bioRxiv Science⌕ Search

bioRxiv · 10.1101/320630

Full Rescue of F508del-CFTR Processing and Function by CFTR Modulators can be Achieved by Removal of Two Unique Regulatory Regions

Abstract

Background and Purpose: Cystic Fibrosis (CF) is caused by mutations in the CF Transmembrane conductance Regulator (CFTR), the only ABC transporter functioning as a channel. Unique to CFTR are two highly conformationally dynamic regions: the regulatory extension (RE) and regulatory insertion (RI). Removal of the latter rescues the trafficking defect of CFTR with F508del, the most common CF-causing mutation.\n\nWe aimed here to assess the impact of RE removal (alone or with RI or genetic revertants) on F508del-CFTR traffic and how CFTR modulator drugs corrector VX-809/lumacaftor and potentiator VX-770/ivacaftor rescue these combined variants so as to gain insight into the mechanism of action (MoA) of these drugs.\n\nExperimental Approach. We generated {triangleup}RE and {triangleup}RI CFTR variants (with and without genetic revertants) by site-directed mutagenesis and used them to stably transfect BHK cell lines. We studied CFTR expression and stability by Western blotting and pulse-chase respectively, plasma membrane levels by cell surface biotinylation and channel activity by the iodide efflux technique.\n\nKey Results. Our data demonstrate that {triangleup}RI significantly enhanced rescue of F508del-CFTR by VX-809. Thus, while the presence of the regulatory insertion seems to be precluding full rescue of F508del-CFTR processing by VX-809, this region appears essential to rescue its function by VX-770, thus suggesting some contradictory role in rescue of F508del-CFTR by these two modulators. Nevertheless, this negative impact of RI removal on VX-770-stimulated currents on F508del-CFTR can be compensated by deletion of the regulatory extension which also leads to the stabilization of this mutant. We thus propose that, despite both these regions being conformationally active, RI precludes F508del-CFTR processing while RE affects mostly its stability and channel opening.\n\nSupporting Information: Additional figures with supplementary data

Source connections

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Uliyakina, I., Da Paula, A. C., Afonso, S. C., Lobo, M. J., Felicio, V., Botelho, H. M., Farinha, C. M., Amaral, M. D.. 2018-05-11. Full Rescue of F508del-CFTR Processing and Function by CFTR Modulators can be Achieved by Removal of Two Unique Regulatory Regions. https://doi.org/10.1101/320630

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related preprints

Structure of influenza D virus NS1 reveals a novel Zn-binding site and ssRNA-binding activity

Influenza D virus (IDV) is an emerging pathogen associated with bovine respiratory disease and has potential for zoonotic transmission. Although nonstructural protein 1 (NS1) is a major virulence factor in influenza A and B viruses, the structure and function of IDV NS1 remain poorly defined. Here, we determined crystal structures of the IDV NS1 N-terminal RNA-binding domain (NTD) and C-terminal effector domain (CTD). The NTD retains the conserved homodimeric six-helix fold, whereas the CTD adopts a distinct architecture containing a novel Zn2+-binding site. IDV NS1 CTD preferentially binds single-stranded RNA, and mutagenesis identified lysine and arginine residues critical for this activity. Single-residue substitutions disrupting either the Zn2+-binding site or RNA-binding interface prevented recovery of infectious recombinant IDV. These findings reveal distinct structural and functional features of IDV NS1 and establish the importance of CTD integrity for viral replication. Conservation of key CTD residues in influenza C virus NS1 suggests shared structural features that distinguish influenza C and D virus NS1 proteins from their influenza A and B counterparts.

biochemistry↗

QC-espresso: Brewing quality in proteomics

Data-independent acquisition (DIA) proteomics has become a standard approach for high-throughput proteomics, with DIA-NN emerging as one of the most widely adopted data-analysis platforms. However, despite the detailed information available in DIA-NN output reports, proteomics researchers may lack a streamlined and reproducible approach for assessing acquisition quality, identification consistency, and quantitative reliability across experiments. QC-espresso addresses this need through an automated, report-centered quality-control workflow implemented in R and Quarto. The tool processes a DIA-NN report.parquet file together with the corresponding FASTA database and generates a structured HTML report containing plots, run-level statistics, and exportable summary tables. Application to three experimental datasets allowed the visualization of lower identification depth related to high contaminant content; a chromatographic transition accompanied by altered retention-time and peak-width behavior; and the co-occurrence of systematic mass-error bias with changes in precursor- and protein-level quantitative-quality metrics. QC-espresso can be executed directly in R or through a portable Windows distribution with a graphical launcher, with both modes using the same analytical modules and report-generation workflow. The resulting report provides a consistent record for local inspection and troubleshooting of quality-control metrics within individual DIA proteomics experiments. QC-espresso is freely available at https://github.com/lanfredig/QC-espresso_DIA.

biochemistry↗

Molecular crowding differentially regulates magnetic field-dependent fluorescence, recovery kinetics, and photostability of the magnetosensitive protein MagLOV2

Macromolecular crowding and solvent composition can alter protein conformation, diffusion, hydration, and cofactor photophysics, yet their influence on magnetically sensitive flavoproteins is poorly understood. We tested seven molecular environments in MagLOV2-overexpressing Escherichia coli lysate using a custom-built, high-intensity magnetofluorescence platform. Five-point concentration series of Dextran 70, Ficoll PM70, PEG6000, PEG3350, glycerol, ethylene glycol, and bovine serum albumin (BSA) were measured at 22 mT under continuous 6.12 W/cm2 blue-light excitation. Dextran 70, Ficoll PM70, and PEG6000 progressively attenuated the negative magnetic field effect (MFE), whereas PEG3350 shifted toward mild enhancement at higher concentrations. Glycerol and ethylene glycol enhanced the negative MFE despite producing the strongest slowing of recovery upon the field being switched off (OFF-recovery), while BSA modestly enhanced MFE and accelerated OFF-recovery. Across 105 treatment cuvettes, the change in MFE was not globally correlated with changes in the OFF-recovery time constant (r = -0.07, p = 0.449). The initial pre-field illumination period revealed a second phenotype: Dextran and Ficoll increased late fluorescence loss, whereas glycerol and BSA were photoprotective. Pre-field fluorescence loss correlated moderately with MFE change across the full dataset (r = 0.474, p = 3.28 x 10-7) but not consistently within crowder classes. These findings show that MagLOV2 spin-dependent magnetofluorescence is shaped by crowder chemistry, polymer size, solvent environment, recovery kinetics, and photostability rather than by a single generic crowding or viscosity mechanism.

biochemistry↗