Evidence map›Paper›PMID 28437168›Full record

ArticleCell cycle (Georgetown, Tex.)2017

Regulation of PTEN degradation and NEDD4-1 E3 ligase activity by Numb.

Chen Shao, Zhiguo Li, Nihal Ahmad, Xiaoqi Liu

Open access · bronzeAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.1field-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

24 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. The HECT family of E3 ubiquitin ligases and PTEN.Seminars in cancer biology · 2022
    Review
  8. International journal of molecular sciences · 2021
    Article
  9. Article
  10. Adaptors as the regulators of HECT ubiquitin ligases.Cell death and differentiation · 2021
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. HECT E3 Ligases: A Tale With Multiple Facets.Frontiers in physiology · 2019
    Review
  19. 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

4 authors at 3 institutions in 1 country.

Chen Shaoa Department of Biochemistry , Purdue University , West Lafayette , IN , USA.
Zhiguo Lia Department of Biochemistry , Purdue University , West Lafayette , IN , USA.
Nihal Ahmadb Department of Dermatology , University of Wisconsin , Madison , WI , USA.
Xiaoqi Liua Department of Biochemistry , Purdue University , West Lafayette , IN , USA.
Purdue University West Lafayette · USCenter for Cancer Research · USUniversity of Wisconsin–Madison · US

Funding

Role of Polo-Like Kinase-1 in Melanocytic TransformationR01AR059130 · NIAMS · UNIVERSITY OF WISCONSIN-MADISON · PI AHMAD, NIHAL · 2010 to 2019
$3.8M
Role of SIRT1 in melanocyte biology and melanocyte transformationR01CA176748 · NCI · UNIVERSITY OF WISCONSIN-MADISON · PI AHMAD, NIHAL · 2013 to 2017
$1.6M
BD Fortessa Flow Cytometer for Multi-User Shared FacilityS10OD020029 · OD · PURDUE UNIVERSITY · PI RATLIFF, TIMOTHY L. · 2015 to 2015
$412k
NCI NIH HHS R01 CA176748NIAMS NIH HHS R01 AR059130NIH HHS S10 OD020029
6 · The paper itself

Abstract

The critical tumor suppressor PTEN is regulated by numerous post-translational modifications including phosphorylation, acetylation and ubiquitination. Ubiquitination of PTEN was reported to control both PTEN stability and nuclear localization. Notably, the HECT E3-ligase NEDD4-1 was identified as the ubiquitin ligase for PTEN, mediating its degradation and down-stream events. However, the mechanisms how NEDD4-1 is regulated by up-stream signaling pathways or interaction with other proteins in promoting PTEN degradation remain largely unclear. In the present study, we identified that the adaptor protein Numb, which is demonstrated to be a novel binding partner of NEDD4-1, plays important roles in controlling PTEN ubiquitination through regulating NEDD4-1 activity and the association between PTEN and NEDD4-1. Furthermore, we provided data to show that Numb regulates cell proliferation and glucose metabolism in a PTEN-dependent manner. Overall, our study revealed a novel regulation of the well-documented NEDD4-1/PTEN pathway and its oncogenic behavior.

Indexed as

ProteolysisHumansMCF-7 CellsMembrane ProteinsNedd4 Ubiquitin Protein LigasesNerve Tissue ProteinsProtein BindingProtein StabilityPTEN PhosphohydrolaseSignal TransductionUbiquitinationUbiquitin-Protein LigasesMembrane ProteinsNedd4 protein, humanNedd4 Ubiquitin Protein LigasesNerve Tissue ProteinsNUMB protein, humanPTEN PhosphohydrolaseUbiquitin-Protein LigasesCell growthGlucose metabolismProtein degradationUbiquitination

Identifiers

PMID28437168
PMCPMC5462079
OpenAlexW2608594137

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.