Evidence map›Paper›PMID 23720779›Full record

ArticleThe Journal of biological chemistry2013

X-linked inhibitor of apoptosis protein (XIAP) regulation of cyclin D1 protein expression and cancer cell anchorage-independent growth via its E3 ligase-mediated protein phosphatase 2A/c-Jun axis.

Zipeng Cao, Ruowen Zhang, Jingxia Li, Haishan Huang, Dongyun Zhang, Jingjie Zhang, Jimin Gao, Jingyuan Chen, Chuanshu Huang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. 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
1.9field-weighted citation impact, top 14% 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, 41 citations in OpenAlex.

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  3. The cross talk of ubiquitination and chemotherapy tolerance in colorectal cancer.Journal of cancer research and clinical oncology · 2024
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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

9 authors at 3 institutions in 2 countries.

Zipeng CaoNelson Institute of Environmental Medicine, New York University School of Medicine, Tuxedo, New York 10987, USA.
Ruowen Zhang
Jingxia Li
Haishan Huang
Dongyun Zhang
Jingjie Zhang
Jimin Gao
Jingyuan Chen
Chuanshu Huang
New York University · USAir Force Medical University · CNWenzhou Medical University · CN

Funding

Vaccine FacilityP30CA016087 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI ADRIANA HEGUY · 1985 to 2026
$83.1M
RESEARCH IN ENVIRONMENTAL HEALTH SCIENCES (CENTER GRANT)P30ES000260 · NIEHS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI COSTA, MAX · 1985 to 2020
$26.1M
Reagent/Service CoreP01CA165980 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI WU, XUE-RU · 2013 to 2023
$13.5M
Molecular Mechanisms of Nickel-Induced TumorigenicityR01CA112557 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI HUANG, CHUANSHU · 2004 to 2016
$2.9M
Mechanisms underlying therapeutic effect of a new compound Isorhapontigenin (ISO)R01CA177665 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI HUANG, CHUANSHU · 2013 to 2018
$1.7M
NCI NIH HHS CA112557NCI NIH HHS P01 CA165980NCI NIH HHS P30 CA016087NCI NIH HHS R01 CA112557NCI NIH HHS R01 CA177665NIEHS NIH HHS ES000260NIEHS NIH HHS P30 ES000260
6 · The paper itself

Abstract

The X-linked inhibitor of apoptosis protein (XIAP) is a well known potent inhibitor of apoptosis; however, it is also involved in other cancer cell biological behavior. In the current study, we discovered that XIAP and its E3 ligase played a crucial role in regulation of cyclin D1 expression in cancer cells. We found that deficiency of XIAP expression resulted in a marked reduction in cyclin D1 expression. Consistently, cell cycle transition and anchorage-independent cell growth were also attenuated in XIAP-deficient cancer cells compared with those of the parental wild-type cells. Subsequent studies demonstrated that E3 ligase activity within the RING domain of XIAP is crucial for its ability to regulate cyclin D1 transcription, cell cycle transition, and anchorage-independent cell growth by up-regulating transactivation of c-Jun/AP-1. Moreover, we found that E3 ligase within RING domain was required for XIAP inhibition of phosphatase PP2A activity by up-regulation of PP2A phosphorylation at Tyr-307 in its catalytic subunit. Such PP2A phosphorylation and inactivation resulted in phosphorylation and activation of its downstream target c-Jun in turn leading to cyclin D1 expression. Collectively, our studies uncovered a novel function of E3 ligase activity of XIAP in the up-regulation of cyclin D1 expression, providing significant insight into the understanding of the biomedical significance of overexpressed XIAP in cancer development, further offering a new molecular basis for utilizing XIAP E3 ligase as a cancer therapeutic target.

Indexed as

Cell ProliferationBinding SitesBlotting, WesternCell AdhesionColonic NeoplasmsCyclin D1G1 PhaseGene Expression Regulation, NeoplasticHCT116 CellsHumansMutationPhosphorylationProtein Phosphatase 2Proto-Oncogene Proteins c-junReverse Transcriptase Polymerase Chain ReactionRNA InterferenceCyclin D1PPP2CA protein, humanProtein Phosphatase 2Proto-Oncogene Proteins c-junTranscription Factor AP-1TyrosineUbiquitin-Protein LigasesXIAP protein, humanX-Linked Inhibitor of Apoptosis ProteinAP-1 Transcription FactorCyclin D1E3 Ubiquitin LigasePP2AXIAP

Identifiers

PMID23720779
PMCPMC3711291
OpenAlexW2079838606

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.