Evidence map›Paper›PMID 25723258›Full record

ArticleNucleus (Austin, Tex.)2015

The tumor suppressor SHIP1 colocalizes in nucleolar cavities with p53 and components of PML nuclear bodies.

Patrick Ehm, Marcus M Nalaskowski, Torsten Wundenberg, Manfred Jücker

Open access · goldAbstract read
In one paragraph

Article in Nucleus (Austin, Tex.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

14 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. When PIPFrontiers in cell and developmental biology · 2022
    Review
  8. Review
  9. Article
  10. Review
  11. The nuclear phosphoinositide response to stress.Cell cycle (Georgetown, Tex.) · 2020
    Review
  12. The nucleolus, an ally, and an enemy of cancer cells.Histochemistry and cell biology · 2018
    Review
  13. Article
  14. Review
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.

Patrick Ehma Institute of Biochemistry and Signal Transduction ; University Medical Center Hamburg-Eppendorf ; Hamburg , Germany.
Marcus M Nalaskowski
Torsten Wundenberg
Manfred Jücker
University Medical Center Hamburg-Eppendorf · DEUniversität Hamburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The inositol 5-phosphatase SHIP1 is a negative regulator of signaling processes in haematopoietic cells. By converting PI(3,4,5)P3 to PtdIns(3,4)P2 at the plasma membrane, SHIP1 modifies PI3-kinase mediated signaling. We have recently demonstrated that SHIP1 is a nucleo-cytoplasmic shuttling protein and SHIP1 nuclear puncta partially colocalize with FLASH, a component of nuclear bodies. In this study, we demonstrate that endogenous SHIP1 localizes to intranucleolar regions of both normal and leukemic haematopoietic cells. In addition, we report that ectopically expressed SHIP1 accumulates in nucleolar cavities and colocalizes with the tumor suppressor protein p53 and components of PML nuclear bodies (e.g. SP100, SUMO-1 and CK2). Moreover, SHIP1 also colocalizes in nucleolar cavities with components of the ubiquitin-proteasome pathway. By using confocal microscopy data, we generated 3D-models revealing the enormous extent of the SHIP1 aggresomes in the nucleolus. Furthermore, treatment of cells with the proteasome inhibitor MG132 causes an enlargement of nucleolar SHIP1 containing structures. Unexpectedly, this accumulation can be partially prevented by treatment with the inhibitor of nuclear protein export Leptomycin B. In recent years, several proteins aggregating in nucleolar cavities were shown to be key factors of neurodegenerative diseases and cancerogenesis. Our findings support current relevance of nuclear localized SHIP1.

Indexed as

AnimalsCarcinogenesisCell LineCell NucleolusGreen Fluorescent ProteinsHematopoiesisHumansImaging, Three-DimensionalInositol Polyphosphate 5-PhosphatasesIntranuclear Inclusion BodiesMicePhosphatidylinositol-3,4,5-Trisphosphate 5-PhosphatasesPhosphoric Monoester HydrolasesProteasome Endopeptidase ComplexProtein TransportTumor Suppressor Protein p53enhanced green fluorescent proteinGreen Fluorescent ProteinsInositol Polyphosphate 5-PhosphatasesINPP5D protein, humanInpp5d protein, mousePhosphatidylinositol-3,4,5-Trisphosphate 5-PhosphatasesPhosphoric Monoester HydrolasesProteasome Endopeptidase ComplexTumor Suppressor Protein p53aggresomecancerDFC, dense fibrillar componentDIC, Differential interference contrastEGFP, enhanced green fluorescent proteinFC, fibrillar centerGC, granular componentleptomycin BLMB, leptomycin BMG132NES, nuclear export signalnucleolar cavitiesnucleusp53PBMC, Peripheral Blood Mononuclear CellPML bodiesPML, Promyelocytic LeukemiaPtdIns(3, 4, 5)P3, phosphatidylinositol-(3, 4, 5)-trisphosphatePtdIns(3, 4)P2, phosphatidylinositol-(3, 4)-bisphosphateRNA pol, RNA polymeraseSHIP1SHIP1, src homology 2 domain-containing inositol phosphatase 1ubiquitin proteasome pathwayUPP, ubiquitin-proteasome pathway.

Identifiers

PMID25723258
PMCPMC4615814
OpenAlexW1580351058

What Socratic 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 Socratic graph.