Evidence map›Paper›PMID 12836692›Full record

ReviewJournal of structural and functional genomics2003

Crystallin genes: specialization by changes in gene regulation may precede gene duplication.

Joram Piatigorsky

Abstract readReview
PubMed
In one paragraph

Review in Journal of structural and functional genomics, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
11.4field-weighted citation impact, top 1% 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

32 citing papers in PubMed, 70 citations in OpenAlex.

  1. Review
  2. Moonlighting enzymes: when cellular context defines specificity.Cellular and molecular life sciences : CMLS · 2023
    Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Lens Biology and Biochemistry.Progress in molecular biology and translational science · 2015
    Review
  10. Article
  11. Article
  12. Earliest Holozoan expansion of phosphotyrosine signaling.Molecular biology and evolution · 2014
    Article
  13. Article
  14. Article
  15. Divergence and convergence in enzyme evolution.The Journal of biological chemistry · 2012
    Review
  16. Article
  17. Review
  18. Aggregation of γ-crystallins associated with human cataracts via domain swapping at the C-terminal β-strands.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  19. Article
  20. Article
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

1 author at 1 institution in 1 country.

Joram PiatigorskyLaboratory of Molecular and Developmental Biology, National Eye Institute, NIH, Bethesda, Maryland 20892-2730, USA. joramp@nei.nih.gov
National Eye Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The crystallins account for 80-90% of the water-soluble proteins of the transparent lens. These diverse proteins are responsible for the optical properties of the lens and have been recruited from metabolic enzymes and stress proteins. They often differ among species (i.e. are taxon-specific) and may be expressed outside of the lens where they have non-refractive roles (a situation we call gene sharing). Crystallin recruitment has occurred by changes in gene regulation resulting in high lens expression. Duck lactate dehydrogenase/epsilon-crystallin and alpha-enolase/tau-crystallin are each encoded in single-copy genes, consistent with these enzymes acquiring a crystallin role, without loss of their nonlens metabolic function, by a change in gene regulation in the absence of gene duplication. The small heat shock protein/alpha-crystallins and avian argininosuccinate lyase/delta-crystallins were also recruited by a change in gene regulation leading to high lens expression, except this was followed by a gene duplication with further lens specialization of the alphaA and the delta1 (in chickens) crystallin genes. Cephalopod (squid and octopus) S-crystallins were recruited from glutathione S-transferase apparently after duplication of the original gene encoding the enzyme, although this remains uncertain. We speculate that one of the new genes (glutathione S-transferase/S11-crystallin) specialized for lens expression by a change in gene regulation and subsequently duplicated many times to form the lens-specialized, multiple S-crystallins that lack enzymatic activity. That similar transcription factors (e.g. Pax-6, retinoic acid receptors, maf, Sox, AP-1, CREB) regulate different crystallin genes suggest that common features of lens-specific expression have played a pivotal role for recruiting the diverse, multifunctional proteins as crystallins.

Indexed as

Evolution, MolecularGene DuplicationGene Expression RegulationAnimalsCrystallinsInvertebratesLens, CrystallineCrystallins

Identifiers

PMID12836692
OpenAlexW1571987077

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.