Evidence map›Paper›PMID 21555589›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Bidirectional autoregulatory mechanism of metastasis-associated protein 1-alternative reading frame pathway in oncogenesis.

Da-Qiang Li, Suresh B Pakala, Sirigiri Divijendra Natha Reddy, Kazufumi Ohshiro, Jun-Xiang Zhang, Lei Wang, Yanping Zhang, Ignacio Moreno de Alborán, M Radhakrishna Pillai, Jeyanthy Eswaran and 1 more

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 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 18% 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, 29 citations in OpenAlex.

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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

11 authors at 6 institutions in 3 countries.

Da-Qiang LiDepartment of Biochemistry and Molecular Biology, The George Washington University Medical Center, Washington, DC 20037, USA.
Suresh B Pakala
Sirigiri Divijendra Natha Reddy
Kazufumi Ohshiro
Jun-Xiang Zhang
Lei Wang
Yanping Zhang
Ignacio Moreno de Alborán
M Radhakrishna Pillai
Jeyanthy Eswaran
Rakesh Kumar
George Washington University · USBaylor College of Medicine · USCentro Nacional de Biotecnología · ESMcCormick (United States) · USRajiv Gandhi Centre for Biotechnology · INUniversity of North Carolina at Chapel Hill · US

Funding

Regulation of MDM2 by the ribosomal protein L11R01CA100302 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ZHANG, YANPING · 2003 to 2013
$3.2M
Role of Metastatic Tumor Antigen-1 in Mammary GlandR01CA098823 · NCI · UNIVERSITY OF TX MD ANDERSON CAN CTR · PI KUMAR, RAKESH · 2003 to 2013
$3.1M
In vivo function of Mdm2 E3 ubiquitin ligaseR01CA127770 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ZHANG, YANPING · 2008 to 2013
$1.5M
NCI NIH HHS CA98823NCI NIH HHS CA98823S1NCI NIH HHS R01 CA098823NCI NIH HHS R01 CA100302NCI NIH HHS R01 CA127770
6 · The paper itself

Abstract

Although metastasis-associated protein 1 (MTA1), a component of the nucleosome remodeling and histone deacetylation complex, is widely up-regulated in human cancers and correlates with tumor metastasis, its regulatory mechanism and related signaling pathways remain unknown. Here, we report a previously unrecognized bidirectional autoregulatory loop between MTA1 and tumor suppressor alternative reading frame (ARF). MTA1 transactivates ARF transcription by recruiting the transcription factor c-Jun onto the ARF promoter in a p53-independent manner. ARF, in turn, negatively regulates MTA1 expression independently of p53 and c-Myc. In this context, ARF interacts with transcription factor specificity protein 1 (SP1) and promotes its proteasomal degradation by enhancing its interaction with proteasome subunit regulatory particle ATPase 6, thereby abrogating the ability of SP1 to stimulate MTA1 transcription. ARF also physically associates with MTA1 and affects its protein stability. Thus, MTA1-mediated activation of ARF and ARF-mediated functional inhibition of MTA1 represent a p53-independent bidirectional autoregulatory mechanism in which these two opposites act in concert to regulate cell homeostasis and oncogenesis, depending on the cellular context and the environment.

Indexed as

Cell LineCyclin-Dependent Kinase Inhibitor p16Gene Expression RegulationHistone DeacetylasesHomeostasisHumansNeoplasmsReading FramesRepressor ProteinsTrans-ActivatorsTranscriptional ActivationTumor Suppressor Protein p53Cdkn2a protein, mouseCyclin-Dependent Kinase Inhibitor p16Histone DeacetylasesMTA1 protein, humanRepressor ProteinsTrans-ActivatorsTumor Suppressor Protein p53

Identifiers

PMID21555589
PMCPMC3102345
OpenAlexW2004526623

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.