Evidence map›Paper›PMID 24141722›Full record

ArticleCell death and differentiation2014

p34 is a novel regulator of the oncogenic behavior of NEDD4-1 and PTEN.

S-W Hong, J-H Moon, J-S Kim, J-S Shin, K-A Jung, W-K Lee, S-Y Jeong, J J Hwang, S-J Lee, Y-A Suh and 12 more

Open access · bronzeAbstract read
In one paragraph

Article in Cell death and differentiation, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

28 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
  2. Article
  3. The HECT family of E3 ubiquitin ligases and PTEN.Seminars in cancer biology · 2022
    Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  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

22 authors at 5 institutions in 1 country.

S-W Hong1] Innovative Cancer Research, Asan Medical Center, Asan Institute for Life Science, University of Ulsan College of Medicine, Seoul, Republic of Korea [2] Department of Oncology, Asan Medical Center, University of Ulsan College of Medicine, Seoul, Republic of Korea.
J-H Moon
J-S Kim
J-S Shin
K-A Jung
W-K Lee
S-Y Jeong
J J Hwang
S-J Lee
Y-A Suh
I Kim
K-Y Nam
S Han
J E Kim
K-P Kim
Y S Hong
J-L Lee
W-J Lee
E K Choi
J S Lee
D-H Jin
T W Kim
University of Ulsan · KRAsan Medical Center · KRUlsan College · KRMyongji University · KRGachon University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

PTEN is one of the most frequently mutated or deleted tumor suppressors in human cancers. NEDD4-1 was recently identified as the E3 ubiquitin ligase for PTEN; however, a number of important questions remain regarding the role of ubiquitination in regulating PTEN function and the mechanisms by which PTEN ubiquitination is regulated. In the present study, we demonstrated that p34, which was identified as a binding partner of NEDD4-1, controls PTEN ubiquitination by regulating NEDD4-1 protein stability. p34 interacts with the WW1 domain of NEDD4-1, an interaction that enhances NEDD4-1 stability. Expression of p34 promotes PTEN poly-ubiquitination, leading to PTEN protein degradation, whereas p34 knockdown results in PTEN mono-ubiquitination. Notably, an inverse correlation between PTEN and p34/NEDD4-1 levels was confirmed in tumor samples from colon cancer patients. Thus, p34 acts as a key regulator of the oncogenic behavior of NEDD4-1 and PTEN.

Indexed as

Cell Line, TumorCell ProliferationEndosomal Sorting Complexes Required for TransportHEK293 CellsHumansMCF-7 CellsNedd4 Ubiquitin Protein LigasesNuclear ProteinsProtein StabilityProtein Structure, TertiaryPTEN PhosphohydrolaseRNA InterferenceRNA, Small InterferingTrans-ActivatorsTranscription FactorsUbiquitinationEndosomal Sorting Complexes Required for TransportNedd4 protein, humanNedd4 Ubiquitin Protein LigasesNuclear ProteinsPTEN PhosphohydrolaseRNA, Small InterferingSERTAD1 protein, humanTrans-ActivatorsTranscription FactorsUbiquitin-Protein Ligases

Identifiers

PMID24141722
PMCPMC3857621
OpenAlexW2093806359

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.