Evidence map›Paper›PMID 21454687›Full record

ArticleThe Journal of biological chemistry2011

Protein interactions of phosphatase and tensin homologue (PTEN) and its cancer-associated G20E mutant compared by using stable isotope labeling by amino acids in cell culture-based parallel affinity purification.

Jayantha Gunaratne, Mei Xian Goh, Hannah Lee Foon Swa, Fen Yee Lee, Emma Sanford, Loke Meng Wong, Kelly A Hogue, Walter P Blackstock, Koichi Okumura

Open access · hybridAbstract readComparative Study
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

15 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Regulation and modulation of PTEN activity.Molecular biology reports · 2018
    Review
  3. Article
  4. Article
  5. Review
  6. IQGAP1 is a phosphoinositide effector and kinase scaffold.Advances in biological regulation · 2016
    Review
  7. Review
  8. Review
  9. PTEN function: the long and the short of it.Trends in biochemical sciences · 2014
    Review
  10. A mass spectrometry view of stable and transient protein interactions.Advances in experimental medicine and biology · 2014
    Review
  11. Article
  12. Review
  13. Article
  14. The functions and regulation of the PTEN tumour suppressor.Nature reviews. Molecular cell biology · 2012
    Review
  15. Review
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 4 institutions in 1 country.

Jayantha GunaratneCancer Science Institute of Singapore, National University of Singapore, 28 Medical Drive, 117456 Singapore.
Mei Xian Goh
Hannah Lee Foon Swa
Fen Yee Lee
Emma Sanford
Loke Meng Wong
Kelly A Hogue
Walter P Blackstock
Koichi Okumura
Institute of Molecular and Cell Biology · SGNational University Cancer Institute, Singapore · SGNational University of Singapore · SGAgency for Science, Technology and Research · SG

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The tumor suppressor PTEN (phosphatase and tensin homologue) negatively regulates the PI3K pathway through its lipid phosphatase activity and is one of the most commonly lost tumor suppressors in human cancers. Though the tumor suppressive function involves the lipid phosphatase-dependent and -independent activities of PTEN, the mechanism leading to the phosphatase-independent function of PTEN is understood poorly. Some PTEN mutants have lipid phosphatase activity but fail to suppress cell growth. Here, we use a cancer-associated mutant, G20E, to gain insight into the phosphatase-independent function of PTEN by investigating protein-protein interactions using MS-based stable isotope labeling by amino acids in cell culture (SILAC). A strategy named parallel affinity purification (PAP) and SILAC has been developed to prioritize interactors and to compare the interactions between wild-type and G20E PTEN. Clustering of the prioritized interactors acquired by the PAP-SILAC approach shows three distinct clusters: 1) wild-type-specific interactors, 2) interactors unique to the G20E mutant, and 3) proteins common to wild-type and mutant. These interactors are involved mainly in cell migration and apoptosis pathways. We further demonstrate that the wild-type-specific interactor, NUDTL16L1, is required for the regulatory function of wild-type PTEN in cell migration. These findings contribute to a better understanding of the mechanisms of the phosphatase-dependent and -independent functions of PTEN.

Indexed as

Mutation, MissenseAmino AcidsCell Line, TumorHumansIsotope LabelingNeoplasm ProteinsNeoplasmsPTEN PhosphohydrolaseAmino AcidsNeoplasm ProteinsPTEN PhosphohydrolasePTEN protein, human

Identifiers

PMID21454687
PMCPMC3093882
OpenAlexW2134005025

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.