ArticleScientific reports2015
Mutational Analysis of Intracellular Loops Identify Cross Talk with Nucleotide Binding Domains of Yeast ABC Transporter Cdr1p.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 38 citations in OpenAlex.
- Article
- Cdr1 in focus: a personal reflection on multidrug transporter research.FEMS yeast research · 2025Article
- Use of gain-of-function suppressor screening to elucidateFrontiers in microbiology · 2025Article
- Probing the allosteric NBD-TMD crosstalk in the ABC transporter MsbA by solid-state NMR.Communications biology · 2024Article
- Clorgyline Analogs Synergize with Azoles against Drug Efflux inJournal of fungi (Basel, Switzerland) · 2023Article
- Directed Mutational Strategies Reveal Drug Binding and Transport by the MDR Transporters ofJournal of fungi (Basel, Switzerland) · 2021Review
- FK506 Resistance ofAntimicrobial agents and chemotherapy · 2019Article
- Targeting efflux pumps to overcome antifungal drug resistance.Future medicinal chemistry · 2016Review
- Newly identified motifs in Candida albicans Cdr1 protein nucleotide binding domains are pleiotropic drug resistance subfamily-specific and functionally asymmetric.Scientific reports · 2016Article
- Mutations of charged amino acids at the cytoplasmic end of transmembrane helix 2 affect transport activity of the budding yeast multidrug resistance protein Pdr5p.FEMS yeast research · 2016Article
- A New Endogenous Overexpression System of Multidrug Transporters of Candida albicans Suitable for Structural and Functional Studies.Frontiers in microbiology · 2016Article
- The ABCs of Candida albicans Multidrug Transporter Cdr1.Eukaryotic cell · 2015Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ABC transporter Cdr1 protein (Cdr1p) of Candida albicans, which plays a major role in antifungal resistance, has two transmembrane domains (TMDs) and two nucleotide binding domains (NBDs) that are interconnected by extracellular (ECLs) and intracellular (ICLs) loops. To examine the communication interface between the NBDs and ICLs of Cdr1p, we subjected all four ICLs to alanine scanning mutagenesis, replacing each of the 85 residues with an alanine. The resulting ICL mutant library was analyzed by biochemical and phenotypic mapping. Only 18% of the mutants from this library displayed enhanced drug susceptibility. Most of the drug-susceptible mutants displayed uncoupling between ATP hydrolysis and drug transport. The two drug-susceptible ICL1 mutants (I574A and S593A) that lay within or close to the predicted coupling helix yielded two chromosomal suppressor mutations that fall near the Q-loop of NBD2 (R935) and in the Walker A motif (G190) of NBD1. Based on a 3D homology model and kinetic analysis of drug transport, our data suggest that large distances between ICL residues and their respective chromosomal suppressor mutations rule out a direct interaction between them. However, they impact the transport cycle by restoring the coupling interface via indirect downstream signaling.
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