Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Functional rescue of a misfolded eukaryotic ATP-binding cassette transporter by domain replacement.

The Journal of biological chemistry - 12 Nov 2010

Louie Raymond J, Pagant Silvere, Youn Ji-Young, Halliday John J, Huyer Gregory, Michaelis Susan, Miller Elizabeth A

Abstract excerpt

ATP-binding cassette (ABC) transporters are integral membrane proteins that couple ATP binding/hydrolysis with the transport of hydrophilic substrates across lipid barriers. Deletion of Phe-670 in the first nucleotide-binding domain (NBD1) of the yeast ABC transporter, Yor1p, perturbs interdomain associations, reduces functionality, and hinders proper transport to the plasma membrane. Functionality of Yor1p-ΔF...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to ATP-Binding Cassette Transporters
Share to Endoplasmic Reticulum

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Eukaryotic Cells

Share to Green Fluorescent Proteins

Share to Immunoblotting

Share to Microscopy, Confocal

Share to Protein Folding

Share to Protein Transport

Source

Open in PubMed Open full text

Identifiers

PMID: 20843810
DOI: 10.1074/jbc.M110.160523
PMCID: PMC2975245

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Functional rescue of a misfolded eukaryotic ATP-binding cassette transporter by domain replacement.PMID 20843810Read ↗

Inhibiting endoplasmic reticulum (ER)-associated degradation of misfolded Yor1p does not permit ER export despite the presence of a diacidic sorting signal.Semantic proximity Read ↗

The primary folding defect and rescue of ΔF508 CFTR emerge during translation of the mutant domain.Semantic proximity Read ↗

The signaling interface of the yeast multidrug transporter Pdr5 adopts a cis conformation, and there are functional overlap and equivalence of the deviant and canonical Q-loop residues.Semantic proximity Read ↗

Identification of a NBD1-Binding Pharmacological Chaperone that Corrects the Trafficking Defect of F508del-CFTRSemantic proximity Read ↗

ABC Transporters in Saccharomyces cerevisiae and Their Interactors: New Technology Advances the Biology of the ABCC (MRP) SubfamilySemantic proximity Read ↗

A yeast phenomic model for the gene interaction network modulating CFTR-ΔF508 protein biogenesisSemantic proximity Read ↗

Pharmacological chaperones improve intra-domain stability and inter-domain assembly via distinct binding sites to rescue misfolded CFTR.Semantic proximity Read ↗

Correction of both NBD1 energetics and domain interface is required to restore ΔF508 CFTR folding and function.Semantic proximity Read ↗

Yeast cells reveal the misfolding and the cellular mislocalization of the human BRCA1 protein.Semantic proximity Read ↗

Requirement of the N-terminal extension for vacuolar trafficking and transport activity of yeast Ycf1p, an ATP-binding cassette transporter.Semantic proximity Read ↗

The yeast ATP-binding cassette (ABC) transporter Ycf1p enhances the recruitment of the soluble SNARE Vam7p to vacuoles for efficient membrane fusion.Semantic proximity Read ↗

Diminished self-chaperoning activity of the DeltaF508 mutant of CFTR results in protein misfolding.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.