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Articles by Juliette Fedry
Cotranslational membrane protein biogenesis by an EMC-bound translocon
Abstract Secretory and membrane protein biogenesis occurs at ribosome-bound translocons in the endoplasmic reticulum (ER) membrane. Translocons consist of the Sec61 protein-conducting channel and various maturation factors including chaperones, modification enzymes and membrane insertases, which assemble dynamically in response to the biogenesis needs of a nascent polypeptide.
Visualization of translation reorganization upon persistent ribosome collision stress in mammalian cells
Highlights • The native disome interface extends to the L1 stalk and eEF2 • Collisions vary in composition and conformation over time, with some bound to GCN1 • Saturation of the RQC leads to accumulation of non-functional tRNA-bound 60S complexes • The accumulation of aberrant 40S complexes indicates an impairment of initiation Summary Aberrantly slow ribosomes incur collisions, a sentinel of stress that triggers quality control, signaling, and translation attenuation.
Visualization of translation reorganization upon persistent ribosome collision stress in mammalian cells
Highlights • The native disome interface extends to the L1 stalk and eEF2 • Collisions vary in composition and conformation over time, with some bound to GCN1 • Saturation of the RQC leads to accumulation of non-functional tRNA-bound 60S complexes • The accumulation of aberrant 40S complexes indicates an impairment of initiation Summary Aberrantly slow ribosomes incur collisions, a sentinel of stress that triggers quality control, signaling, and translation attenuation.
TMX4-driven LINC complex disassembly and asymmetric autophagy of the nuclear envelope upon acute ER stress - Nature Communications
Antibodies, expression plasmids Commercial antibodies used in this study: Lamp1 (DSHB Hybridoma Product 1D4B deposited by J. T. August, Immunofluorescence (IF) 1:50), V5 (Western blot (WB) 1:5000 Thermo Fisher Scientific), GFP (WB 1:1000 IEM: 1:50 Abcam), TMX4 (WB 1:1000, IEM:1:20 Proteintech), TEX264 (IEM: 1:50 Novus), LC3B (IF: 1:50 Sigma), GAPDH (WB 1:30000 Millipore), KDEL (WB 1:1000 Stressgen), HaloTag (WB 1:1000 Promega), PDI (WB 1:100 Stressgen), Erp72 (WB 1:100 Stressgen).
Visualization of translation reorganization upon persistent collision stress in mammalian cells
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Visualization of translation and protein biogenesis at the ER membrane - Nature
Abstract The dynamic ribosome–translocon complex, which resides at the endoplasmic reticulum (ER) membrane, produces a major fraction of the human proteome1,2. It governs the synthesis, translocation, membrane insertion, N-glycosylation, folding and disulfide-bond formation of nascent proteins. Although individual components of this machinery have been studied at high resolution in isolation3,4,5,6,7, insights into their interplay in the native membrane remain limited.
Structural insights into the cross-neutralization of SARS-CoV and SARS-CoV-2 by the human monoclonal antibody 47D11
Abstract The emergence of SARS-CoV-2 antibody escape mutations highlights the urgent need for broadly neutralizing therapeutics. We previously identified a human monoclonal antibody, 47D11, capable of cross-neutralizing SARS-CoV-2 and SARS-CoV and protecting against the associated respiratory disease in an animal model. Here, we report cryo-EM structures of both trimeric spike ectodomains in complex with the 47D11 Fab.
Species-Specific Functional Regions of the Green Alga Gamete Fusion Protein HAP2 Revealed by Structural Studies
The cellular fusion protein HAP2, which is structurally homologous to viral class II fusion proteins, drives gamete fusion across several eukaryotic kingdoms. Gamete fusion is a highly controlled process in eukaryotes, and is allowed only between same species gametes. In spite of a conserved architecture, HAP2 displays several species-specific functional regions that were not resolved in the available X-ray structure of the green alga Chlamydomonas reinhardtii HAP2 ectodomain.
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