Evidence map›Paper›PMID 21709252›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

RefilinB (FAM101B) targets filamin A to organize perinuclear actin networks and regulates nuclear shape.

Olivia Gay, Benoît Gilquin, Fumihiko Nakamura, Zandra A Jenkins, Rosannah McCartney, Deborah Krakow, Alexandre Deshiere, Nicole Assard, John H Hartwig, Stephen P Robertson and 1 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed, 1 pooled it
3.3field-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

50 citing papers in PubMed, 1 synthesis or guideline pooled it, 80 citations in OpenAlex.

  1. Pooled it
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  4. NovelJournal of pediatric genetics · 2024
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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 6 institutions in 3 countries.

Olivia GayInstitut National de la Santé et de la Recherche Médicale, Unité 873, F-38054 Grenoble, France.
Benoît Gilquin
Fumihiko Nakamura
Zandra A Jenkins
Rosannah McCartney
Deborah Krakow
Alexandre Deshiere
Nicole Assard
John H Hartwig
Stephen P Robertson
Jacques Baudier
Institut de Recherches en Technologies et Sciences pour le Vivant · FRUniversity of Otago · NZInserm · FRBrigham and Women's Hospital · USCedars-Sinai Medical Center · USHarvard University · US

Funding

REGULATION OF PLATELET SHAPE CHANGESR01HL056252 · NHLBI · BRIGHAM AND WOMEN'S HOSPITAL · PI HARTWIG, JOHN H · 1996 to 2008
$3.3M
NHLBI NIH HHS HL-56252NHLBI NIH HHS R01 HL056252
6 · The paper itself

Abstract

The intracellular localization and shape of the nucleus plays a central role in cellular and developmental processes. In fibroblasts, nuclear movement and shape are controlled by a specific perinuclear actin network made of contractile actin filament bundles called transmembrane actin-associated nuclear (TAN) lines that form a structure called the actin cap. The identification of regulatory proteins associated with this specific actin cytoskeletal dynamic is a priority for understanding actin-based changes in nuclear shape and position in normal and pathological situations. Here, we first identify a unique family of actin regulators, the refilin proteins (RefilinA and RefilinB), that stabilize specifically perinuclear actin filament bundles. We next identify the actin-binding filamin A (FLNA) protein as the downstream effector of refilins. Refilins act as molecular switches to convert FLNA from an actin branching protein into one that bundles. In NIH 3T3 fibroblasts, the RefilinB/FLNA complex organizes the perinuclear actin filament bundles forming the actin cap. Finally, we demonstrate that in epithelial normal murine mammary gland (NmuMG) cells, the RefilinB/FLNA complex controls formation of a new perinuclear actin network that accompanies nuclear shape changes during the epithelial-mesenchymal transition (EMT). Our studies open perspectives for further functional analyses of this unique actin-based network and shed light on FLNA function during development and in human syndromes associated with FLNA mutations.

Indexed as

ActinsAmino Acid SequenceAnimalsAstrocytomaBase SequenceCarrier ProteinsCell LineCell Line, TumorCell NucleusContractile ProteinsDimerizationEpithelial-Mesenchymal TransitionFemaleFilaminsHumansMammary Glands, AnimalActinsCarrier ProteinsContractile ProteinsF-actin-binding proteinsFilaminsMicrofilament ProteinsMultiprotein ComplexesRNA, Small Interfering

Identifiers

PMID21709252
PMCPMC3136255
OpenAlexW2128316146

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.