Evidence map›Paper›PMID 26483553›Full record

ArticleThe Journal of cell biology2015

NF2/Merlin mediates contact-dependent inhibition of EGFR mobility and internalization via cortical actomyosin.

Christine Chiasson-MacKenzie, Zachary S Morris, Quentin Baca, Brett Morris, Joanna K Coker, Rossen Mirchev, Anne E Jensen, Thomas Carey, Shannon L Stott, David E Golan and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.5field-weighted citation impact, top 8% 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

38 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
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  5. The molecular biology of NF2/Merlin on tumorigenesis and development.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
    Review
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  15. Mechanical disruption of E-cadherin complexes with epidermal growth factor receptor actuates growth factor-dependent signaling.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  16. Review
  17. Review
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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

11 authors at 3 institutions in 1 country.

Christine Chiasson-MacKenzieCenter for Cancer Research, Massachusetts General Hospital, Charlestown, MA 02129 Department of Pathology, Massachusetts General Hospital, Charlestown, MA 02129 Department of Pathology, Harvard Medical School, Boston, MA 02115.
Zachary S MorrisCenter for Cancer Research, Massachusetts General Hospital, Charlestown, MA 02129 Department of Pathology, Massachusetts General Hospital, Charlestown, MA 02129 Department of Pathology, Harvard Medical School, Boston, MA 02115.
Quentin BacaDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.
Brett MorrisCenter for Cancer Research, Massachusetts General Hospital, Charlestown, MA 02129 Department of Pathology, Massachusetts General Hospital, Charlestown, MA 02129 Department of Pathology, Harvard Medical School, Boston, MA 02115.
Joanna K CokerCenter for Cancer Research, Massachusetts General Hospital, Charlestown, MA 02129 Department of Pathology, Massachusetts General Hospital, Charlestown, MA 02129 Department of Pathology, Harvard Medical School, Boston, MA 02115.
Rossen MirchevDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.
Anne E JensenCenter for Cancer Research, Massachusetts General Hospital, Charlestown, MA 02129 BioMEMs Resource Center, Massachusetts General Hospital, Charlestown, MA 02129.
Thomas CareyCenter for Cancer Research, Massachusetts General Hospital, Charlestown, MA 02129 BioMEMs Resource Center, Massachusetts General Hospital, Charlestown, MA 02129.
Shannon L StottCenter for Cancer Research, Massachusetts General Hospital, Charlestown, MA 02129 BioMEMs Resource Center, Massachusetts General Hospital, Charlestown, MA 02129 Department of Medicine, Harvard Medical School, Boston, MA 02115.
David E GolanDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.
Andrea I McClatcheyCenter for Cancer Research, Massachusetts General Hospital, Charlestown, MA 02129 Department of Pathology, Massachusetts General Hospital, Charlestown, MA 02129 Department of Pathology, Harvard Medical School, Boston, MA 02115 mcclatch@helix.mgh.harvard.edu.
Center for Cancer Research · USHarvard University · USMassachusetts General Hospital · US

Funding

Training in Pharmacological SciencesT32GM007306 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI GOLAN, DAVID E. · 1985 to 2018
$6.6M
Molecular Function of the Nf2 Tumor Suppressor, MerlinR01CA113733 · NCI · MASSACHUSETTS GENERAL HOSPITAL · PI MCCLATCHEY, ANDREA I · 2005 to 2014
$3.1M
Molecular Regulation of Adhesive Integrin Interactions in Erythroblastic IslandsR01HL032854 · NHLBI · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI GOLAN, DAVID E. · 1985 to 2011
$2.0M
Integrin-Based Mechanisms in Terminal Erythroid MaturationR01HL116327 · NHLBI · HARVARD MEDICAL SCHOOL · PI GOLAN, DAVID E. · 2012 to 2015
$1.7M
Minority Predoctoral Fellowship ProgramF31GM078720 · NIGMS · HARVARD MEDICAL SCHOOL · PI BACA, QUENTIN J · 2008 to 2010
$124k
NCI NIH HHS R01 CA113733NHLBI NIH HHS R01 HL032854NHLBI NIH HHS R01 HL116327NIGMS NIH HHS F31 GM078720NIGMS NIH HHS F31 GM78720NIGMS NIH HHS T32 GM007306NIGMS NIH HHS T32 GM07306
6 · The paper itself

Abstract

The proliferation of normal cells is inhibited at confluence, but the molecular basis of this phenomenon, known as contact-dependent inhibition of proliferation, is unclear. We previously identified the neurofibromatosis type 2 (NF2) tumor suppressor Merlin as a critical mediator of contact-dependent inhibition of proliferation and specifically found that Merlin inhibits the internalization of, and signaling from, the epidermal growth factor receptor (EGFR) in response to cell contact. Merlin is closely related to the membrane-cytoskeleton linking proteins Ezrin, Radixin, and Moesin, and localization of Merlin to the cortical cytoskeleton is required for contact-dependent regulation of EGFR. We show that Merlin and Ezrin are essential components of a mechanism whereby mechanical forces associated with the establishment of cell-cell junctions are transduced across the cell cortex via the cortical actomyosin cytoskeleton to control the lateral mobility and activity of EGFR, providing novel insight into how cells inhibit mitogenic signaling in response to cell contact.

Indexed as

Actin CytoskeletonActomyosinAnimalsCell ProliferationCells, CulturedContact InhibitionCytoskeletal ProteinsErbB ReceptorsEzrinIntercellular JunctionsMechanotransduction, CellularMembrane ProteinsMiceMicrofilament ProteinsNeurofibromin 2Nonmuscle Myosin Type IIAActomyosinCytoskeletal ProteinsEGFR protein, mouseErbB ReceptorsEzrinMembrane ProteinsMicrofilament ProteinsmoesinNeurofibromin 2Nonmuscle Myosin Type IIAradixinRNA, Small Interfering

Identifiers

PMID26483553
PMCPMC4621825
OpenAlexW1852638080

What OpenQuestion holds

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LicenceCC BY-NC-SA
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.