Evidence map›Paper›PMID 12388758›Full record

ArticleMolecular biology of the cell2002

Subcellular recruitment of fibrillarin to nucleoplasmic proteasomes: implications for processing of a nucleolar autoantigen.

Min Chen, Thomas Rockel, Gabriele Steinweger, Peter Hemmerich, Jakob Risch, Anna von Mikecz

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

19 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
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  3. SUMO: A Swiss Army Knife for Eukaryotic Topoisomerases.Frontiers in molecular biosciences · 2022
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  7. Interferons, signal transduction pathways, and the central nervous system.Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research · 2014
    Review
  8. Article
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  10. Article
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  12. Article
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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

6 authors at 2 institutions in 1 country.

Min ChenJunior Research Group of Molecular Cell Biology, Institute of Environmental Health Research, Heinrich-Heine-University, Düsseldorf, Germany.
Thomas Rockel
Gabriele Steinweger
Peter Hemmerich
Jakob Risch
Anna von Mikecz
Heinrich Heine University Düsseldorf · DEInstitute of Molecular Biology · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A prerequisite for proteins to interact in a cell is that they are present in the same intracellular compartment. Although it is generally accepted that proteasomes occur in both, the cytoplasm and the nucleus, research has been focusing on cytoplasmic protein breakdown and antigen processing, respectively. Thus, little is known on the functional organization of the proteasome in the nucleus. Here we report that within the nucleus 20S and 26S proteasomes occur throughout the nucleoplasm and partially colocalize with splicing factor-containing speckles. Because proteasomes are absent from the nucleolus, a recruitment system was used to analyze the molecular fate of nucleolar protein fibrillarin: Subtoxic concentrations of mercuric chloride (HgCl(2)) induce subcellular redistribution of fibrillarin and substantial colocalization (33%) with nucleoplasmic proteasomes in different cell lines and in primary cells isolated from mercury-treated mice. Accumulation of fibrillarin and fibrillarin-ubiquitin conjugates in lactacystin-treated cells suggests that proteasome-dependent processing of this autoantigen occurs upon mercury induction. The latter observation might constitute the cell biological basis of autoimmune responses that specifically target fibrillarin in mercury-mouse models and scleroderma.

Indexed as

Antigen PresentationAcetylcysteineAnimalsAutoantigensCell LineCell NucleusChromosomal Proteins, Non-HistoneCysteine EndopeptidasesCysteine Proteinase InhibitorsDual-Specificity PhosphatasesFemaleHumansMercuric ChlorideMiceMultienzyme ComplexesPeptide HydrolasesAcetylcysteineATP dependent 26S proteaseAutoantigensChromosomal Proteins, Non-HistoneCysteine EndopeptidasesCysteine Proteinase InhibitorsDual-Specificity PhosphatasesDUSP5 protein, humanfibrillarinlactacystinMercuric ChlorideMultienzyme ComplexesPeptide Hydrolasesphosphoprotein C23PhosphoproteinsProteasome Endopeptidase ComplexProtein Tyrosine PhosphatasesUbiquitin

Identifiers

PMID12388758
PMCPMC129967
OpenAlexW2105010726

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.