Evidence map›Paper›PMID 22393046›Full record

ArticleThe Journal of biological chemistry2012

RhoGDI SUMOylation at Lys-138 increases its binding activity to Rho GTPase and its inhibiting cancer cell motility.

Jianxiu Yu, Dongyun Zhang, Jinyi Liu, Jingxia Li, Yonghui Yu, Xue-Ru Wu, Chuanshu Huang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
4.0field-weighted citation impact, top 5% 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

51 citing papers in PubMed, 68 citations in OpenAlex.

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  10. Electrostatic Forces Mediate the Specificity of RHO GTPase-GDI Interactions.International journal of molecular sciences · 2021
    Article
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  20. [Human RhoA is modified by SUMO2/3].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2018
    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

7 authors at 1 institution in 1 country.

Jianxiu YuNelson Institute of Environmental Medicine, New York University School of Medicine, Tuxedo, New York 10987, USA.
Dongyun Zhang
Jinyi Liu
Jingxia Li
Yonghui Yu
Xue-Ru Wu
Chuanshu Huang
New York University · US

Funding

RESEARCH IN ENVIRONMENTAL HEALTH SCIENCES (CENTER GRANT)P30ES000260 · NIEHS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI COSTA, MAX · 1985 to 2020
$26.1M
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
NCI NIH HHS CA112557NCI NIH HHS R01 CA112557NIEHS NIH HHS ES000260NIEHS NIH HHS ES010344NIEHS NIH HHS P30 ES000260NIEHS NIH HHS P42 ES010344
6 · The paper itself

Abstract

The Rho GDP dissociation inhibitor (RhoGDI) can bind to small GTPases and keep them in a biologically inactive state in cytoplasm, through which it affects actin polymerization and cell motility. However, mechanisms underlying how RhoGDI regulates Rho GTPase complex formation/membrane extraction/GTPase dissociation remain largely unexplored. Our previous studies reported that X-linked inhibitor of apoptosis protein (XIAP) interacted with RhoGDI via its RING domain and negatively modulated RhoGDI SUMOylation and HCT116 cancer cell migration. Here, we identified that RhoGDI SUMOylation specifically occurred at Lys-138, which was inhibited by XIAP domain. We further demonstrated that RhoGDI SUMOylation at Lys-138 was crucial for inhibiting actin polymerization and cytoskeleton formation as well as cancer cell motility. Moreover, SUMO-RhoGDI had a much higher binding affinity to small Rho GTPase compared with the un-SUMOylated form of RhoGDI. Taken together, our study demonstrated a novel modification of RhoGDI, SUMOylation at Lys-138, which played a key role in regulating Rho GTPase activation in cancer cells. The physiological regulation of RhoGDI SUMOylation by the RING domain of XIAP may account for modulation of cancer cell invasion and metastasis by XIAP.

Indexed as

Gene Expression Regulation, NeoplasticCell Line, TumorCell MovementGuanine Nucleotide Dissociation InhibitorsHumansLysineModels, BiologicalNeoplasm InvasivenessNeoplasm MetastasisNeoplasmsrho GTP-Binding Proteinsrho Guanine Nucleotide Dissociation Inhibitor alpharho-Specific Guanine Nucleotide Dissociation InhibitorsSumoylationWound HealingX-Linked Inhibitor of Apoptosis ProteinARHGDIA protein, humanGuanine Nucleotide Dissociation InhibitorsLysinerho GTP-Binding Proteinsrho Guanine Nucleotide Dissociation Inhibitor alpharho-Specific Guanine Nucleotide Dissociation InhibitorsX-Linked Inhibitor of Apoptosis Protein

Identifiers

PMID22393046
PMCPMC3340185
OpenAlexW2000129411

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.