Evidence map›Paper›PMID 21173145›Full record

ArticleThe Journal of biological chemistry2011

ATP induces conformational changes in the carboxyl-terminal region of ClC-5.

Leigh Wellhauser, Cesar Luna-Chavez, Christina D'Antonio, John Tainer, Christine E Bear

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

15 citing papers in PubMed, 19 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Making a Dent in Dent Disease.Function (Oxford, England) · 2020
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Regulation of ClC-2 gating by intracellular ATP.Pflugers Archiv : European journal of physiology · 2013
    Article
  11. Article
  12. Article
  13. Article
  14. ClC-5 mutations associated with Dent's disease: a major role of the dimer interface.Pflugers Archiv : European journal of physiology · 2012
    Review
  15. 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

5 authors at 4 institutions in 2 countries.

Leigh WellhauserProgramme of Molecular Structure and Function, Research Institute, the Hospital for Sick Children, Toronto, Ontario M5G 1X8, Canada.
Cesar Luna-Chavez
Christina D'Antonio
John Tainer
Christine E Bear
University of Toronto · CAHospital for Sick Children · CALawrence Berkeley National Laboratory · USUniversity of California, Berkeley · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ATP binding enhances the activity of ClC-5, the transporter mutated in Dent disease, a disease affecting the renal proximal tubule. Previously, the ATP binding site was revealed in x-ray crystal structures of the cytoplasmic region of this membrane protein. Disruption of this site by mutagenesis (Y617A-ClC-5) reduced the functional expression and ATP-dependent regulation of the full-length transporter in Xenopus oocytes. However, insight into the conformational changes underlying ATP-dependent regulation is lacking. Here, we show that ATP binding induces a change in protein conformation. Specifically, small angle x-ray scattering experiments indicate that ATP binding promotes a clamp-like closure of the isolated ClC-5 carboxyl-terminal region. Limited proteolysis studies show that ATP binding induces conformational compaction of the carboxyl-terminal region in the intact membrane protein as well. In the context of fibroblasts and proximal tubule epithelial cells, disruption of the ATP binding site in full-length ClC-5 (Y617A-ClC-5) led to a defect in processing and trafficking out of the endoplasmic reticulum. These latter findings account for the decrease in functional expression previously reported for this ATP-binding mutant and prompt future study of a model whereby conformational compaction caused by ATP binding promotes biosynthetic maturation.

Indexed as

Adenosine TriphosphateAmino Acid SubstitutionAnimalsBinding SitesCHO CellsCricetinaeCricetulusDent DiseaseEndoplasmic ReticulumHumansMutagenesisMutation, MissenseOocytesPeptide MappingProtein Structure, TertiaryProtein TransportAdenosine TriphosphateCIC protein, humanRepressor Proteins

Identifiers

PMID21173145
PMCPMC3057859
OpenAlexW2047110768

What OpenQuestion holds

Textmetadata
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.