Evidence map›Paper›PMID 22532870›Full record

ArticlePloS one2012

E3 ligase activity of XIAP RING domain is required for XIAP-mediated cancer cell migration, but not for its RhoGDI binding activity.

Jinyi Liu, Dongyun Zhang, Wenjing Luo, Jianxiu Yu, Jingxia Li, Yonghui Yu, Xinhai Zhang, Jingyuan Chen, Xue-Ru Wu, Chuanshu Huang

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

29 citing papers in PubMed, 40 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

10 authors at 2 institutions in 2 countries.

Jinyi LiuNelson Institute of Environmental Medicine, New York University School of Medicine, Tuxedo, New York, United States of America.
Dongyun Zhang
Wenjing Luo
Jianxiu Yu
Jingxia Li
Yonghui Yu
Xinhai Zhang
Jingyuan Chen
Xue-Ru Wu
Chuanshu Huang
New York University · USAir Force Medical University · CN

Funding

Water/sediment &model &criteria for arsenic &chromeP42ES010344 · NIEHS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI COSTA, MAX · 2000 to 2010
$15.0M
Molecular Mechanisms of Nickel-Induced TumorigenicityR01CA112557 · NCI · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI HUANG, CHUANSHU · 2004 to 2016
$2.9M
Mechanisms of As-Induced CarcinogenesisR01CA119028 · NCI · UNIVERSITY OF KENTUCKY · PI SHI, XIANGLIN · 2006 to 2010
$1.8M
Mechanisms of Tumor Promotion Effects of B[a]PDER01ES012451 · NIEHS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI HUANG, CHUANSHU · 2004 to 2008
$1.7M
NCI NIH HHS CA112557NCI NIH HHS CA119028-05S110NCI NIH HHS R01 CA112557NCI NIH HHS R01 CA119028NIEHS NIH HHS ES010344NIEHS NIH HHS ES012451NIEHS NIH HHS P42 ES010344NIEHS NIH HHS R01 ES012451
6 · The paper itself

Abstract

Although an increased expression level of XIAP is associated with cancer cell metastasis, the underlying molecular mechanisms remain largely unexplored. To verify the specific structural basis of XIAP for regulation of cancer cell migration, we introduced different XIAP domains into XIAP(-/-) HCT116 cells, and found that reconstitutive expression of full length HA-XIAP and HA-XIAP ΔBIR, both of which have intact RING domain, restored β-Actin expression, actin polymerization and cancer cell motility. Whereas introduction of HA-XIAP ΔRING or H467A mutant, which abolished its E3 ligase function, did not show obvious restoration, demonstrating that E3 ligase activity of XIAP RING domain played a crucial role of XIAP in regulation of cancer cell motility. Moreover, RING domain rather than BIR domain was required for interaction with RhoGDI independent on its E3 ligase activity. To sum up, our present studies found that role of XIAP in regulating cellular motility was uncoupled from its caspase-inhibitory properties, but related to physical interaction between RhoGDI and its RING domain. Although E3 ligase activity of RING domain contributed to cell migration, it was not involved in RhoGDI binding nor its ubiquitinational modification.

Indexed as

ApoptosisCaspasesCell Line, TumorCell MovementCell ProliferationGuanine Nucleotide Dissociation InhibitorsHumansNeoplasmsProtein Structure, Tertiaryrho Guanine Nucleotide Dissociation Inhibitor alpharho-Specific Guanine Nucleotide Dissociation InhibitorsTumor Cells, CulturedUbiquitin-Protein LigasesX-Linked Inhibitor of Apoptosis ProteinARHGDIA protein, humanCaspasesGuanine Nucleotide Dissociation Inhibitorsrho Guanine Nucleotide Dissociation Inhibitor alpharho-Specific Guanine Nucleotide Dissociation InhibitorsUbiquitin-Protein LigasesXIAP protein, humanX-Linked Inhibitor of Apoptosis Protein

Identifiers

PMID22532870
PMCPMC3330820
OpenAlexW1996321741

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.