Evidence map›Paper›PMID 15883195›Full record

ArticleThe Journal of cell biology2005

Promotion of importin alpha-mediated nuclear import by the phosphorylation-dependent binding of cargo protein to 14-3-3.

Christian Faul, Stefan Hüttelmaier, Jun Oh, Virginie Hachet, Robert H Singer, Peter Mundel

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

32 citing papers in PubMed, 50 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Synaptopodin-2: a potential tumor suppressor.Cancer cell international · 2023
    Review
  5. Podocytes and the quest for precision medicines for kidney diseases.Pflugers Archiv : European journal of physiology · 2017
    Review
  6. Myopodin methylation is a prognostic biomarker and predicts antiangiogenic response in advanced kidney cancer.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Diagnostic and prognostic utility of methylation and protein expression patterns of myopodin in colon cancer.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2012
    Article
  12. Article
  13. Article
  14. Article
  15. FGF23 induces left ventricular hypertrophy.The Journal of clinical investigation · 2011
    Article
  16. Article
  17. Cardiac Z-disc signaling network.The Journal of biological chemistry · 2011
    Review
  18. Review
  19. 14-3-3zeta escorts CCTalpha for calcium-activated nuclear import in lung epithelia.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2010
    Article
  20. 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

6 authors at 3 institutions in 2 countries.

Christian FaulDepartment of Medicine, Albert Einstein College of Medicine, Bronx, NY 10461, USA.
Stefan Hüttelmaier
Jun Oh
Virginie Hachet
Robert H Singer
Peter Mundel
Albert Einstein College of Medicine · USIcahn School of Medicine at Mount Sinai · USEuropean Molecular Biology Laboratory · DE

Funding

Role of B7-1 in Podocytes in Pathogenesis of ProteinuriaR01DK062472 · NIDDK · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI SOBERMAN, ROY · 2004 to 2017
$5.3M
CELL AND MOLECULAR BIOLOGICAL ANALYSIS OF SYNAPTOPODINR01DK057683 · NIDDK · YESHIVA UNIVERSITY · PI SOBERMAN, ROY · 2001 to 2015
$4.8M
MECHANISM OF ACTIN MRNA LOCALIZATIONR01AR041480 · NIAMS · YESHIVA UNIVERSITY · PI SINGER, ROBERT H · 1992 to 2007
$2.3M
SYNAPTOPODIN: BIOGENESIS &PLASTICITY OF SPINE APPARATUSR01DA018886 · NIDA · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI MUNDEL, PETER H · 2004 to 2008
$1.8M
NIAMS NIH HHS AR41480NIAMS NIH HHS R01 AR041480NIDA NIH HHS DA18886NIDA NIH HHS R01 DA018886NIDDK NIH HHS DK062472NIDDK NIH HHS DK57683NIDDK NIH HHS R01 DK057683NIDDK NIH HHS R01 DK062472
6 · The paper itself

Abstract

14-3-3 proteins are phosphoserine/threonine-binding proteins that play important roles in many regulatory processes, including intracellular protein targeting. 14-3-3 proteins can anchor target proteins in the cytoplasm and in the nucleus or can mediate their nuclear export. So far, no role for 14-3-3 in mediating nuclear import has been described. There is also mounting evidence that nuclear import is regulated by the phosphorylation of cargo proteins, but the underlying mechanism remains elusive. Myopodin is a dual-compartment, actin-bundling protein that functions as a tumor suppressor in human bladder cancer. In muscle cells, myopodin redistributes between the nucleus and the cytoplasm in a differentiation-dependent and stress-induced fashion. We show that importin alpha binding and the subsequent nuclear import of myopodin are regulated by the serine/threonine phosphorylation-dependent binding of myopodin to 14-3-3. These results establish a novel paradigm for the promotion of nuclear import by 14-3-3 binding. They provide a molecular explanation for the phosphorylation-dependent nuclear import of nuclear localization signal-containing cargo proteins.

Indexed as

14-3-3 ProteinsActive Transport, Cell Nucleusalpha KaryopherinsAmino Acid SubstitutionAnimalsCell LineCell NucleusHumansMiceMicrofilament ProteinsModels, BiologicalMutationMyoblastsPhosphorylationProtein BindingProtein Structure, Tertiary14-3-3 Proteinsalpha KaryopherinsMicrofilament ProteinsSYNPO2 protein, humanSynpo2 protein, mouse

Identifiers

PMID15883195
PMCPMC2171942
OpenAlexW2047708528

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.