Evidence map›Paper›PMID 24176936›Full record

ReviewAdvances in biological regulation2014

Disentangling biological signaling networks by dynamic coupling of signaling lipids to modifying enzymes.

Raymond D Blind

Open access · greenAbstract readReview
In one paragraph

Review in Advances in biological regulation, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

20 citing papers in PubMed, 27 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. SF-1 Induces Nuclear PIP2.Biomolecules · 2023
    Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. Nuclear phosphoinositide regulation of chromatin.Journal of cellular physiology · 2018
    Review
  11. Review
  12. Review
  13. Phospholipid regulation of the nuclear receptor superfamily.Advances in biological regulation · 2017
    Review
  14. Review
  15. IQGAP1 is a phosphoinositide effector and kinase scaffold.Advances in biological regulation · 2016
    Review
  16. Article
  17. Article
  18. Review
  19. Review
  20. The signaling phospholipid PIP3 creates a new interaction surface on the nuclear receptor SF-1.Proceedings of the National Academy of Sciences of the United States of America · 2014
    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

1 author at 1 institution in 1 country.

Raymond D BlindDepartment of Cellular and Molecular Pharmacology, University of California San Francisco, San Francisco, CA 94158, USA. Electronic address: ray.blind@gmail.com.
University of California, San Francisco · US

Funding

Cancer cell signaling through lipids complexed to proteinsK01CA172957 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI BLIND, RAYMOND DANIEL · 2012 to 2015
$449k
NCI NIH HHS K01 CA172957
6 · The paper itself

Abstract

An unresolved problem in biological signal transduction is how particular branches of highly interconnected signaling networks can be decoupled, allowing activation of specific circuits within complex signaling architectures. Although signaling dynamics and spatiotemporal mechanisms serve critical roles, it remains unclear if these are the only ways cells achieve specificity within networks. The transcription factor Steroidogenic Factor-1 (SF-1) is an excellent model to address this question, as it forms dynamic complexes with several chemically distinct lipid species (phosphatidylinositols, phosphatidylcholines and sphingolipids). This property is important since lipids bound to SF-1 are modified by lipid signaling enzymes (IPMK & PTEN), regulating SF-1 biological activity in gene expression. Thus, a particular SF-1/lipid complex can interface with a lipid signaling enzyme only if SF-1 has been loaded with a chemically compatible lipid substrate. This mechanism permits dynamic downstream responsiveness to constant upstream input, disentangling specific pathways from the full network. The potential of this paradigm to apply generally to nuclear lipid signaling is discussed, with particular attention given to the nuclear receptor superfamily of transcription factors and their phospholipid ligands.

Indexed as

Lipid MetabolismAnimalsHumansSignal TransductionSteroidogenic Factor 1Steroidogenic Factor 1

Identifiers

PMID24176936
PMCPMC3946453
OpenAlexW2034870498

What OpenQuestion holds

Textmetadata
LicenceTDM
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.