Evidence map›Paper›PMID 18504607›Full record

ArticleDevelopment genes and evolution2008

Context-dependent regulation of Hox protein functions by CK2 phosphorylation sites.

Ouarda Taghli-Lamallem, Cheryl Hsia, Matthew Ronshaugen, William McGinnis

Open access · greenAbstract read
In one paragraph

Article in Development genes and evolution, 2008. 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
1.7field-weighted citation impact, top 17% 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, 27 citations in OpenAlex.

  1. Review
  2. Mechanisms of Specificity for Hox Factor Activity.Journal of developmental biology · 2016
    Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Hox specificity unique roles for cofactors and collaborators.Current topics in developmental biology · 2009
    Review
  12. 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

4 authors at 3 institutions in 2 countries.

Ouarda Taghli-LamallemNeuroscience & Aging Research Center, The Burnham Institute for Medical Research, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.
Cheryl Hsia
Matthew Ronshaugen
William McGinnis
University of California, San Diego · USLGBT Foundation · GBSanford Burnham Prebys Medical Discovery Institute · US

Funding

Specificity in Homeotic Response ElementsR37HD028315 · NICHD · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI MCGINNIS, WILLIAM JAMES · 2006 to 2015
$2.9M
NICHD NIH HHS R37 HD028315
6 · The paper itself

Abstract

Variations in Hox protein sequences and functions have been proposed to contribute to evolutionary changes in appendage shape and number in crustaceans and insects. One model is that insect Hox proteins of the Ultrabithorax (UBX) ortholog class evolved increased abilities to repress Distal-less (Dll) transcription and appendage development in part through the loss of serine and threonine residues in casein kinase 2 (CK2) phosphorylation sites. To explore this possibility, we constructed and tested the appendage repression function of chimeric proteins with insertions of different CK2 consensus sites or phosphomimetics of CK2 sites in C-terminal regions of Drosophila melanogaster UBX. Our results indicate that CK2 sites C-terminal to the homeodomain can inhibit the appendage repression functions of UBX proteins, but only in the context of specific amino acid sequences. Our results, combined with previous findings on evolutionary changes in Hox protein, suggest how intra-protein regulatory changes can diversify Hox protein function, and thus animal morphology.

Indexed as

Amino Acid SequenceAnimalsAnimals, Genetically ModifiedBinding SitesBody PatterningCasein Kinase IIChimeraDrosophila melanogasterDrosophila ProteinsEmbryo, NonmammalianGene Expression Regulation, DevelopmentalHomeodomain ProteinsMolecular Sequence DataPhosphorylationRecombinant Fusion ProteinsSequence Homology, Amino AcidCasein Kinase IIDrosophila ProteinsHomeodomain ProteinsRecombinant Fusion ProteinsTranscription FactorsUbx protein, Drosophila

Identifiers

PMID18504607
PMCPMC2443945
OpenAlexW2132567131

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.