Evidence map›Paper›PMID 19740742›Full record

ArticleThe Journal of biological chemistry2009

Analysis of PTEN complex assembly and identification of heterogeneous nuclear ribonucleoprotein C as a component of the PTEN-associated complex.

Sherly Mosessian, Nuraly K Avliyakulov, David J Mulholland, Pinmanee Boontheung, Joseph A Loo, Hong Wu

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. 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
0.7field-weighted citation impact, top 30% 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, 19 citations in OpenAlex.

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  15. PTEN-Associated Complexes: An Overview.Current topics in biochemical research · 2010
    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

6 authors at 2 institutions in 1 country.

Sherly MosessianDepartment of Molecular and Medical Pharmacology, Institute for Molecular Medicine, University of California, Los Angeles, California 90095, USA.
Nuraly K Avliyakulov
David J Mulholland
Pinmanee Boontheung
Joseph A Loo
Hong Wu
University of California, Los Angeles · USInstitute for Molecular Medicine · US

Funding

UCLA SPORE IN PROSTATE CANCERP50CA092131 · NCI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI FREEMAN, MICHAEL R · 2002 to 2023
$42.6M
MOUSE MODELS FOR PROSTATE CANCERU01CA084128 · NCI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI SAWYERS, CHARLES L. · 1999 to 2008
$8.0M
PTEN and Prostate Cancer ProgressionR01CA107166 · NCI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WU, HONG · 2004 to 2008
$1.7M
Deciphering Beta-Catenin Contributions in Prostate CanceF32CA112988 · NCI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI MULHOLLAND, DAVID · 2005 to 2008
$138k
NCI NIH HHS F32CA112988-01NCI NIH HHS P50 CA092131NCI NIH HHS PC031130NCI NIH HHS R01 CA107166NCI NIH HHS U01 CA084128NCI NIH HHS U01 CA84128-06
6 · The paper itself

Abstract

PTEN (phosphatase and tensin homolog deleted on chromosome 10) is well characterized for its role in antagonizing the phosphoinositide 3-kinase pathway. Previous studies using size-exclusion chromatography demonstrated PTEN recruitment into high molecular mass complexes and hypothesized that PTEN phosphorylation status and PDZ binding domain may be required for such complex formation. In this study, we set out to test the structural requirements for PTEN complex assembly and identify the component(s) of the PTEN complex(es). Our results demonstrated that the PTEN catalytic function and PDZ binding domain are not absolutely required for its complex formation. On the other hand, PTEN phosphorylation status has a significant impact on its complex assembly. Our results further demonstrate enrichment of the PTEN complex in nuclear lysates, suggesting a mechanism through which PTEN phosphorylation may regulate its complex assembly. These results prompted further characterization of other protein components within the PTEN complex(es). Using size-exclusion chromatography and two-dimensional difference gel electrophoresis followed by mass spectrometry analysis, we identified heterogeneous nuclear ribonucleoprotein C (hnRNP C) as a novel protein recruited to higher molecular mass fractions in the presence of PTEN. Further analysis indicates that endogenous hnRNP C and PTEN interact and co-localize within the nucleus, suggesting a potential role for PTEN, alongside hnRNP C, in RNA regulation.

Indexed as

Active Transport, Cell NucleusCell Line, TumorChromatography, GelElectrophoresis, Gel, Two-DimensionalHeterogeneous-Nuclear Ribonucleoprotein Group CHumansMaleMass SpectrometryMultiprotein ComplexesNuclear ProteinsPhosphorylationPTEN PhosphohydrolaseHeterogeneous-Nuclear Ribonucleoprotein Group CMultiprotein ComplexesNuclear ProteinsPTEN PhosphohydrolasePTEN protein, human

Identifiers

PMID19740742
PMCPMC2781571
OpenAlexW2090574097

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.