Evidence map›Paper›PMID 21460224›Full record

ArticleThe Journal of biological chemistry2011

Post-transcriptional control of Na,K-ATPase activity and cell growth by a splice variant of FXYD2 protein with modified mRNA.

Kathleen J Sweadner, Jennifer L Pascoa, Cynthia A Salazar, Elena Arystarkhova

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 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.5field-weighted citation impact, top 35% 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

8 citing papers in PubMed, 10 citations in OpenAlex.

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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

4 authors at 2 institutions in 1 country.

Kathleen J SweadnerLaboratory of Membrane Biology, Department of Neurosurgery, Massachusetts General Hospital and Harvard Medical School, Boston, Massachusetts 02114, USA.
Jennifer L Pascoa
Cynthia A Salazar
Elena Arystarkhova
Massachusetts General Hospital · USHarvard University · US

Funding

STRUCTURE OF NA, K-ATPASE--MONOCLONAL ANTIBODY PROBESR01HL036271 · NHLBI · MASSACHUSETTS GENERAL HOSPITAL · PI SWEADNER, KATHLEEN J · 1987 to 2004
$1.7M
Cellular/molecular Na,K-ATPase regulation in choroid plexusR01NS050696 · NINDS · MASSACHUSETTS GENERAL HOSPITAL · PI SWEADNER, KATHLEEN J · 2007 to 2010
$1.4M
Novel Target for Ciliary Epithelium Transport RegulationR03EY014390 · NEI · MASSACHUSETTS GENERAL HOSPITAL · PI SWEADNER, KATHLEEN J · 2003 to 2005
$519k
New Modulators of Na, K-ATPase in the CNSR21NS045083 · NINDS · MASSACHUSETTS GENERAL HOSPITAL · PI SWEADNER, KATHLEEN J · 2003 to 2004
$411k
NEI NIH HHS R03 EY014390NHLBI NIH HHS HL036271NHLBI NIH HHS R01 HL036271NINDS NIH HHS NS045083NINDS NIH HHS NS050696NINDS NIH HHS R01 NS050696NINDS NIH HHS R21 NS045083
6 · The paper itself

Abstract

In kidney, FXYD proteins regulate Na,K-ATPase in a nephron segment-specific way. FXYD2 is the most abundant renal FXYD but is not expressed in most renal cell lines unless induced by hypertonicity. Expression by transfection of FXYD2a or FXYD2b splice variants in NRK-52E cells reduces the apparent Na(+) affinity of the Na,K-ATPase and slows the cell proliferation rate. Based on RT-PCR, mRNAs for both splice variants were expressed in wild type NRK-52E cells as low abundance species. DNA sequencing of the PCR products revealed a base alteration from C to T in FXYD2b but not FXYD2a from both untreated and hypertonicity-treated NRK-52E cells. The 172C→T sequence change exposed a cryptic KKXX endoplasmic reticulum retrieval signal via a premature stop codon. The truncation affected trafficking of FXYD2b and its association with Na,K-ATPase and blocked its effect on enzyme kinetics and cell growth. The data may be explained by altered splicing or selective RNA editing of FXYD2b, a supplementary process that would ensure that it was inactive even if transcribed and translated, in these cells that normally express only FXYD2a. 172C→T mutation was also identified after mutagenesis of FXYD2b by error-prone PCR coupled with a selection for cell proliferation. Furthermore, the error-prone PCR alone introduced the mutation with high frequency, implying a structural peculiarity. The data confirm truncation of FXYD2b as a potential mechanism to regulate the amount of FXYD2 at the cell surface to control activity of Na,K-ATPase and cell growth.

Indexed as

AnimalsCell Line, TumorEndoplasmic ReticulumIsoenzymesMutationProtein Sorting SignalsRatsRNA EditingRNA, MessengerSodium-Potassium-Exchanging ATPaseFxyd2 protein, ratIsoenzymesProtein Sorting SignalsRNA, MessengerSodium-Potassium-Exchanging ATPase

Identifiers

PMID21460224
PMCPMC3093901
OpenAlexW2031301918

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.