Evidence map›Paper›PMID 15190118›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2004

Espins are multifunctional actin cytoskeletal regulatory proteins in the microvilli of chemosensory and mechanosensory cells.

Gabriella Sekerková, Lili Zheng, Patricia A Loomis, Benjarat Changyaleket, Donna S Whitlon, Enrico Mugnaini, James R Bartles

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
2.9field-weighted citation impact, top 9% 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

56 citing papers in PubMed, 88 citations in OpenAlex.

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  19. Developing a sense of touch.Development (Cambridge, England) · 2017
    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

7 authors at 1 institution in 1 country.

Gabriella SekerkováDepartment of Cell and Molecular Biology, Feinberg School of Medicine, Northwestern University, Chicago, Illinois 60611, USA.
Lili Zheng
Patricia A Loomis
Benjarat Changyaleket
Donna S Whitlon
Enrico Mugnaini
James R Bartles
Northwestern University · US

Funding

THE ROLES OF ESPINS IN HAIR CELL STEREOCILIAR01DC004314 · NIDCD · NORTHWESTERN UNIVERSITY AT CHICAGO · PI BARTLES, JAMES R · 2000 to 2019
$8.0M
DETERMINANTS OF NEURONAL CONNECTIVITY IN THE COCHLEAR01DC000653 · NIDCD · UNIVERSITY OF WISCONSIN MADISON · PI WHITLON, DONNA S. · 1995 to 2005
$1.6M
NIDCD NIH HHS R01 DC000653NIDCD NIH HHS R01 DC004314NIDCD NIH HHS R01 DC00653
6 · The paper itself

Abstract

Espins are associated with the parallel actin bundles of hair cell stereocilia and are the target of mutations that cause deafness and vestibular dysfunction in mice and humans. Here, we report that espins are also concentrated in the microvilli of a number of other sensory cells: vomeronasal organ sensory neurons, solitary chemoreceptor cells, taste cells, and Merkel cells. Moreover, we show that hair cells and these other sensory cells contain novel espin isoforms that arise from a different transcriptional start site and differ significantly from other espin isoforms in their complement of ligand-binding activities and their effects on actin polymerization. The novel espin isoforms of sensory cells bundled actin filaments with high affinity in a Ca(2+)-resistant manner, bound actin monomer via a WASP (Wiskott-Aldrich syndrome protein) homology 2 domain, bound profilin via a single proline-rich peptide, and caused a dramatic elongation of microvillus-type parallel actin bundles in transfected epithelial cells. In addition, the novel espin isoforms of sensory cells differed from other espin isoforms in that they potently inhibited actin polymerization in vitro, did not bind the Src homology 3 domain of the adapter protein insulin receptor substrate p53, and did not bind the acidic, signaling phospholipid phosphatidylinositol 4,5-bisphosphate. Thus, the espins constitute a family of multifunctional actin cytoskeletal regulatory proteins with the potential to differentially influence the organization, dimensions, dynamics, and signaling capabilities of the actin filament-rich, microvillus-type specializations that mediate sensory transduction in various mechanosensory and chemosensory cells.

Indexed as

Signal TransductionActinsAnimalsAnimals, NewbornBlotting, WesternCalciumChemoreceptor CellsCytoskeletal ProteinsDeafnessFemaleFluorescent Antibody TechniqueHair Cells, AuditoryImmunoenzyme TechniquesImmunohistochemistryMaleMechanoreceptorsActinsCalciumCytoskeletal Proteinsespin protein, mouseEspn protein, ratMicrofilament ProteinsPolymersProlineProtein IsoformsType C Phospholipases

Identifiers

PMID15190118
PMCPMC2855134
OpenAlexW2128463171

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.