Evidence map›Paper›PMID 20368450›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Microtubule-mediated transport of the tumor-suppressor protein Merlin and its mutants.

Lorena B Benseñor, Kari Barlan, Sarah E Rice, Richard G Fehon, Vladimir I Gelfand

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

25 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
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  5. Article
  6. Article
  7. Review
  8. Article
  9. Roles of Membrane and Vesicular Traffic in Regulation of the Hippo Pathway.Frontiers in cell and developmental biology · 2019
    Review
  10. Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Nanoscale clustering of carbohydrate thiols in mixed self-assembled monolayers on gold.Langmuir : the ACS journal of surfaces and colloids · 2012
    Article
  20. 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

5 authors at 2 institutions in 1 country.

Lorena B BenseñorDepartment of Cell and Molecular Biology, Northwestern University Feinberg School of Medicine, Chicago, IL 60611, USA.
Kari Barlan
Sarah E Rice
Richard G Fehon
Vladimir I Gelfand
Northwestern University · USUniversity of Chicago · US

Funding

FUNCTIONS OF DMERLIN--A NF2 GENE HOMOLOGUER01NS034783 · NINDS · UNIVERSITY OF CHICAGO · PI Richard G Fehon · 1996 to 2026
$8.4M
REGULATION OF MYOSIN DRIVEN ORGANELLE TRANSPORTR01GM052111 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI GELFAND, VLADIMIR I · 1999 to 2018
$8.3M
The Mechanism of Kinesin Self-RegulationR01GM072656 · NIGMS · NORTHWESTERN UNIVERSITY AT CHICAGO · PI RICE, SARAH E. · 2005 to 2014
$2.5M
MICROTUBULE MOTORS--SPECIFICITY AND REGULATIONR55GM052111 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI GELFAND, VLADIMIR I · 1995 to 1995
–
NIGMS NIH HHS GM52111NIGMS NIH HHS R01 GM052111NIGMS NIH HHS R01 GM072656NINDS NIH HHS R01 NS034783
6 · The paper itself

Abstract

The neurofibromatosis type 2 (NF2) tumor-suppressor protein Merlin is a member of the ERM family of proteins that links the cytoskeleton to the plasma membrane. In humans, mutations in the NF2 gene cause neurofibromatosis type-2 (NF2), a cancer syndrome characterized by the development of tumors of the nervous system. Previous reports have suggested that the subcellular distribution of Merlin is critical to its function, and that several NF2 mutants that lack tumor-suppressor activity present improper localization. Here we used a Drosophila cell culture model to study the distribution and mechanism of intracellular transport of Merlin and its mutants. We found that Drosophila Merlin formed cytoplasmic particles that move bidirectionally along microtubules. A single NF2-causing amino acid substitution in the FERM domain dramatically inhibited Merlin particle movement. Surprisingly, the presence of this immotile Merlin mutant also inhibited trafficking of the WT protein. Analysis of the movement of WT protein using RNAi and pull-downs showed that Merlin particles are associated with and moved by microtubule motors (kinesin-1 and cytoplasmic dynein), and that binding of motors and movement is regulated by Merlin phosphorylation. Inhibition of Merlin transport by expression of the dominant-negative mutant or depletion of kinesin-1 results in increased nuclear accumulation of the transcriptional coactivator Yorkie. These results demonstrate the requirement of microtubule-dependent transport for Merlin function.

Indexed as

AnimalsBiological TransportConcanavalin ACytoplasmDrosophila melanogasterDrosophila ProteinsDyneinsEndocytosisGreen Fluorescent ProteinsKinesinsMicrotubulesModels, BiologicalNeurofibromin 2Nuclear ProteinsPhosphorylationProtein Structure, TertiaryConcanavalin ADrosophila ProteinsDyneinsGreen Fluorescent ProteinsKinesinsmerlin, DrosophilaNeurofibromin 2Nuclear ProteinsTrans-ActivatorsYAP-Signaling ProteinsYki protein, Drosophila

Identifiers

PMID20368450
PMCPMC2867680
OpenAlexW1978013295

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.