Evidence map›Paper›PMID 23339871›Full record

ArticleMolecular and cellular biology2013

The nucleus- and endoplasmic reticulum-targeted forms of protein tyrosine phosphatase 61F regulate Drosophila growth, life span, and fecundity.

Bree J Buszard, Travis K Johnson, Tzu-Ching Meng, Richard Burke, Coral G Warr, Tony Tiganis

Abstract read
In one paragraph

Article in Molecular and cellular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
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

14 citing papers in PubMed.

  1. mBio · 2026
    Article
  2. Gene model for the ortholog ofmicroPublication biology · 2026
    Article
  3. Article
  4. Article
  5. Gene model for the ortholog ofmicroPublication biology · 2025
    Article
  6. Gene model for the ortholog ofmicroPublication biology · 2025
    Article
  7. Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. PTP61F Mediates Cell Competition and Mitigates Tumorigenesis.International journal of molecular sciences · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. 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

6 authors.

Bree J BuszardSchool of Biological Sciences, Monash University, Clayton, Victoria, Australia.
Travis K Johnson
Tzu-Ching Meng
Richard Burke
Coral G Warr
Tony Tiganis

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The protein tyrosine phosphatases (PTPs) T cell PTP (TCPTP) and PTP1B share a high level of catalytic domain sequence and structural similarity yet display distinct differences in substrate recognition and function. Their noncatalytic domains contribute to substrate selectivity and function by regulating TCPTP nucleocytoplasmic shuttling and targeting PTP1B to the endoplasmic reticulum (ER). The Drosophila TCPTP/PTP1B orthologue PTP61F has two variants with identical catalytic domains that are differentially targeted to the ER and nucleus. Here we demonstrate that the PTP61F variants differ in their ability to negatively regulate insulin signaling in vivo, with the nucleus-localized form (PTP61Fn) being more effective than the ER-localized form (PTP61Fm). We report that PTP61Fm is reliant on the adaptor protein Dock to attenuate insulin signaling in vivo. Also, we show that the PTP61F variants differ in their capacities to regulate growth, with PTP61Fn but not PTP61Fm attenuating cellular proliferation. Furthermore, we generate a mutant lacking both PTP61F variants, which displays a reduction in median life span and a decrease in female fecundity, and show that both variants are required to rescue these mutant phenotypes. Our findings define the role of PTP61F in life span and fecundity and reinforce the importance of subcellular localization in mediating PTP function in vivo.

Indexed as

Adaptor Proteins, Signal TransducingAnimalsCell Growth ProcessesCell NucleusDrosophilaDrosophila ProteinsEndoplasmic ReticulumFemaleFertilityInsulinMutationNerve Tissue ProteinsPhenotypeProtein Tyrosine Phosphatase, Non-Receptor Type 1Protein Tyrosine Phosphatase, Non-Receptor Type 2Protein Tyrosine Phosphatases, Non-ReceptorAdaptor Proteins, Signal Transducingdock protein, DrosophilaDrosophila ProteinsInsulinNerve Tissue ProteinsProtein Tyrosine Phosphatase, Non-Receptor Type 1Protein Tyrosine Phosphatase, Non-Receptor Type 2Protein Tyrosine Phosphatases, Non-ReceptorPtp61F protein, DrosophilaReceptor, InsulinStat92E protein, DrosophilaSTAT Transcription Factors

Identifiers

PMID23339871
PMCPMC3624282

What OpenQuestion holds

Textmetadata
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Registered trials

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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.