Evidence map›Paper›PMID 21486941›Full record

ArticleJournal of cell science2011

Structural protein 4.1R is integrally involved in nuclear envelope protein localization, centrosome-nucleus association and transcriptional signaling.

Adam J Meyer, Donna K Almendrala, Minjoung M Go, Sharon Wald Krauss

Abstract read
In one paragraph

Article in Journal of cell science, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed, 28 citations in OpenAlex.

  1. The role of inner nuclear membrane protein emerin in myogenesis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2025
    Review
  2. Review
  3. Review
  4. Review
  5. The Role of Emerin in Cancer Progression and Metastasis.International journal of molecular sciences · 2021
    Review
  6. Review
  7. Article
  8. Spectrin and its interacting partners in nuclear structure and function.Experimental biology and medicine (Maywood, N.J.) · 2018
    Review
  9. Review
  10. Diseases of the Nucleoskeleton.Comprehensive Physiology · 2016
    Review
  11. Review
  12. Emerin in health and disease.Seminars in cell & developmental biology · 2014
    Review
  13. Article
  14. Lamins at a glance.Journal of cell science · 2012
    Review
  15. Review
  16. Review
  17. 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 1 institution in 1 country.

Adam J MeyerDepartment of Genome Dynamics, University of California, Berkeley, CA 94720, USA.
Donna K Almendrala
Minjoung M Go
Sharon Wald Krauss
Lawrence Berkeley National Laboratory · US

Funding

RED CELL CYTOSKELETAL PROTEIN 4.1 DURING CELL DIVISIONR01DK059079 · NIDDK · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI KRAUSS, SHARON W · 2000 to 2008
$2.0M
NIDDK NIH HHS DK059079NIDDK NIH HHS R01 DK059079
6 · The paper itself

Abstract

The multifunctional structural protein 4.1R is required for assembly and maintenance of functional nuclei but its nuclear roles are unidentified. 4.1R localizes within nuclei, at the nuclear envelope, and in cytoplasm. Here we show that 4.1R, the nuclear envelope protein emerin and the intermediate filament protein lamin A/C co-immunoprecipitate, and that 4.1R-specific depletion in human cells by RNA interference produces nuclear dysmorphology and selective mislocalization of proteins from several nuclear subcompartments. Such 4.1R-deficiency causes emerin to partially redistribute into the cytoplasm, whereas lamin A/C is disorganized at nuclear rims and displaced from nucleoplasmic foci. The nuclear envelope protein MAN1, nuclear pore proteins Tpr and Nup62, and nucleoplasmic proteins NuMA and LAP2α also have aberrant distributions, but lamin B and LAP2β have normal localizations. 4.1R-deficient mouse embryonic fibroblasts show a similar phenotype. We determined the functional effects of 4.1R-deficiency that reflect disruption of the association of 4.1R with emerin and A-type lamin: increased nucleus-centrosome distances, increased β-catenin signaling, and relocalization of β-catenin from the plasma membrane to the nucleus. Furthermore, emerin- and lamin-A/C-null cells have decreased nuclear 4.1R. Our data provide evidence that 4.1R has important functional interactions with emerin and A-type lamin that impact upon nuclear architecture, centrosome-nuclear envelope association and the regulation of β-catenin transcriptional co-activator activity that is dependent on β-catenin nuclear export.

Indexed as

Animalsbeta CateninCell Line, TumorCell NucleusCentrosomeCytoskeletal ProteinsDogsHEK293 CellsHeLa CellsHumansImmunoprecipitationLamin Type AMembrane ProteinsNuclear EnvelopeNuclear ProteinsProtein Bindingbeta CateninCytoskeletal Proteinsemerinerythrocyte membrane band 4.1 proteinLamin Type AMembrane ProteinsNuclear Proteins

Identifiers

PMID21486941
PMCPMC3078812
OpenAlexW2121320546

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.