Evidence map›Paper›PMID 25107277›Full record

ArticleeLife2014

The Drosophila F-box protein Fbxl7 binds to the protocadherin fat and regulates Dachs localization and Hippo signaling.

Justin A Bosch, Taryn M Sumabat, Yassi Hafezi, Brett J Pellock, Kevin D Gandhi, Iswar K Hariharan

Open access · goldAbstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

33 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Cortical tension promotes Kibra degradation via Par-1.Molecular biology of the cell · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Biallelic mutation of FBXL7 suggests a novel form of Hennekam syndrome.American journal of medical genetics. Part A · 2020
    Article
  17. Article
  18. Fat-regulated adaptor protein Dlish binds the growth suppressor Expanded and controls its stability and ubiquitination.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  19. Article
  20. Journal of clinical medicine · 2018
    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

6 authors at 2 institutions in 1 country.

Justin A BoschDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States.
Taryn M SumabatDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States.
Yassi HafeziDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States.
Brett J PellockDepartment of Biology, Providence College, Providence, United States.
Kevin D GandhiDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States.
Iswar K HariharanDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United States ikh@berkeley.edu.
University of California, Berkeley · USProvidence College · US

Funding

Training in Developmental Cardiovascular BiologyT32HL007544 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SRIVASTAVA, DEEPAK · 1985 to 2021
$4.5M
REGULATION OF CELL AND ORGAN SIZE IN VIVOR01GM061672 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI HARIHARAN, ISWAR K. · 2000 to 2017
$4.5M
NHLBI NIH HHS T32 HL007544NIGMS NIH HHS R01 GM061672NIGMS NIH HHS R01GM61672
6 · The paper itself

Abstract

The Drosophila protocadherin Fat (Ft) regulates growth, planar cell polarity (PCP) and proximodistal patterning. A key downstream component of Ft signaling is the atypical myosin Dachs (D). Multiple regions of the intracellular domain of Ft have been implicated in regulating growth and PCP but how Ft regulates D is not known. Mutations in Fbxl7, which encodes an F-box protein, result in tissue overgrowth and abnormalities in proximodistal patterning that phenocopy deleting a specific portion of the intracellular domain (ICD) of Ft that regulates both growth and PCP. Fbxl7 binds to this same portion of the Ft ICD, co-localizes with Ft to the proximal edge of cells and regulates the levels and asymmetry of D at the apical membrane. Fbxl7 can also regulate the trafficking of proteins between the apical membrane and intracellular vesicles. Thus Fbxl7 functions in a subset of pathways downstream of Ft and links Ft to D localization.

Indexed as

AnimalsBinding SitesBody PatterningCell Adhesion MoleculesCell PolarityDrosophila melanogasterDrosophila ProteinsF-Box ProteinsGene Expression Regulation, DevelopmentalHippo KinasesIntracellular Signaling Peptides and ProteinsMutationMyosinsProtein BindingProtein Serine-Threonine KinasesProtein Structure, TertiaryCell Adhesion Moleculesdachs protein, DrosophilaDrosophila ProteinsF-Box ProteinsFbxl7 protein, Drosophilaft protein, DrosophilaHippo Kinaseshpo protein, DrosophilaIntracellular Signaling Peptides and ProteinsMyosinsProtein Serine-Threonine Kinasescadherincell proliferationHippo pathwayplanar cell polarityubiquitinvesicle

Identifiers

PMID25107277
PMCPMC4144329
OpenAlexW2101421527

What OpenQuestion holds

Textmetadata
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.