Evidence map›Paper›PMID 24814346›Full record

ArticleNature structural & molecular biology2014

PTEN is a protein tyrosine phosphatase for IRS1.

Yuji Shi, Junru Wang, Sarat Chandarlapaty, Justin Cross, Craig Thompson, Neal Rosen, Xuejun Jiang

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

70 citing papers in PubMed, 125 citations in OpenAlex.

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  16. Article
  17. The HECT family of E3 ubiquitin ligases and PTEN.Seminars in cancer biology · 2022
    Review
  18. Review
  19. Article
  20. Review

10 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

7 authors at 1 institution in 1 country.

Yuji ShiCell Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York, USA.
Junru WangCell Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York, USA.
Sarat ChandarlapatyHuman Oncology and Pathogenesis Program, Memorial Sloan-Kettering Cancer Center, New York, New York, USA.
Justin CrossCancer Biology and Genetics Program, Memorial Sloan-Kettering Cancer Center, New York, New York, USA.
Craig ThompsonCancer Biology and Genetics Program, Memorial Sloan-Kettering Cancer Center, New York, New York, USA.
Neal RosenMolecular Pharmacology and Chemistry Program, Memorial Sloan-Kettering Cancer Center, New York, New York, USA.
Xuejun JiangCell Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York, USA.
Memorial Sloan Kettering Cancer Center · US

Funding

X-RAY CRYSTALLOGRAPHYP30CA008748 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI Hongbiao Carl Lekaye · 1985 to 2026
$347.4M
SPORE In Prostate CancerP50CA092629 · NCI · SLOAN-KETTERING INSTITUTE FOR CANCER RES · PI JAMES A EASTHAM · 2001 to 2026
$63.0M
Mechanisms and Function of Autophagy in CancerR01CA166413 · NCI · SLOAN-KETTERING INST CAN RESEARCH · PI JIANG, XUEJUN · 2013 to 2023
$3.9M
NCI NIH HHS P30 CA008748NCI NIH HHS P50 CA092629NCI NIH HHS R01 CA166413
6 · The paper itself

Abstract

The biological function of the PTEN tumor suppressor is mainly attributed to its lipid phosphatase activity. This study demonstrates that mammalian PTEN is a protein tyrosine phosphatase that selectively dephosphorylates insulin receptor substrate-1 (IRS1), a mediator of insulin and IGF signals. IGF signaling was defective in cells lacking NEDD4, a PTEN ubiquitin ligase, whereas AKT activation triggered by EGF or serum was unimpaired. Defective IGF signaling caused by NEDD4 deletion, including phosphorylation of IRS1 and AKT, was rescued by PTEN ablation. We demonstrate the nature of PTEN as an IRS1 phosphatase by direct biochemical analysis and cellular reconstitution, showing that NEDD4 supports insulin-mediated glucose metabolism and is required for the proliferation of IGF1 receptor-dependent but not EGF receptor-dependent tumor cells. Thus, PTEN is a protein phosphatase for IRS1, and its antagonism by NEDD4 promotes signaling by IGF and insulin.

Indexed as

AnimalsCells, CulturedEndosomal Sorting Complexes Required for TransportGene DeletionGene Knockdown TechniquesInsulinInsulin Receptor Substrate ProteinsMiceNedd4 Ubiquitin Protein LigasesPhosphorylationPTEN PhosphohydrolaseSignal TransductionSomatomedinsUbiquitin-Protein LigasesEndosomal Sorting Complexes Required for TransportInsulinInsulin Receptor Substrate ProteinsIrs1 protein, mouseNedd4l protein, mouseNedd4 Ubiquitin Protein LigasesPTEN PhosphohydrolasePten protein, mouseSomatomedinsUbiquitin-Protein Ligases

Identifiers

PMID24814346
PMCPMC4167033
OpenAlexW2092767792

What OpenQuestion holds

Textmetadata
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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.