Evidence map›Paper›PMID 12724421›Full record

ArticleMolecular and cellular biology2003

Nonmuscle myosin promotes cytoplasmic localization of PBX.

He Huang, Miltiadis Paliouras, Isabel Rambaldi, Paul Lasko, Mark Featherstone

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

20 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Research progress of PBX1 in developmental and regenerative medicine.International journal of medical sciences · 2023
    Review
  3. The regulation of PBXs and their emerging role in cancer.Journal of cellular and molecular medicine · 2022
    Review
  4. Review
  5. Article
  6. Article
  7. Biochemistry of the tale transcription factors PREP, MEIS, and PBX in vertebrates.Developmental dynamics : an official publication of the American Association of Anatomists · 2014
    Review
  8. Hox regulation of transcription: more complex(es).Developmental dynamics : an official publication of the American Association of Anatomists · 2014
    Review
  9. Review
  10. Article
  11. Hox specificity unique roles for cofactors and collaborators.Current topics in developmental biology · 2009
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. The protein ENH is a cytoplasmic sequestration factor for Id2 in normal and tumor cells from the nervous system.Proceedings of the National Academy of Sciences of the United States of America · 2006
    Article
  19. 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

5 authors at 1 institution in 1 country.

He HuangMcGill Cancer Centre, Division of Experimental Medicine, Department of Medicine, McGill University, Montréal, Québec, Canada H3G 1Y6.
Miltiadis Paliouras
Isabel Rambaldi
Paul Lasko
Mark Featherstone
McGill University Health Centre · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the absence of MEIS family proteins, two mechanisms are known to restrict the PBX family of homeodomain (HD) transcription factors to the cytoplasm. First, PBX is actively exported from the nucleus via a CRM1-dependent pathway. Second, nuclear localization signals (NLSs) within the PBX HD are masked by intramolecular contacts. In a screen to identify additional proteins directing PBX subcellular localization, we identified a fragment of murine nonmuscle myosin II heavy chain B (NMHCB). The interaction of NMHCB with PBX was verified by coimmunoprecipitation, and immunofluorescence staining revealed colocalization of NMHCB with cytoplasmic PBX in the mouse embryo distal limb bud. The interaction domain in PBX mapped to a conserved PBC-B region harboring a potential coiled-coil structure. In support of the cytoplasmic retention function, the NMHCB fragment competes with MEIS1A to redirect PBX, and the fly PBX homologue EXD, to the cytoplasm of mammalian and insect cells. Interestingly, MEIS1A also localizes to the cytoplasm in the presence of the NMHCB fragment. These activities are largely independent of nuclear export. We show further that the subcellular localization of EXD is deregulated in Drosophila zipper mutants that are depleted of nonmuscle myosin heavy chain. This study reveals a novel and evolutionarily conserved mechanism controlling the subcellular distribution of PBX and EXD proteins.

Indexed as

AnimalsCell LineCOS CellsCytoplasmDNA-Binding ProteinsDrosophilaExtremitiesGenetic VectorsHumansMiceMicroscopy, FluorescenceModels, GeneticMyosinsNonmuscle Myosin Type IIBPre-B-Cell Leukemia Transcription Factor 1Precipitin TestsDNA-Binding ProteinsMyosinsNonmuscle Myosin Type IIBPBX1 protein, humanPre-B-Cell Leukemia Transcription Factor 1Proto-Oncogene Proteins

Identifiers

PMID12724421
PMCPMC164772
OpenAlexW2152539820

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.