Evidence map›Paper›PMID 37232489›Full record

ArticleeLife2023

The prolactin receptor scaffolds Janus kinase 2 via co-structure formation with phosphoinositide-4,5-bisphosphate.

Raul Araya-Secchi, Katrine Bugge, Pernille Seiffert, Amalie Petry, Gitte W Haxholm, Kresten Lindorff-Larsen, Stine Falsig Pedersen, Lise Arleth, Birthe B Kragelund

Open access · goldAbstract read
In one paragraph

Article in eLife, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

12 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. A membrane insertion code for intrinsically disordered proteins.bioRxiv : the preprint server for biology · 2026
    Article
  3. Review
  4. Review
  5. Review
  6. ProlineJournal of the American Chemical Society · 2025
    Article
  7. Review
  8. Review
  9. Current Insights in Prolactin Signaling and Ovulatory Function.International journal of molecular sciences · 2024
    Review
  10. Review
  11. Article
  12. 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

9 authors at 1 institution in 2 countries.

Raul Araya-SecchiStructural Biophysics, Section for Neutron and X-ray Science, Niels Bohr Institute, University of Copenhagen, Copenhagen, Denmark.ORCID 0000-0002-4872-3553
Katrine Bugge *Structural Biology and NMR Laboratory (SBiNLab), Department of Biology, University of Copenhagen, Copenhagen, Denmark.ORCID 0000-0002-6286-6243
Pernille Seiffert *Structural Biology and NMR Laboratory (SBiNLab), Department of Biology, University of Copenhagen, Copenhagen, Denmark.ORCID 0000-0003-4213-5336
Amalie PetrySection for Cell Biology and Physiology, Department of Biology, University of Copenhagen, Copenhagen, Denmark.
Gitte W HaxholmStructural Biology and NMR Laboratory (SBiNLab), Department of Biology, University of Copenhagen, Copenhagen, Denmark.
Kresten Lindorff-LarsenStructural Biology and NMR Laboratory (SBiNLab), Department of Biology, University of Copenhagen, Copenhagen, Denmark.ORCID 0000-0002-4750-6039
Stine Falsig PedersenSection for Cell Biology and Physiology, Department of Biology, University of Copenhagen, Copenhagen, Denmark.ORCID 0000-0002-3044-7714
Lise ArlethStructural Biophysics, Section for Neutron and X-ray Science, Niels Bohr Institute, University of Copenhagen, Copenhagen, Denmark.ORCID 0000-0002-4694-4299
Birthe B KragelundStructural Biology and NMR Laboratory (SBiNLab), Department of Biology, University of Copenhagen, Copenhagen, Denmark.ORCID 0000-0002-7454-1761
University of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Class 1 cytokine receptors transmit signals through the membrane by a single transmembrane helix to an intrinsically disordered cytoplasmic domain that lacks kinase activity. While specific binding to phosphoinositides has been reported for the prolactin receptor (PRLR), the role of lipids in PRLR signaling is unclear. Using an integrative approach combining nuclear magnetic resonance spectroscopy, cellular signaling experiments, computational modeling, and simulation, we demonstrate co-structure formation of the disordered intracellular domain of the human PRLR, the membrane constituent phosphoinositide-4,5-bisphosphate (PI(4,5)P

Indexed as

Janus Kinase 2Receptors, ProlactinCarrier ProteinsHumansPhosphorylationProlactinSignal TransductionSTAT5 Transcription FactorCarrier ProteinsJAK2 protein, humanJanus Kinase 2ProlactinReceptors, ProlactinSTAT5 Transcription FactorhumanIDPintegrative structural biologyJAK2molecular biophysicsNMRsimulationsingle pass receptorstructural biology

Identifiers

PMID37232489
PMCPMC10260020
OpenAlexW4378347833

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.