Evidence map›Paper›PMID 20406475›Full record

ArticleBMC developmental biology2010

The Drosophila Fry protein interacts with Trc and is highly mobile in vivo.

Xiaolan Fang, Qiuheng Lu, Kazou Emoto, Paul N Adler

Open access · hybridAbstract read
In one paragraph

Article in BMC developmental biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

18 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Homer condensates orchestrate YAP-Wnt signaling crosstalk downstream of the Crumbs polarity complex.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Frontiers in oncology · 2019
    Article
  10. Article
  11. Article
  12. Fryl deficiency is associated with defective kidney development and function in mice.Experimental biology and medicine (Maywood, N.J.) · 2018
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. 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

4 authors at 2 institutions in 2 countries.

Xiaolan FangBiology Department, Cell Biology Department, Cancer Center, Morphogenesis and Regenerative Medicine Institute, University of Virginia, Charlottesville, VA 22903, USA.
Qiuheng Lu
Kazou Emoto
Paul N Adler
University of Virginia · USHoward Hughes Medical Institute · US

Funding

MOLECULAR GENETICS OF THE FZ LOCUSR01GM037163 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI ADLER, PAUL N. · 1986 to 2014
$5.0M
GENETIC ANALYSIS OF PREHAIR MORPHOGENESISR01GM053498 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI ADLER, PAUL N. · 1996 to 2005
$995k
NIGMS NIH HHS R01 GM037163NIGMS NIH HHS R01 GM053498
6 · The paper itself

Abstract

backgroundCell polarity is a common feature of eukaryotic cells. The NDR kinases have been found to regulate polarized growth in both animal cells and fungi. Drosophila Tricornered is an NDR kinase that is essential for the normal polarized growth of extensions of epidermal cells and for the tiling and branching of dendrites of da sensory neurons. Tricornered function requires interacting with the large Furry protein (3479 amino acid).

resultsWe constructed a furry (fry) transgene and established that it rescued the lethality of fry null mutations. The encoded protein was tagged at both its amino and carboxy termini and this allowed us to demonstrate that the protein existed as an uncleaved protein in vivo. We used the C terminal GFP tag to follow the protein in vivo and found it to be highly mobile. Interestingly Fry accumulated at the distal tip of growing bristles. We established that Fry and Trc could be co-immunoprecipitated from wing discs.

conclusionsThe mobility of Fry in both bristles and dendrites suggests that it could function in directing/mediating the intracellular transport needed for polarized growth. Our observations that full length Fry and Trc show only partial co-localization in growing bristles while an amino terminal fragment of Fry shows close to complete co-localization with Trc suggests that the interaction between these proteins is transient and regulated.

Indexed as

Amino Acid SequenceAnimalsCell PolarityDNA Transposable ElementsDrosophila melanogasterDrosophila ProteinsGenes, LethalMolecular Sequence DataProtein Interaction Domains and MotifsProtein Serine-Threonine KinasesSequence AlignmentWings, AnimalDNA Transposable ElementsDrosophila Proteinsfry protein, DrosophilaProtein Serine-Threonine Kinasestrc protein, Drosophila

Identifiers

PMID20406475
PMCPMC2868802
OpenAlexW2053225930

What OpenQuestion holds

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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.