Evidence map›Paper›PMID 20663896›Full record

ArticleThe Journal of biological chemistry2010

Apical scaffolding protein NHERF2 modulates the localization of alternatively spliced plasma membrane Ca2+ pump 2B variants in polarized epithelial cells.

Rita Padányi, Yuning Xiong, Géza Antalffy, Krisztina Lór, Katalin Pászty, Emanuel E Strehler, Agnes Enyedi

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

18 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. The Whitish Inner Mantle of the Giant Clam,Frontiers in physiology · 2017
    Article
  7. PMCA2 regulates HER2 protein kinase localization and signaling and promotes HER2-mediated breast cancer.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Plasma membrane calcium ATPases as novel candidates for therapeutic agent development.Journal of pharmacy & pharmaceutical sciences : a publication of the Canadian Society for Pharmaceutical Sciences, Societe canadienne des sciences pharmaceutiques · 2013
    Review
  15. Article
  16. Article
  17. Apical localization of PMCA2w/b is enhanced in terminally polarized MDCK cells.Biochemical and biophysical research communications · 2011
    Article
  18. Emanuel Strehler's work on calcium pumps and calcium signaling.World journal of biological chemistry · 2011
    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

7 authors at 3 institutions in 2 countries.

Rita PadányiDepartment of Molecular Cell Biology, National Blood Center, H-1113 Budapest, Hungary.
Yuning Xiong
Géza Antalffy
Krisztina Lór
Katalin Pászty
Emanuel E Strehler
Agnes Enyedi
Hungarian National Blood Transfusion Service · HUMayo Clinic · USHungarian Academy of Sciences · HU

Funding

PILOT AND FEASIBILTY PROGRAMP30DK084567 · NIDDK · MAYO CLINIC ROCHESTER · PI Nicholas F. LaRusso · 2009 to 2026
$22.2M
Membrane Targeting of Calcium-Pumping ATPaseR01NS051769 · NINDS · MAYO CLINIC ROCHESTER · PI STREHLER, EMANUEL ERNST · 2007 to 2010
$1.4M
NIDDK NIH HHS P30 DK084567NINDS NIH HHS NS51769NINDS NIH HHS R01 NS051769
6 · The paper itself

Abstract

The membrane localization of the plasma membrane Ca(2+)-ATPase isoform 2 (PMCA2) in polarized cells is determined by alternative splicing; the PMCA2w/b splice variant shows apical localization, whereas the PMCA2z/b and PMCA2x/b variants are mostly basolateral. We previously reported that PMCA2b interacts with the PDZ protein Na(+)/H(+) exchanger regulatory factor 2 (NHERF2), but the role of this interaction for the specific membrane localization of PMCA2 is not known. Here we show that co-expression of NHERF2 greatly enhanced the apical localization of GFP-tagged PMCA2w/b in polarized Madin-Darby canine kidney cells. GFP-PMCA2z/b was also redirected to the apical membrane by NHERF2, whereas GFP-PMCA2x/b remained exclusively basolateral. In the presence of NHERF2, GFP-PMCA2w/b co-localized with the actin-binding protein ezrin even after disruption of the actin cytoskeleton by cytochalasin D or latrunculin B. Surface biotinylation and fluorescence recovery after photobleaching experiments demonstrated that NHERF2-mediated anchorage to the actin cytoskeleton reduced internalization and lateral mobility of the pump. Our results show that the specific interaction with NHERF2 enhances the apical concentration of PMCA2w/b by anchoring the pump to the apical membrane cytoskeleton. The data also suggest that the x/b splice form of PMCA2 contains a dominant lateral targeting signal, whereas the targeting and localization of the z/b form are more flexible and not fully determined by intrinsic sequence features.

Indexed as

ActinsAlternative SplicingAnimalsBridged Bicyclo Compounds, HeterocyclicCell MembraneCell PolarityCytochalasin DCytoskeletal ProteinsCytoskeletonDogsEpithelial CellsEzrinHeLa CellsHumansIsoenzymesNucleic Acid Synthesis InhibitorsActinsATP2B2 protein, humanBridged Bicyclo Compounds, HeterocyclicCytochalasin DCytoskeletal ProteinsEzrinIsoenzymeslatrunculin BNucleic Acid Synthesis InhibitorsPhosphoproteinsPlasma Membrane Calcium-Transporting ATPasessodium-hydrogen exchanger regulatory factorSodium-Hydrogen ExchangersThiazolidines

Identifiers

PMID20663896
PMCPMC2951242
OpenAlexW1966949599

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.