Evidence map›Paper›PMID 23437151›Full record

ArticlePloS one2013

FCHSD1 and FCHSD2 are expressed in hair cell stereocilia and cuticular plate and regulate actin polymerization in vitro.

Huiren Cao, Xiaolei Yin, Yujie Cao, Yecheng Jin, Shan Wang, Yanhui Kong, Yuexing Chen, Jiangang Gao, Stefan Heller, Zhigang Xu

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.0field-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

30 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
  2. Article
  3. Key genes and immune infiltration patterns and the clinical implications in psoriasis patients.Skin research and technology : official journal of International Society for Bioengineering and the Skin (ISBS) [and] International Society for Digital Imaging of Skin (ISDIS) [and] International Society for Skin Imaging (ISSI) · 2024
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  4. Review
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  9. Loss of FCHSD1 leads to amelioration of chronic obstructive pulmonary disease.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
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  15. 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

10 authors at 2 institutions in 2 countries.

Huiren CaoShandong Provincial Key Laboratory of Animal Cells and Developmental Biology, Institute of Developmental Biology, School of Life Sciences, Shandong University, Jinan, Shandong, People's Republic of China.
Xiaolei Yin
Yujie Cao
Yecheng Jin
Shan Wang
Yanhui Kong
Yuexing Chen
Jiangang Gao
Stefan Heller
Zhigang Xu
Shandong University · CNStanford University · US

Funding

Molecular Mechanisms of Inner Ear FunctionR01DC004563 · NIDCD · STANFORD UNIVERSITY · PI HELLER, STEFAN · 2001 to 2014
$5.1M
Stanford OHNS Core CenterP30DC010363 · NIDCD · STANFORD UNIVERSITY · PI RICCI, ANTHONY J · 2009 to 2016
$3.0M
NIDCD NIH HHS DC004563NIDCD NIH HHS DC010363NIDCD NIH HHS P30 DC010363NIDCD NIH HHS R01 DC004563
6 · The paper itself

Abstract

Mammalian FCHSD1 and FCHSD2 are homologous proteins containing an amino-terminal F-BAR domain and two SH3 domains near their carboxyl-termini. We report here that FCHSD1 and FCHSD2 are expressed in mouse cochlear sensory hair cells. FCHSD1 mainly localizes to the cuticular plate, whereas FCHSD2 mainly localizes along the stereocilia in a punctuate pattern. Nervous Wreck (Nwk), the Drosophila ortholog of FCHSD1 and FCHSD2, has been shown to bind Wsp and play an important role in F-actin assembly. We show that, like its Drosophila counterpart, FCHSD2 interacts with WASP and N-WASP, the mammalian orthologs of Drosophila Wsp, and stimulates F-actin assembly in vitro. In contrast, FCHSD1 doesn't bind WASP or N-WASP, and can't stimulate F-actin assembly when tested in vitro. We found, however, that FCHSD1 binds via its F-BAR domain to the SH3 domain of Sorting Nexin 9 (SNX9), a well characterized BAR protein that has been shown to promote WASP-Arp2/3-dependent F-actin polymerization. FCHSD1 greatly enhances SNX9's WASP-Arp2/3-dependent F-actin polymerization activity. In hair cells, SNX9 was detected in the cuticular plate, where it colocalizes with FCHSD1. Our results suggest that FCHSD1 and FCHSD2 could modulate F-actin assembly or maintenance in hair cell stereocilia and cuticular plate.

Indexed as

Actin CytoskeletonActinsAmino Acid SequenceAnimalsCarrier ProteinsCochleaHair Cells, AuditoryHumansMembrane ProteinsMicesrc Homology DomainsStereociliaWiskott-Aldrich Syndrome ProteinWiskott-Aldrich Syndrome Protein, NeuronalActinsCarrier ProteinsFCHSD1 protein, humanFCHSD2 protein, humanMembrane ProteinsWasl protein, mouseWiskott-Aldrich Syndrome ProteinWiskott-Aldrich Syndrome Protein, Neuronal

Identifiers

PMID23437151
PMCPMC3577914
OpenAlexW2058824498

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.