Evidence map›Paper›PMID 15688033›Full record

ArticleOncogene2005

Membrane localization of the U2 domain of Protein 4.1B is necessary and sufficient for meningioma growth suppression.

Victoria A Robb, Mark A Gerber, Elizabeth K Hart-Mahon, David H Gutmann

Abstract read
PubMed Publisher
In one paragraph

Article in Oncogene, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

16 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. 4.1N is involved in a flotillin-1/β-catenin/Wnt pathway and suppresses cell proliferation and migration in non-small cell lung cancer cell lines.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
    Article
  6. Article
  7. Article
  8. Article
  9. Tumor suppressor role of protein 4.1B/DAL-1.Cellular and molecular life sciences : CMLS · 2014
    Review
  10. Article
  11. Article
  12. Aberrant signaling pathways in meningiomas.Journal of neuro-oncology · 2010
    Review
  13. Review
  14. Protein 4.1B suppresses prostate cancer progression and metastasis.Proceedings of the National Academy of Sciences of the United States of America · 2007
    Article
  15. Article
  16. 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

4 authors at 1 institution in 1 country.

Victoria A RobbDepartment of Neurology, Washington University School of Medicine, St Louis, MO 63110, USA.
Mark A Gerber
Elizabeth K Hart-Mahon
David H Gutmann
Washington University in St. Louis · US

Funding

PROTEIN 4.1 TUMOR SUPPRESSORS IN MENINGIOMA PATHOGENESISR01NS041520 · NINDS · WASHINGTON UNIVERSITY · PI GUTMANN, DAVID H. · 2001 to 2003
$807k
Mechanisms of Protein 4.1B Tumor SuppressionF32CA097816 · NCI · WASHINGTON UNIVERSITY · PI HILDEBRANDT, VICTORIA A · 2002 to 2003
$85k
NCI NIH HHS 1-F32-CA-097816-01NINDS NIH HHS NS41520
6 · The paper itself

Abstract

Meningiomas are common central nervous system tumors; however, the molecular mechanisms underlying their pathogenesis are largely undefined. Previous work has implicated Protein 4.1B as an important tumor suppressor involved in the development of these neoplasms. In this report, we demonstrate that the U2 domain is necessary and sufficient for the ability of Protein 4.1B to function as a meningioma growth suppressor. Using a series of truncation and deletion constructs of DAL-1 (a fragment of Protein 4.1B that retains all the growth suppressive properties), we narrowed the domain required for 4.1B growth suppression to a fragment containing a portion of the FERM domain and the U2 domain using clonogenic assays on meningioma cells. Deletion of the U2 domain in the context of the full-length DAL-1 molecule eliminated growth suppressor function, as measured by thymidine incorporation and caspase-3 activation. Moreover, targeting the U2 domain to the plasma membrane using a membrane localization signal (MLS) reduced cell proliferation, similar to wild-type DAL-1. Collectively, the data suggest that the U2 domain, when properly targeted to the plasma membrane, contains all the residues necessary for mediating Protein 4.1B growth suppression.

Indexed as

Cell DivisionAnimalsBase SequenceCell Line, TumorCell MembraneDNA PrimersHumansMembrane ProteinsMeningeal NeoplasmsMeningiomaMicrofilament ProteinsPolymerase Chain ReactionRatsSequence DeletionTransfectionDNA PrimersEPB41L3 protein, humanMembrane ProteinsMicrofilament Proteins

Identifiers

PMID15688033
OpenAlexW2007379437

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.