Evidence map›Paper›PMID 23144950›Full record

ArticlePloS one2012

Tmod1 and CP49 synergize to control the fiber cell geometry, transparency, and mechanical stiffness of the mouse lens.

David S Gokhin, Roberta B Nowak, Nancy E Kim, Ernest E Arnett, Albert C Chen, Robert L Sah, John I Clark, Velia M Fowler

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
2.2field-weighted citation impact, top 13% 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

57 citing papers in PubMed, 67 citations in OpenAlex.

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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

8 authors at 3 institutions in 1 country.

David S GokhinDepartment of Cell Biology, The Scripps Research Institute, La Jolla, California, United States of America.
Roberta B Nowak
Nancy E Kim
Ernest E Arnett
Albert C Chen
Robert L Sah
John I Clark
Velia M Fowler
Scripps Research Institute · USUniversity of California, San Diego · USUniversity of Washington · US

Funding

Vision Research CoreP30EY001730 · NEI · UNIVERSITY OF WASHINGTON · PI MAUREEN E NEITZ · 1985 to 2026
$23.5M
DEVELOPMENT AND MAINTENANCE OF TRANSPARENCY IN LENSESR01EY004542 · NEI · UNIVERSITY OF WASHINGTON · PI CLARK, JOHN IRWIN · 1985 to 2013
$7.1M
Membrane Skeleton Regulation of Cell Shape and Interactions in Lens DevelopmentR01EY017724 · NEI · UNIVERSITY OF DELAWARE · PI FOWLER, VELIA M · 2008 to 2024
$6.9M
BLOOD SYSTEMS IN COAGULATION AND VESSEL DISEASET32HL007195 · NHLBI · SCRIPPS RESEARCH INSTITUTE, THE · PI RUF, WOLFRAM · 1985 to 2011
$5.1M
Howard Hughes Medical InstituteNEI NIH HHS P30 EY001730NEI NIH HHS R01 EY004542NEI NIH HHS R01-EY004542NEI NIH HHS R01 EY017724NEI NIH HHS R01-EY017724NHLBI NIH HHS T32 HL007195NHLBI NIH HHS T32-HL007195
6 · The paper itself

Abstract

The basis for mammalian lens fiber cell organization, transparency, and biomechanical properties has contributions from two specialized cytoskeletal systems: the spectrin-actin membrane skeleton and beaded filament cytoskeleton. The spectrin-actin membrane skeleton predominantly consists of α₂β₂-spectrin strands interconnecting short, tropomyosin-coated actin filaments, which are stabilized by pointed-end capping by tropomodulin 1 (Tmod1) and structurally disrupted in the absence of Tmod1. The beaded filament cytoskeleton consists of the intermediate filament proteins CP49 and filensin, which require CP49 for assembly and contribute to lens transparency and biomechanics. To assess the simultaneous physiological contributions of these cytoskeletal networks and uncover potential functional synergy between them, we subjected lenses from mice lacking Tmod1, CP49, or both to a battery of structural and physiological assays to analyze fiber cell disorder, light scattering, and compressive biomechanical properties. Findings show that deletion of Tmod1 and/or CP49 increases lens fiber cell disorder and light scattering while impairing compressive load-bearing, with the double mutant exhibiting a distinct phenotype compared to either single mutant. Moreover, Tmod1 is in a protein complex with CP49 and filensin, indicating that the spectrin-actin network and beaded filament cytoskeleton are biochemically linked. These experiments reveal that the spectrin-actin membrane skeleton and beaded filament cytoskeleton establish a novel functional synergy critical for regulating lens fiber cell geometry, transparency, and mechanical stiffness.

Indexed as

ActinsAnimalsBiomechanical PhenomenaCell ShapeCytoskeletonEye ProteinsIntermediate Filament ProteinsLens, CrystallineMiceMice, Inbred C57BLMice, Inbred StrainsMutagenesis, Site-DirectedOptics and PhotonicsTropomodulinActinsEye ProteinsIntermediate Filament ProteinsphakininTmod1 protein, mouseTropomodulin

Identifiers

PMID23144950
PMCPMC3492431
OpenAlexW1976441768

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.