Lucie Bergdoll

ORCID: 0000-0001-6068-238X
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About
Contact & Profiles
Research Areas
  • Mitochondrial Function and Pathology
  • ATP Synthase and ATPases Research
  • Metabolism and Genetic Disorders
  • Photosynthetic Processes and Mechanisms
  • Metabolomics and Mass Spectrometry Studies
  • Receptor Mechanisms and Signaling
  • Fuel Cells and Related Materials
  • RNA and protein synthesis mechanisms
  • Neuroscience and Neuropharmacology Research
  • Electrochemical Analysis and Applications
  • Ion channel regulation and function
  • Electron Spin Resonance Studies
  • Lipid Membrane Structure and Behavior
  • Microbial Inactivation Methods
  • Nanopore and Nanochannel Transport Studies
  • thermodynamics and calorimetric analyses
  • Mass Spectrometry Techniques and Applications
  • Advanced NMR Techniques and Applications
  • Gene Regulatory Network Analysis
  • Medical Imaging Techniques and Applications
  • Photoreceptor and optogenetics research
  • Advanced Thermodynamics and Statistical Mechanics
  • Gas Dynamics and Kinetic Theory
  • Chemistry and Stereochemistry Studies
  • Advanced MRI Techniques and Applications

Centre National de la Recherche Scientifique
2012-2024

Aix-Marseille Université
2012-2024

Laboratoire d'Ingénierie des Systèmes Macromoléculaires
2023-2024

Laboratoire de Photochimie et d'Ingénierie Macromoléculaire
2023

University of California, Los Angeles
2017-2020

Institut de Biologie Physico-Chimique
2012-2016

Laboratoire de Biologie Physico-Chimique des Protéines Membranaires
2014-2016

Université Paris Cité
2012-2014

Sorbonne Université
2012

Délégation Provence et Corse
2012

Voltage-dependent anion channel-1 (VDAC1) is a highly regulated β-barrel membrane protein that mediates transport of ions and metabolites between the mitochondria cytosol cell. VDAC1 co-purifies with cholesterol functionally by cholesterol, among other endogenous lipids. Molecular modeling studies based on NMR observations have suggested five cholesterol-binding sites in VDAC1, but direct experimental evidence for these lacking. Here, to determine binding, we photolabeled purified mouse...

10.1074/jbc.m116.773069 article EN cc-by Journal of Biological Chemistry 2017-04-11

10.1016/j.bbabio.2016.06.006 article EN publisher-specific-oa Biochimica et Biophysica Acta (BBA) - Bioenergetics 2016-06-22

Voltage-dependent anion channel (VDAC) is the major pathway for transport of ions and metabolites across mitochondrial outer membrane. Among three known mammalian VDAC isoforms, VDAC3 least characterized, but unique functional roles have been proposed in cellular animal models. Yet, a high-sequence similarity between VDAC1 indicative similar pore-forming structure. Here, we conclusively show that forms stable, highly conductive voltage-gated channels that, much like VDAC1, are weakly...

10.1085/jgp.201912501 article EN cc-by-nc-sa The Journal of General Physiology 2020-01-14

Dimeric tubulin, an abundant water-soluble cytosolic protein known primarily for its role in the cytoskeleton, is routinely found to be associated with mitochondrial outer membranes, although structure and physiological of mitochondria-bound tubulin are still unknown. There also no consensus on whether a peripheral membrane or integrated into membrane. Here results five independent techniques-surface plasmon resonance, electrochemical impedance spectroscopy, bilayer overtone analysis,...

10.1073/pnas.1619806114 article EN Proceedings of the National Academy of Sciences 2017-04-18

The voltage-dependent anion channel (VDAC) is the most abundant protein in outer mitochondrial membrane and constitutes primary pathway for exchange of ions metabolites between cytosol mitochondria. There accumulating evidence supporting VDAC's role metabolic regulation apoptosis, where VDAC oligomerization has been implicated with these processes. Herein, we report a specific pH-dependent dimerization murine VDAC1 (mVDAC1) identified by double electron-electron resonance native mass...

10.1073/pnas.1715464115 article EN Proceedings of the National Academy of Sciences 2017-12-26

Mitochondrial physiology is intricately linked to the oligomerization of voltage-dependent anion channels (VDAC), acting as gatekeepers mitochondria. However, molecular determinants VDAC remain poorly understood. Here, we used atomic force microscopy investigate effects three lipids Outer Membrane (MOM) on assemblies. We observed that forms lipid-sensitive clusters, termed honeycombs, and their compaction regulated by cholesterol. Molecular dynamics simulations revealed VDAC’s affinity for...

10.1101/2024.06.26.597124 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2024-06-26

Identifying sites of protein-ligand interaction is important for structure-based drug discovery and understanding protein structure-function relationships. Mass spectrometry (MS) has emerged as a useful tool identifying residues covalently modified by ligands. Current methods use database searches that are dependent on acquiring interpretable fragmentation spectra (MS2) peptide-ligand adducts. This problematic hydrophobic ligand incorporation in integral membrane proteins (IMPs), where poor...

10.1021/acs.analchem.6b05003 article EN Analytical Chemistry 2017-01-27

The voltage-dependent anion channel (VDAC) is a β-barrel of the mitochondrial outer membrane (MOM) that passively transports ions, metabolites, polypeptides, and single-stranded DNA. VDAC responds to transmembrane potential by "gating," i.e. transitioning one variety low-conducting states unknown structure. gated state results in nearly complete suppression multivalent metabolite (such as ATP ADP) transport, while enhancing calcium transport. Voltage gating universal property channels, but...

10.1021/jacs.2c03316 article EN Journal of the American Chemical Society 2022-08-04

Supralinear scaling is found when functional groups attached to the pore inner wall have opposite charges those located in nanochannel's outer surface.

10.1039/d4na00540f article EN cc-by Nanoscale Advances 2024-01-01

10.1016/j.bbabio.2012.06.364 article EN publisher-specific-oa Biochimica et Biophysica Acta (BBA) - Bioenergetics 2012-08-09

10.1016/j.bbabio.2014.05.329 article publisher-specific-oa Biochimica et Biophysica Acta (BBA) - Bioenergetics 2014-06-26
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