Evidence map›Paper›PMID 19889974›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

The receptor protein tyrosine phosphatase LAR promotes R7 photoreceptor axon targeting by a phosphatase-independent signaling mechanism.

Kerstin Hofmeyer, Jessica E Treisman

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

27 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Article
  3. Structure and evolution of neuronal wiring receptors and ligands.Developmental dynamics : an official publication of the American Association of Anatomists · 2023
    Review
  4. Article
  5. Article
  6. Article
  7. Spatial confinement of receptor activity by tyrosine phosphatase during directional cell migration.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  8. Article
  9. Mechanisms of PTPσ-Mediated Presynaptic Differentiation.Frontiers in synaptic neuroscience · 2019
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Loss of syd-1 from R7 neurons disrupts two distinct phases of presynaptic development.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012
    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

2 authors at 1 institution in 1 country.

Kerstin HofmeyerDepartment of Cell Biology, New York University School of Medicine, Kimmel Center for Biology and Medicine of the Skirball Institute, New York, NY 10016, USA.
Jessica E Treisman
New York University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Receptor protein tyrosine phosphatases (RPTPs) control many aspects of nervous system development. At the Drosophila neuromuscular junction (NMJ), regulation of synapse growth and maturation by the RPTP LAR depends on catalytic phosphatase activity and on the extracellular ligands Syndecan and Dally-like. We show here that the function of LAR in controlling R7 photoreceptor axon targeting in the visual system differs in several respects. The extracellular domain of LAR important for this process is distinct from the domains known to bind Syndecan and Dally-like, suggesting the involvement of a different ligand. R7 targeting does not require LAR phosphatase activity, but instead depends on the phosphatase activity of another RPTP, PTP69D. In addition, a mutation that prevents dimerization of the intracellular domain of LAR interferes with its ability to promote R7 targeting, although it does not disrupt phosphatase activity or neuromuscular synapse growth. We propose that LAR function in R7 is independent of its phosphatase activity, but requires structural features that allow dimerization and may promote the assembly of downstream effectors.

Indexed as

AnimalsAxonsDrosophila melanogasterDrosophila ProteinsNeuromuscular JunctionPhotoreceptor Cells, InvertebrateReceptor-Like Protein Tyrosine PhosphatasesSignal TransductionDrosophila ProteinsLar protein, DrosophilaReceptor-Like Protein Tyrosine Phosphatases

Identifiers

PMID19889974
PMCPMC2780745
OpenAlexW2065799209

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.