Evidence map›Paper›PMID 25561737›Full record

ArticleThe Journal of biological chemistry2015

Analysis of the binding moiety mediating the interaction between monocarboxylate transporters and carbonic anhydrase II.

Sina Ibne Noor, Steffen Dietz, Hella Heidtmann, Christopher D Boone, Robert McKenna, Joachim W Deitmer, Holger M Becker

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

21 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Acid affairs in anti-tumour immunity.Cancer cell international · 2024
    Review
  3. Review
  4. Role of pH Regulatory Proteins and Dysregulation of pH in Prostate Cancer.Reviews of physiology, biochemistry and pharmacology · 2022
    Article
  5. Proton Transport in Cancer Cells: The Role of Carbonic Anhydrases.International journal of molecular sciences · 2021
    Review
  6. Review
  7. Heteromeric Solute Carriers: Function, Structure, Pathology and Pharmacology.Advances in experimental medicine and biology · 2021
    Review
  8. Article
  9. Review
  10. Review
  11. Article
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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

7 authors at 2 institutions in 2 countries.

Sina Ibne NoorFrom the Department of Biology, Division of Zoology/Membrane Transport and.
Steffen DietzFrom the Department of Biology, Division of Zoology/Membrane Transport and.
Hella HeidtmannFrom the Department of Biology, Division of Zoology/Membrane Transport and the Department of Biology, Division of General Zoology, University of Kaiserslautern, D-67653 Kaiserslautern, Germany and.
Christopher D Boonethe Department of Biochemistry and Molecular Biology, University of Florida, Gainesville, Florida 32610.
Robert McKennathe Department of Biochemistry and Molecular Biology, University of Florida, Gainesville, Florida 32610.
Joachim W Deitmerthe Department of Biology, Division of General Zoology, University of Kaiserslautern, D-67653 Kaiserslautern, Germany and.
Holger M BeckerFrom the Department of Biology, Division of Zoology/Membrane Transport and h.becker@biologie.uni-kl.de.
University of Florida · USUniversity of Kaiserslautern · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proton-coupled monocarboxylate transporters (MCTs) mediate the exchange of high energy metabolites like lactate between different cells and tissues. We have reported previously that carbonic anhydrase II augments transport activity of MCT1 and MCT4 by a noncatalytic mechanism, while leaving transport activity of MCT2 unaltered. In the present study, we combined electrophysiological measurements in Xenopus oocytes and pulldown experiments to analyze the direct interaction between carbonic anhydrase II (CAII) and MCT1, MCT2, and MCT4, respectively. Transport activity of MCT2-WT, which lacks a putative CAII-binding site, is not augmented by CAII. However, introduction of a CAII-binding site into the C terminus of MCT2 resulted in CAII-mediated facilitation of MCT2 transport activity. Interestingly, introduction of three glutamic acid residues alone was not sufficient to establish a direct interaction between MCT2 and CAII, but the cluster had to be arranged in a fashion that allowed access to the binding moiety in CAII. We further demonstrate that functional interaction between MCT4 and CAII requires direct binding of the enzyme to the acidic cluster (431)EEE in the C terminus of MCT4 in a similar fashion as previously shown for binding of CAII to the cluster (489)EEE in the C terminus of MCT1. In CAII, binding to MCT1 and MCT4 is mediated by a histidine residue at position 64. Taken together, our results suggest that facilitation of MCT transport activity by CAII requires direct binding between histidine 64 in CAII and a cluster of glutamic acid residues in the C terminus of the transporter that has to be positioned in surroundings that allow access to CAII.

Indexed as

Amino Acid SequenceAnimalsBinding SitesBiological TransportCarbonic Anhydrase IIElectrophysiologyHumansHydrogen-Ion ConcentrationMolecular Sequence DataMonocarboxylic Acid TransportersMutagenesis, Site-DirectedMutationOocytesProtein BindingProtein IsoformsRatsCarbonic Anhydrase IIMonocarboxylic Acid TransportersProtein IsoformsIon-sensitive ElectrodeLactic AcidpH RegulationProtein ComplexProtein ExpressionProton TransportXenopus

Identifiers

PMID25561737
PMCPMC4326851
OpenAlexW2009523653

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.