011-2025

Université de Rennes
2012-2025

Centre National de la Recherche Scientifique
2012-2025

Inserm
2023-2025

Université Européenne de Bretagne
2011-2012

Structure Fédérative de Recherche en Biologie et Santé de Rennes
2012

ETH Zurich
2008-2011

European Molecular Biology Laboratory
2000-2008

European Bioinformatics Institute
2004

European Molecular Biology Laboratory
2001

The nuclear pore complexes (NPCs) are evolutionarily conserved assemblies that allow traffic between the cytoplasm and nucleus. In this study, we have identified characterized a novel human protein, hNup133, through its homology with Saccharomyces cerevisiae nucleoporin scNup133. Two-hybrid screens immunoprecipitation experiments revealed direct interaction Nup133 Nup84/Nup107 indicated hNup133 hNup107 part of NPC subcomplex contains two other nucleoporins (the previously hNup96 designated...

10.1083/jcb.200101081 article EN public-domain The Journal of Cell Biology 2001-09-17

In eukaryotes, bidirectional transport of macromolecules between the cytoplasm and nucleus occurs through elaborate supramolecular structures embedded in nuclear envelope, pore complexes (NPCs). NPCs are composed multiple copies approximately 30 different proteins termed nucleoporins, which several can be biochemically isolated as subcomplexes. One such building block NPC, Nup107-160 complex vertebrates, was so far demonstrated to six nucleoporins. Here, we identify three WD (Trp-Asp)-repeat...

10.1091/mbc.e03-12-0878 article EN Molecular Biology of the Cell 2004-05-18

During mitosis in higher eukaryotes, nuclear pore complexes (NPCs) disassemble prophase and are rebuilt anaphase telophase. NPC formation is hypothesized to occur by the interaction of mitotically stable subcomplexes that form defined structural intermediates. To determine sequence events lead breakdown reformation functional NPCs during mitosis, we present here our quantitative assay based on confocal time-lapse microscopy single dividing cells. We use this systematically investigate...

10.1083/jcb.200707026 article EN The Journal of Cell Biology 2008-03-03

ABSTRACT The CC-chemokine receptor CCR5 mediates fusion and entry of the most commonly transmitted human immunodeficiency virus type 1 (HIV-1) strains. We have isolated six new anti-CCR5 murine monoclonal antibodies (MAbs), designated PA8, PA9, PA10, PA11, PA12, PA14. A panel alanine point mutants was used to map epitopes these MAbs previously described MAb 2D7 specific amino acid residues in N terminus and/or second extracellular loop regions CCR5. This structural information correlated...

10.1128/jvi.73.5.4145-4155.1999 article EN Journal of Virology 1999-05-01

The technique of fluorescence recovery after photobleaching (FRAP) was introduced in the mid-1970s to study diffusion biomolecules living cells. For several years, it used mainly by a small number biophysicists who had developed their own systems. Since mid-1990s, FRAP has gained increasing popularity because conjunction two factors: First, techniques are easily implemented on confocal laser-scanning microscopes (CLSMs), and so become available anyone access such equipment. Second, advent...

10.1101/pdb.top90 article EN Cold Spring Harbor Protocols 2010-12-01

Breakdown of the nuclear envelope (NE) was analyzed in live starfish oocytes using a size series fluorescently labeled dextrans, membrane dyes, and GFP-tagged proteins pore complex (NPC) lamina. Permeabilization nucleus occurred two sequential phases. In phase I NE became increasingly permeable for molecules up to ∼40 nm diameter, concurrent with loss peripheral components over time course 10 min. The remained intact on ultrastructural level during this time. II completely permeabilized...

10.1083/jcb.200211076 article EN The Journal of Cell Biology 2003-03-24

Summary Live cell imaging has become an indispensable technique for biologists. However, when grown on coverslip glass used live many cultured cells move even during relatively short observation times and focus can drift as a result of mechanical instabilities and/or temperature fluctuations. Time‐lapse therefore requires constant adjustment the field position to keep interest centred in imaged volume. We show here that this limitation be overcome by tracking fully automated way using mass...

10.1111/j.0022-2720.2004.01404.x article EN Journal of Microscopy 2004-10-28

Cullin-RING ligases (CRLs) are ubiquitin E3 enzymes with variable substrate-adaptor and -receptor subunits. All CRLs activated by modification of the cullin subunit ubiquitin-like protein Nedd8 (neddylation). The CAND1 (Cullin-associated-Nedd8-dissociated-1) also promotes CRL activity, even though it only interacts inactive ligase complexes. molecular mechanism underlying this behaviour remains largely unclear. Here, we find that yeast SCF (Skp1-Cdc53-F-box) complexes remodelled in a...

10.1038/ncomms2628 article EN cc-by-nc-nd Nature Communications 2013-03-27

Multiple extracellular domains of the CC-chemokine receptor CCR5 are important for its function as a human immunodeficiency virus type 1 (HIV-1) coreceptor. We have recently demonstrated by alanine scanning mutagenesis that negatively charged residues in amino-terminal domain essential gp120 binding and coreceptor function. now extended our analysis this to include most polar nonpolar amino acids. Replacement with all four tyrosine serine-17 cysteine-20 decrease or abolish activity....

10.1128/jvi.72.4.3464-3468.1998 article EN Journal of Virology 1998-04-01

Metazoan NXF1-p15 heterodimers promote the nuclear export of bulk mRNA across pore complexes (NPCs). In vitro, forms a stable complex with nucleoporin RanBP2/Nup358, component cytoplasmic filaments NPC, suggesting role for this in export. We show that depletion RanBP2 from Drosophila cells inhibits proliferation and Concomitantly, localization NXF1 at NPC is strongly reduced significant fraction normally protein detected cytoplasm. Under same conditions, steady-state subcellular other or...

10.1128/mcb.24.3.1155-1167.2004 article EN Molecular and Cellular Biology 2004-01-16

Abstract The fungal Bromodomain and Extra‐Terminal (BET) protein Bdf1 is a potential antifungal target against invasive infections. However, the need to selectively inhibit both bromodomains (BDs) over human orthologs lack of molecular tools assess on‐target efficacy hamper efforts develop BD inhibitors as therapeutics. This study reports phenyltriazine compound that inhibits BDs from pathogen Candida glabrata with selectivity orthologous BET Brd4. On‐target activity established by devising...

10.1002/advs.202404260 article EN cc-by Advanced Science 2025-01-16

Ubiquitin-binding domains (UBDs) provide specificity to the ubiquitin system, which is also involved in translesion synthesis (TLS) eukaryotic cells. Upon DNA damage, UBDs (UBM domains) of polymerase iota (Pol ι) interact with ubiquitinated proliferating cell nuclear antigen regulate interchange between processive polymerases and TLS. We report a biophysical analysis solution structures two conserved UBM located C-terminal tail murine Pol ι complex ubiquitin. The 35-amino acid core folds...

10.1074/jbc.m110.135038 article EN cc-by Journal of Biological Chemistry 2010-10-08

Ubiquitylation is a reversible post-translational protein modification that regulates multitude of cellular processes. Detection ubiquitylated proteins often challenging because their low abundance. Here, we present NUbiCA, sensitive protein-fragment complementation assay to facilitate the monitoring ubiquitylation events in cultured cells and model organisms. Using yeast as system, demonstrate NUbiCA enables accurate mono- polyubiquitylation expressed at endogenous levels. We also show it...

10.1242/jcs.240093 article EN publisher-specific-oa Journal of Cell Science 2020-05-14

10.1016/s0960-9822(01)00340-2 article EN publisher-specific-oa Current Biology 2001-07-01
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