Evidence map›Paper›PMID 24121512›Full record

ArticleThe Journal of biological chemistry2013

A substrate access tunnel in the cytosolic domain is not an essential feature of the solute carrier 4 (SLC4) family of bicarbonate transporters.

Volodymyr Shnitsar, Jing Li, Xuyao Li, Charles Calmettes, Arghya Basu, Joseph R Casey, Trevor F Moraes, Reinhart A F Reithmeier

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed, 1 pooled it
2.7field-weighted citation impact, top 10% 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, 1 synthesis or guideline pooled it, 39 citations in OpenAlex.

  1. Pooled it
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  8. Review
  9. Activation of the Ae4 (Slc4a9) cation-driven ClAmerican journal of physiology. Gastrointestinal and liver physiology · 2021
    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

8 authors at 2 institutions in 1 country.

Volodymyr ShnitsarDepartment of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada.
Jing LiDepartment of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada.
Xuyao LiDepartment of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada.
Charles CalmettesDepartment of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada.
Arghya BasuDepartment of Biochemistry and Membrane Protein Disease Research Group, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.
Joseph R CaseyDepartment of Biochemistry and Membrane Protein Disease Research Group, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.
Trevor F MoraesDepartment of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada.
Reinhart A F ReithmeierDepartment of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada. Electronic address: r.reithmeier@utoronto.ca.
University of Toronto · CAUniversity of Alberta · CA

Funding

Y-FAMILY POLYMERASES AND CO-FACTORS IN TRANSLESION REPLICATIONP41RR015301 · NCRR · CORNELL UNIVERSITY ITHACA · PI EISENBERG, DAVID · 2001 to 2011
$28.2M
CIHR MOP102493CIHR MOP115182CIHR MOP13388NCRR NIH HHS P41 RR015301NCRR NIH HHS RR-15301
6 · The paper itself

Abstract

Anion exchanger 1 (AE1; Band 3; SLC4A1) is the founding member of the solute carrier 4 (SLC4) family of bicarbonate transporters that includes chloride/bicarbonate AEs and Na(+)-bicarbonate co-transporters (NBCs). These membrane proteins consist of an amino-terminal cytosolic domain involved in protein interactions and a carboxyl-terminal membrane domain that carries out the transport function. Mutation of a conserved arginine residue (R298S) in the cytosolic domain of NBCe1 (SLC4A4) is linked to proximal renal tubular acidosis and results in impaired transport function, suggesting that the cytosolic domain plays a role in substrate permeation. Introduction of single and double mutations at the equivalent arginine (Arg(283)) and at an interacting glutamate (Glu(85)) in the cytosolic domain of human AE1 (cdAE1) had no effect on the cell surface expression or the transport activity of AE1 expressed in HEK-293 cells. In addition, the membrane domain of AE1 (mdAE1) efficiently mediated anion transport. A 2.1-Å resolution crystal structure of cdΔ54AE1 (residues 55-356 of cdAE1) lacking the amino-terminal and carboxyl-terminal disordered regions, produced at physiological pH, revealed an extensive hydrogen-bonded network involving Arg(283) and Glu(85). Mutations at these residues affected the pH-dependent conformational changes and stability of cdΔ54AE1. As these structural alterations did not impair functional expression of AE1, the cytosolic and membrane domains operate independently. A substrate access tunnel within the cytosolic domain is not present in AE1 and therefore is not an essential feature of the SLC4 family of bicarbonate transporters.

Indexed as

Amino Acid SubstitutionAnion Exchange Protein 1, ErythrocyteCrystallography, X-RayGene Expression RegulationHEK293 CellsHumansHydrogen-Ion ConcentrationIon TransportMutation, MissenseProtein Structure, TertiarySodium-Bicarbonate SymportersAnion Exchange Protein 1, ErythrocyteSLC4A1 protein, humanSLC4A4 protein, humanSodium-Bicarbonate SymportersAnion Exchanger 1 (AE1)Anion TransportBand 3Membrane ProteinsProtein FoldingSite-directed MutagenesisSLC4TraffickingTransportersX-ray Crystallography

Identifiers

PMID24121512
PMCPMC3837127
OpenAlexW1995306114

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.