Evidence map›Paper›PMID 2537316›Full record

ArticleThe Journal of cell biology1989

Ankyrin links fodrin to the alpha subunit of Na,K-ATPase in Madin-Darby canine kidney cells and in intact renal tubule cells.

J S Morrow, C D Cianci, T Ardito, A S Mann, M Kashgarian

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
17.2field-weighted citation impact, top 1% 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

74 citing papers in PubMed, 276 citations in OpenAlex.

  1. An animal-type NaFrontiers in plant science · 2025
    Article
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  3. Review
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  7. Trafficking to the apical and basolateral membranes in polarized epithelial cells.Journal of the American Society of Nephrology : JASN · 2014
    Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Cardiac ankyrins in health and disease.Journal of molecular and cellular cardiology · 2009
    Review
  15. Article
  16. Article
  17. Sodium pump localization in epithelia.Journal of bioenergetics and biomembranes · 2007
    Review
  18. Article
  19. Article
  20. Article

14 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

J S MorrowDepartment of Pathology, Yale University School of Medicine, New Haven, Connecticut 06510.
C D Cianci
T Ardito
A S Mann
M Kashgarian
Yale University · US

Funding

MEMBRANE SKELETAL CONTROL IN HEMOLYTIC DISORDERSR01HL028560 · NHLBI · YALE UNIVERSITY · PI MORROW, JON S · 1985 to 2011
$3.3M
STRUCTURE AND FUNCTION OF THE RENAL EPITHELIAL CELL MEMBRANE SKELETONP01DK038979 · NIDDK · YALE UNIVERSITY · PI MORROW, JON S · 1987 to 1998
–
NHLBI NIH HHS HL28560NIDDK NIH HHS DK38979
6 · The paper itself

Abstract

In nonerythroid cells the distribution of the cortical membrane skeleton composed of fodrin (spectrin), actin, and other proteins varies both temporally with cell development and spatially within the cell and on the membrane. In monolayers of Madin-Darby canine kidney (MDCK) cells, it has previously been shown that fodrin and Na,K-ATPase are codistributed asymmetrically at the basolateral margins of the cell, and that the distribution of fodrin appears to be regulated posttranslationally when confluence is achieved (Nelson, W. J., and P. I. Veshnock. 1987. J. Cell Biol. 104:1527-1537). The molecular mechanisms underlying these changes are poorly understood. We find that (a) in confluent MDCK cells and intact kidney proximal tubule cells, Na,K-ATPase, fodrin, and analogues of human erythrocyte ankyrin are precisely colocalized in the basolateral domain at the ultrastructural level. (b) This colocalization is only achieved in MDCK cells after confluence is attained. (c) Erythrocyte ankyrin binds saturably to Na,K-ATPase in a molar ratio of approximately 1 ankyrin to 4 Na,K-ATPase's, with a kD of 2.6 microM. (d) The binding of ankyrin to Na,K-ATPase is inhibited by the 43-kD cytoplasmic domain of erythrocyte band 3. (e) 125I-labeled ankyrin binds to the alpha subunit of Na,K-ATPase in vitro. There also appears to be a second minor membrane protein of approximately 240 kD that is associated with both erythrocyte and kidney membranes that binds 125I-labeled ankyrin avidly. The precise identity of this component is unknown. These results identify a molecular mechanism in the renal epithelial cell that may account for the polarized distribution of the fodrin-based cortical cytoskeleton.

Indexed as

AnimalsAnkyrinsBlood ProteinsCarrier ProteinsCell LineCell MembraneDogsEpitheliumErythrocyte MembraneHistocytochemistryHumansImmunoblottingImmunoenzyme TechniquesKidneyKidney TubulesMembrane ProteinsAnkyrinsBlood ProteinsCarrier ProteinsMembrane ProteinsMicrofilament ProteinsSodium-Potassium-Exchanging ATPaseSpectrin

Identifiers

PMID2537316
PMCPMC2115445
OpenAlexW2119483155

What OpenQuestion holds

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LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

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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.