Evidence map›Paper›PMID 24595027›Full record

ArticlePloS one2014

Nucleolin regulates phosphorylation and nuclear export of fibroblast growth factor 1 (FGF1).

Torunn Sletten, Michal Kostas, Joanna Bober, Vigdis Sorensen, Mandana Yadollahi, Sjur Olsnes, Justyna Tomala, Jacek Otlewski, Malgorzata Zakrzewska, Antoni Wiedlocha

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

13 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. Targeting the Hippo pathway in Schwann cells ameliorates peripheral nerve degeneration via a polypharmacological mechanism.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2024
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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

10 authors at 3 institutions in 2 countries.

Torunn SlettenDepartment of Biochemistry, Institute for Cancer Research, The Norwegian Radium Hospital, Oslo University Hospital, Oslo, Norway; Centre for Cancer Biomedicine, Faculty of Medicine, University of Oslo, Norway.
Michal KostasDepartment of Protein Biotechnology, Faculty of Biotechnology, University of Wroclaw, Wroclaw, Poland.
Joanna BoberDepartment of Protein Engineering, Faculty of Biotechnology, University of Wroclaw, Wroclaw, Poland.
Vigdis SorensenDepartment of Biochemistry, Institute for Cancer Research, The Norwegian Radium Hospital, Oslo University Hospital, Oslo, Norway; Centre for Cancer Biomedicine, Faculty of Medicine, University of Oslo, Norway.
Mandana YadollahiDepartment of Biochemistry, Institute for Cancer Research, The Norwegian Radium Hospital, Oslo University Hospital, Oslo, Norway; Centre for Cancer Biomedicine, Faculty of Medicine, University of Oslo, Norway.
Sjur OlsnesDepartment of Biochemistry, Institute for Cancer Research, The Norwegian Radium Hospital, Oslo University Hospital, Oslo, Norway; Centre for Cancer Biomedicine, Faculty of Medicine, University of Oslo, Norway.
Justyna TomalaDepartment of Protein Biotechnology, Faculty of Biotechnology, University of Wroclaw, Wroclaw, Poland.
Jacek OtlewskiDepartment of Protein Engineering, Faculty of Biotechnology, University of Wroclaw, Wroclaw, Poland.
Malgorzata ZakrzewskaDepartment of Protein Engineering, Faculty of Biotechnology, University of Wroclaw, Wroclaw, Poland.
Antoni WiedlochaDepartment of Biochemistry, Institute for Cancer Research, The Norwegian Radium Hospital, Oslo University Hospital, Oslo, Norway; Centre for Cancer Biomedicine, Faculty of Medicine, University of Oslo, Norway.
University of Wrocław · PLOslo University Hospital · NOUniversity of Oslo · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Extracellular fibroblast growth factor 1 (FGF1) acts through cell surface tyrosine kinase receptors, but FGF1 can also act directly in the cell nucleus, as a result of nuclear import of endogenously produced, non-secreted FGF1 or by transport of extracellular FGF1 via endosomes and cytosol into the nucleus. In the nucleus, FGF1 can be phosphorylated by protein kinase C δ (PKCδ), and this event induces nuclear export of FGF1. To identify intracellular targets of FGF1 we performed affinity pull-down assays and identified nucleolin, a nuclear multifunctional protein, as an interaction partner of FGF1. We confirmed a direct nucleolin-FGF1 interaction by surface plasmon resonance and identified residues of FGF1 involved in the binding to be located within the heparin binding site. To assess the biological role of the nucleolin-FGF1 interaction, we studied the intracellular trafficking of FGF1. In nucleolin depleted cells, exogenous FGF1 was endocytosed and translocated to the cytosol and nucleus, but FGF1 was not phosphorylated by PKCδ or exported from the nucleus. Using FGF1 mutants with reduced binding to nucleolin and a FGF1-phosphomimetic mutant, we showed that the nucleolin-FGF1 interaction is critical for the intranuclear phosphorylation of FGF1 by PKCδ and thereby the regulation of nuclear export of FGF1.

Indexed as

Active Transport, Cell NucleusAnimalsCell LineCell NucleusFibroblast Growth Factor 1Fibroblast Growth Factor 2HEK293 CellsHumansMiceNIH 3T3 CellsNucleolinPhosphoproteinsPhosphorylationRNA-Binding ProteinsFibroblast Growth Factor 1Fibroblast Growth Factor 2NucleolinPhosphoproteinsRNA-Binding Proteins

Identifiers

PMID24595027
PMCPMC3942467
OpenAlexW2016950581

What OpenQuestion holds

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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.