Evidence map›Paper›PMID 29915393›Full record

ReviewOncogene2018

The dynamic and stress-adaptive signaling hub of 14-3-3: emerging mechanisms of regulation and context-dependent protein-protein interactions.

K L Pennington, T Y Chan, M P Torres, J L Andersen

Open access · hybridAbstract readReview
In one paragraph

Review in Oncogene, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 191 papers.

0numbers the graph read from it
0cells of the map it votes in
191citing papers in PubMed
12.7field-weighted citation impact, top 1% 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

191 citing papers in PubMed, 385 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Restoring the 14-3-3/CRAF regulatory interaction in Noonan syndrome using molecular glues.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Hydrogen-Deuterium Exchange Mass Spectrometry for Molecular Glue Characterization.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  18. Review
  19. Article
  20. Article

131 more citing papers are in PubMed but not listed here.

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

4 authors at 2 institutions in 1 country.

K L PenningtonDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, UT, USA.
T Y ChanDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, UT, USA.
M P TorresSchool of Biological Sciences, Georgia Institute of Technology, Atlanta, GA, USA.
J L AndersenDepartment of Chemistry and Biochemistry, Brigham Young University, Provo, UT, USA. jandersen@chem.byu.edu.
Brigham Young University · USGeorgia Institute of Technology · US

Funding

G gamma N-terminal tails as regulators of G protein signalingR01GM117400 · NIGMS · GEORGIA INSTITUTE OF TECHNOLOGY · PI TORRES, MATT PHILLIP · 2016 to 2019
$1.2M
The regulation and targeting of cell survival pathways in cancerR15CA202618 · NCI · BRIGHAM YOUNG UNIVERSITY · PI ANDERSEN, JOSHUA LYON · 2016 to 2019
$864k
NCI NIH HHS R15 CA202618NIGMS NIH HHS R01 GM117400
6 · The paper itself

Abstract

14-3-3 proteins are a family of structurally similar phospho-binding proteins that regulate essentially every major cellular function. Decades of research on 14-3-3s have revealed a remarkable network of interacting proteins that demonstrate how 14-3-3s integrate and control multiple signaling pathways. In particular, these interactions place 14-3-3 at the center of the signaling hub that governs critical processes in cancer, including apoptosis, cell cycle progression, autophagy, glucose metabolism, and cell motility. Historically, the majority of 14-3-3 interactions have been identified and studied under nutrient-replete cell culture conditions, which has revealed important nutrient driven interactions. However, this underestimates the reach of 14-3-3s. Indeed, the loss of nutrients, growth factors, or changes in other environmental conditions (e.g., genotoxic stress) will not only lead to the loss of homeostatic 14-3-3 interactions, but also trigger new interactions, many of which are likely stress adaptive. This dynamic nature of the 14-3-3 interactome is beginning to come into focus as advancements in mass spectrometry are helping to probe deeper and identify context-dependent 14-3-3 interactions-providing a window into adaptive phosphorylation-driven cellular mechanisms that orchestrate the tumor cell's response to a variety of environmental conditions including hypoxia and chemotherapy. In this review, we discuss emerging 14-3-3 regulatory mechanisms with a focus on post-translational regulation of 14-3-3 and dynamic protein-protein interactions that illustrate 14-3-3's role as a stress-adaptive signaling hub in cancer.

Indexed as

14-3-3 ProteinsAnimalsHumansSignal TransductionStress, Physiological14-3-3 Proteins

Identifiers

PMID29915393
PMCPMC6193947
OpenAlexW2807814263

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.