Evidence map›Paper›PMID 22042986›Full record

ArticleThe Journal of general physiology2011

Structural basis for the channel function of a degraded ABC transporter, CFTR (ABCC7).

Yonghong Bai, Min Li, Tzyh-Chang Hwang

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
6.7field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

39 citing papers in PubMed, 66 citations in OpenAlex.

  1. Review
  2. Structural identification of a selectivity filter in CFTR.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Structural mechanisms of CFTR function and dysfunction.The Journal of general physiology · 2018
    Review
  13. Article
  14. Molecular modelling and molecular dynamics of CFTR.Cellular and molecular life sciences : CMLS · 2017
    Review
  15. Architecture and functional properties of the CFTR channel pore.Cellular and molecular life sciences : CMLS · 2017
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 2 countries.

Yonghong BaiDalton Cardiovascular Research Center, University of Missouri-Columbia, Columbia, MO 65211, USA.
Min Li
Tzyh-Chang Hwang
Cardiovascular Research Center · BRUniversity of Missouri · US

Funding

MOLECULAR PATHOPHYSIOLOGY OF CYSTIC FIBROSISR01DK055835 · NIDDK · UNIVERSITY OF MISSOURI-COLUMBIA · PI HWANG, TZYH-CHANG · 1999 to 2022
$6.1M
GATING OF CFTR CL CHANNELS BY ATP HYDROLYSISR01HL053445 · NHLBI · UNIVERSITY OF MISSOURI-COLUMBIA · PI HWANG, TZYH-CHANG · 2001 to 2009
$2.3M
NHLBI NIH HHS R01 HL053445NHLBI NIH HHS R01HL53445NIDDK NIH HHS R01 DK055835NIDDK NIH HHS R01DK55835
6 · The paper itself

Abstract

Cystic fibrosis transmembrane conductance regulator (CFTR) is a member of the ATP-binding cassette (ABC) transporter superfamily, but little is known about how this ion channel that harbors an uninterrupted ion permeation pathway evolves from a transporter that works by alternately exposing its substrate conduit to the two sides of the membrane. Here, we assessed reactivity of intracellularly applied thiol-specific probes with cysteine residues substituted into the 12th transmembrane segment (TM12) of CFTR. Our experimental data showing high reaction rates of substituted cysteines toward the probes, strong blocker protection of cysteines against reaction, and reaction-induced alterations in channel conductance support the idea that TM12 of CFTR contributes to the lining of the ion permeation pathway. Together with previous work, these findings raise the possibility that pore-lining elements of CFTR involve structural components resembling those that form the substrate translocation pathway of ABC transporters. In addition, comparison of reaction rates in the open and closed states of the CFTR channel leads us to propose that upon channel opening, the wide cytoplasmic vestibule tightens and the pore-lining TM12 rotates along its helical axis. This simple model for gating conformational changes in the inner pore domain of CFTR argues that the gating transition of CFTR and the transport cycle of ABC proteins share analogous conformational changes. Collectively, our data corroborate the popular hypothesis that degradation of the cytoplasmic-side gate turned an ABC transporter into the CFTR channel.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionAnimalsCatalytic DomainCHO CellsCricetinaeCystic Fibrosis Transmembrane Conductance RegulatorMesylatesModels, MolecularProtein BindingProtein ConformationProtein Structure, TertiarySulfhydryl Compounds(2-sulfonatoethyl)methanethiosulfonateCystic Fibrosis Transmembrane Conductance RegulatorMesylatesmethanethiosulfonateSulfhydryl Compounds

Identifiers

PMID22042986
PMCPMC3206304
OpenAlexW2109202316

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.