Evidence map›Paper›PMID 11854310›Full record

ArticleThe Journal of cell biology2002

Drosophila Kelch regulates actin organization via Src64-dependent tyrosine phosphorylation.

Reed J Kelso, Andrew M Hudson, Lynn Cooley

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

39 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. TheiScience · 2022
    Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Proximity labeling reveals novel interactomes in liveDevelopment (Cambridge, England) · 2019
    Article
  13. Article
  14. International journal of molecular sciences · 2018
    Article
  15. Review
  16. Stay Connected: A Germ Cell Strategy.Trends in genetics : TIG · 2017
    Review
  17. Article
  18. Article
  19. Drosophila E-cadherin is required for the maintenance of ring canals anchoring to mechanically withstand tissue growth.Proceedings of the National Academy of Sciences of the United States of America · 2015
    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

3 authors at 1 institution in 1 country.

Reed J KelsoDepartment of Cell Biology, Yale University School of Medicine, New Haven, CT 06520-8005, USA.
Andrew M Hudson
Lynn Cooley
Yale University · US

Funding

STUDIES ON OVARIAN RING CANALS IN DROSOPHILAR01GM052702 · NIGMS · YALE UNIVERSITY · PI COOLEY, LYNN · 1996 to 2009
$2.7M
NIGMS NIH HHS GM52702NIGMS NIH HHS R01 GM052702
6 · The paper itself

Abstract

The Drosophila kelch gene encodes a member of a protein superfamily defined by the presence of kelch repeats. In Drosophila, Kelch is required to maintain actin organization in ovarian ring canals. We set out to study the actin cross-linking activity of Kelch and how Kelch function is regulated. Biochemical studies using purified, recombinant Kelch protein showed that full-length Kelch bundles actin filaments, and kelch repeat 5 contains the actin binding site. Two-dimensional electrophoresis demonstrated that Kelch is tyrosine phosphorylated in a src64-dependent pathway. Site-directed mutagenesis determined that tyrosine residue 627 is phosphorylated. A Kelch mutant with tyrosine 627 changed to alanine (KelY627A) rescued the actin disorganization phenotype of kelch mutant ring canals, but failed to produce wild-type ring canals. Electron microscopy demonstrated that phosphorylation of Kelch is critical for the proper morphogenesis of actin during ring canal growth, and presence of the nonphosphorylatable KelY627A protein phenocopied src64 ring canals. KelY627A protein in ring canals also dramatically reduced the rate of actin monomer exchange. The phenotypes caused by src64 mutants and KelY627A expression suggest that a major function of Src64 signaling in the ring canal is the negative regulation of actin cross-linking by Kelch.

Indexed as

Drosophila ProteinsProto-Oncogene ProteinsActinsAlanineAmino Acid SequenceAnimalsCarrier ProteinsCross-Linking ReagentsDrosophilaFemaleInsect ProteinsMicrofilament ProteinsMicroscopy, ElectronMolecular Sequence DataMutagenesis, Site-DirectedPhosphorylationActinsAlanineCarrier ProteinsCross-Linking ReagentsDrosophila ProteinsInsect Proteinskel protein, DrosophilaMicrofilament ProteinsProtein-Tyrosine KinasesProto-Oncogene ProteinsRecombinant Fusion ProteinsSrc64B protein, DrosophilaTyrosine

Identifiers

PMID11854310
PMCPMC2174084
OpenAlexW2108162466

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.