Evidence map›Paper›PMID 11368764›Full record

ArticleThe Biochemical journal2001

The neurofibromatosis 2 protein product merlin selectively binds F-actin but not G-actin, and stabilizes the filaments through a lateral association.

M F James, N Manchanda, C Gonzalez-Agosti, J H Hartwig, V Ramesh

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2001. 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
1.6field-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

38 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Gene replacement therapy in a schwannoma mouse model of neurofibromatosis type 2.Molecular therapy. Methods & clinical development · 2022
    Article
  5. Article
  6. Article
  7. Article
  8. Hippo-Yap/Taz signaling: Complex network interactions and impact in epithelial cell behavior.Wiley interdisciplinary reviews. Developmental biology · 2020
    Review
  9. Article
  10. Review
  11. International journal of biological sciences · 2019
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. A neuronal function of the tumor suppressor protein merlin.Acta neuropathologica communications · 2014
    Review
  17. Review
  18. Article
  19. Review
  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 2 institutions in 1 country.

M F JamesMolecular Neurogenetics Unit, Massachusetts General Hospital, Building 149, 13th Street, Charlestown, MA 02129, USA.
N Manchanda
C Gonzalez-Agosti
J H Hartwig
V Ramesh
Massachusetts General Hospital · USBrigham and Women's Hospital · US

Funding

PREVENTION OF COLD INDUCED PLATELET STORAGE LESIONP01HL056949 · NHLBI · IMMUNE DISEASE INSTITUTE, INC. · PI WAGNER, DENISA D · 1996 to 2010
$26.2M
Vector Query and Therapy For TSC and NF2 LesionsP01NS024279 · NINDS · MASSACHUSETTS GENERAL HOSPITAL · PI KWIATKOWSKI, DAVID J. · 1987 to 2012
$14.7M
NF2 PROTEIN, MERLIN, AND ACTIN FILAMENT ASSEMBLYF32NS010699 · NINDS · MASSACHUSETTS GENERAL HOSPITAL · PI JAMES, MARIANNE · 1998 to 2000
$39k
NHLBI NIH HHS HL56949NINDS NIH HHS F32-NS10699NINDS NIH HHS NS24279
6 · The paper itself

Abstract

The neurofibromatosis 2 protein product merlin, named for its relatedness to the ezrin, radixin and moesin (ERM) family of proteins, is a tumour suppressor whose absence results in the occurrence of multiple tumours of the nervous system, particularly schwannomas and meningiomas. Merlin's similarity to ERMs suggests that it might share functions, acting as a link between cytoskeletal components and the cell membrane. The N-terminus of merlin has strong sequence identity to the N-terminal actin-binding region of ezrin; here we describe in detail the merlin-actin interaction. Employing standard actin co-sedimentation assays, we have determined that merlin isoform 2 binds F-actin with an apparent binding constant of 3.6 microM and a stoichiometry of 1 mol of merlin per 11.5 mol of actin in filaments at saturation. Further, solid-phase binding assays reveal that merlin isoforms 1 and 2 bind actin filaments differentially, suggesting that the intramolecular interactions in isoform 1 might hinder its ability to bind actin. However, merlin does not bind G-actin. Studies of actin filament dynamics show that merlin slows filament disassembly with no influence on the assembly rate, indicating that merlin binds along actin filament lengths. This conclusion is supported by electron microscopy, which demonstrates that merlin binds periodically along cytoskeletal actin filaments. Comparison of these findings with those reported for ERM proteins reveal a distinct role for merlin in actin filament dynamics.

Indexed as

ActinsAnimalsCytoskeletonHumansIn Vitro TechniquesMembrane ProteinsMeningiomaMicroscopy, ElectronNeurofibromatosis 2Neurofibromin 2Protein BindingProtein IsoformsRabbitsRecombinant Fusion ProteinsTumor Cells, CulturedActinsMembrane ProteinsNeurofibromin 2Protein IsoformsRecombinant Fusion Proteins

Identifiers

PMID11368764
PMCPMC1221848
OpenAlexW2050152356

What OpenQuestion holds

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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.