Evidence map›Paper›PMID 22715935›Full record

ArticleThe FEBS journal2012

A role for γS-crystallin in the organization of actin and fiber cell maturation in the mouse lens.

Jianguo Fan, Lijin Dong, Sanghamitra Mishra, Yingwei Chen, Paul FitzGerald, Graeme Wistow

Open access · bronzeAbstract read
In one paragraph

Article in The FEBS journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

12 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Lens Biology and Biochemistry.Progress in molecular biology and translational science · 2015
    Review
  9. Review
  10. Article
  11. Evolution of crystallins for a role in the vertebrate eye lens.Protein science : a publication of the Protein Society · 2013
    Review
  12. 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

6 authors at 3 institutions in 1 country.

Jianguo FanSection on Molecular Structure and Functional Genomics, National Eye Institute, National Institutes of Health, Bethesda, MD 20892-0608, USA.
Lijin Dong
Sanghamitra Mishra
Yingwei Chen
Paul FitzGerald
Graeme Wistow
National Institutes of Health · USNational Eye Institute · USUniversity of California, Davis · US

Funding

NEI Genetic Engineering CoreZICEY000458 · NEI · NATIONAL EYE INSTITUTE · PI DONG, LIJIN · 2009 to 2025
$22.6M
VISION RESEARCH CORE GRANTP30EY012576 · NEI · UNIVERSITY OF CALIFORNIA DAVIS · PI LISA M OAKES · 1999 to 2026
$18.9M
Molecular Structure and Function of CrystallinsZIAEY000255 · NEI · NATIONAL EYE INSTITUTE · PI WISTOW, GRAEME J · 2009 to 2025
$6.6M
MOLECULAR ANALYSIS OF OCULAR LENS BEADED FILAMENTSR01EY008747 · NEI · UNIVERSITY OF CALIFORNIA DAVIS · PI FITZGERALD, PAUL GILLESPIE · 1990 to 2010
$4.5M
Intramural NIH HHS ZIA EY000255NEI NIH HHS EY08747NEI NIH HHS P30 EY012576NEI NIH HHS P30 EY12576NEI NIH HHS R01 EY008747
6 · The paper itself

Abstract

γS-crystallin (γS) is a highly conserved component of the eye lens. To gain insights into the functional role(s) of this protein, the mouse gene (Crygs) was deleted. Although mutations in γS can cause severe cataracts, loss of function of γS in knockout (KO) mice produced no obvious lens opacity, but was associated with focusing defects. Electron microscopy showed no major differences in lens cell organization, suggesting that the optical defects are primarily cytoplasmic in origin. KO lenses were also grossly normal by light microscopy but showed evidence of incomplete clearance of cellular organelles in maturing fiber cells. Phalloidin labeling showed an unusual distribution of F-actin in a band of mature fiber cells in KO lenses, suggesting a defect in the organization or processing of the actin cytoskeleton. Indeed, in wild-type lenses, γS and F-actin colocalize along the fiber cell plasma membrane. Relative levels of F-actin and G-actin in wild-type and KO lenses were estimated from fluorescent staining profiles and from isolation of actin fractions from whole lenses. Both methods showed a two-fold reduction in the F-actin/G-actin ratio in KO lenses, whereas no difference in tubulin organization was detected. In vitro experiments showed that recombinant mouse γS can directly stabilize F-actin. This suggests that γS may have a functional role related to actin, perhaps in 'shepherding' filaments to maintain the optical properties of the lens cytoplasm and normal fiber cell maturation.

Indexed as

ActinsAnimalsgamma-CrystallinsLens, CrystallineMiceMice, KnockoutActinsgamma-Crystallins

Identifiers

PMID22715935
PMCPMC3429115
OpenAlexW1502612631

What OpenQuestion holds

Textmetadata
LicenceTDM
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.