Evidence map›Paper›PMID 12686602›Full record

ArticleMolecular biology of the cell2003

Nestin promotes the phosphorylation-dependent disassembly of vimentin intermediate filaments during mitosis.

Ying-Hao Chou, Satya Khuon, Harald Herrmann, Robert D Goldman

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

79 citing papers in PubMed, 196 citations in OpenAlex.

  1. Article
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  4. Vimentin undergoes liquid-liquid phase separation to form droplets which wet and stabilize actin fibers.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Review
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  8. Distribution, contribution and regulation of nestinJournal of advanced research · 2024
    Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Vimentin and cytokeratin: Good alone, bad together.Seminars in cancer biology · 2022
    Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article

19 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

Ying-Hao ChouDepartment of Cell and Molecular Biology, Northwestern University, 303 East Chicago Avenue, Chicago, IL 60611, USA.
Satya Khuon
Harald Herrmann
Robert D Goldman
Northwestern University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The expression of the intermediate filament (IF) protein nestin is closely associated with rapidly proliferating progenitor cells during neurogenesis and myogenesis, but little is known about its function. In this study, we examine the effects of nestin expression on the assembly state of vimentin IFs in nestin-free cells. Nestin is introduced by transient transfection and is positively correlated with the disassembly of vimentin IFs into nonfilamentous aggregates or particles in mitotic but not interphase cells. This nestin-mediated disassembly of IFs is dependent on the phosphorylation of vimentin by the maturation/M-phase-promoting factor at ser-55 in the amino-terminal head domain. In addition, the disassembly of vimentin IFs during mitosis appears to be a unique feature of nestin-expressing cell types. Furthermore, when the expression of nestin is downregulated by the nestin-specific small interfering RNA in nestin-expressing cells, vimentin IFs remain assembled throughout all stages of mitosis. Previous studies suggest that nonfilamentous vimentin particles are IF precursors and can be transported rapidly between different cytoplasmic compartments along microtubule tracks. On the basis of these observations, we speculate that nestin may play a role in the trafficking and distribution of IF proteins and potentially other cellular factors to daughter cells during progenitor cell division.

Indexed as

Nerve Tissue ProteinsAnimalsBase SequenceCattleCell LineCricetinaeDown-RegulationHumansIntermediate Filament ProteinsIntermediate FilamentsMiceMitosisNestinPhosphorylationProtein Structure, TertiaryRatsIntermediate Filament ProteinsNerve Tissue ProteinsNES protein, humanNes protein, mouseNes protein, ratNestinRecombinant ProteinsVimentin

Identifiers

PMID12686602
PMCPMC153115
OpenAlexW2169603159

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.